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Amino acid synthesis
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For the non-biological synthesis of amino acids, see Strecker amino acid synthesis.
Amino acid biosynthesis overview. The drawn molecules are in their neutral forms and do not fully correspond to their presented names. Humans can not synthesize all of these amino acids.
Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. Humans are an excellent example of this, since humans can only synthesize 11 of the 20 standard amino acids (a.k.a. non-essential amino acid), and in time of accelerated growth, histidine, can be considered an essential amino acid.[1]
A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.
In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.
Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
Contents
[hide]
1 Nitrogen fixation
2 Transamination
3 From intermediates of the citric acid cycle and other pathways
4 Regulation by feedback inhibition
4.1 α-Ketoglutarates
4.2 Erythrose 4-phosphate and phosphoenolpyruvate
4.3 Oxaloacetate/aspartate
4.3.1 Aspartate
4.3.2 Lysine
4.3.3 Asparagine
4.3.4 Methionine
4.3.5 Threonine
4.3.6 Isoleucine
4.4 Ribose 5-phosphates
4.5 3-Phosphoglycerates
4.5.1 Serine
4.5.2 Glycine
4.5.3 Cysteine
4.6 Pyruvates
4.6.1 Alanine
4.6.2 Valine
4.6.3 Leucine
4.6.4 ilvEDA operon
5 Amino acids as precursors to other biomolecules
6 References
7 External links
Nitrogen fixation[edit]
Microorganisms use ATP and reduced ferredoxin, a powerful reductant, to reduce atmospheric nitrogen (N2) to ammonia (NH3). An iron-molybdenum cluster in nitrogenase deftly catalyzes the fixation of N2, a very inert molecule. Higher organisms consume the fixed nitrogen to synthesize amino acids, nucleotides, and other nitrogen-containing biomolecules. The major points of entry of ammonia into metabolism are glutamine or glutamate.
Transamination[edit]
Most amino acids are synthesized from α-ketoacids, and later transaminated from another amino acid, usually glutamate. The enzyme involved in this reaction is an aminotransferase.
α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate
Glutamate itself is formed by amination of α-ketoglutarate:
α-ketoglutarate + NH+
4 ⇄ glutamate
From intermediates of the citric acid cycle and other pathways[edit]
Of the basic set of twenty amino acids (not counting selenocysteine), there are eight that human beings cannot synthesize. In addition, the amino acids arginine, cysteine, glycine, glutamine, histidine, proline, serine, and tyrosine are considered conditionally essential, meaning they are not normally required in the diet, but must be supplied exogenously to specific populations that do not synthesize it in adequate amounts.[2][3] For example, enough arginine is synthesized by the urea cycle to meet the needs of an adult but perhaps not those of a growing child. Amino acids that must be obtained from the diet are called essential amino acids. Nonessential amino acids are produced in the body. The pathways for the synthesis of nonessential amino acids are quite simple. Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate. A transamination reaction takes place in the synthesis of most amino acids. At this step, the chirality of the amino acid is established. Alanine and aspartate are synthesized by the transamination of pyruvate and oxaloacetate, respectively. Glutamine is synthesized from NH4+ and glutamate, and asparagine is synthesized similarly. Proline and arginine are derived from glutamate. Serine, formed from 3-phosphoglycerate, is the precursor of glycine and cysteine. Tyrosine is synthesized by the hydroxylation of phenylalanine, an essential amino acid. The pathways for the biosynthesis of essential amino acids are much more complex than those for the nonessential ones. Activated Tetrahydrofolate, a carrier of one-carbon units, plays an important role in the metabolism of amino acids and nucleotides. This coenzyme carries one-carbon units at three oxidation states, which are interconvertible: most reduced—methyl; intermediate—methylene; and most oxidized—formyl, formimino, and methenyl. The major donor of activated methyl groups is S-adenosylmethionine, which is synthesized by the transfer of an adenosyl group from ATP to the sulfur atom of methionine. S-Adenosylhomocysteine is formed when the activated methyl group is transferred to an acceptor. It is hydrolyzed to adenosine and homocysteine, the latter of which is then methylated to methionine to complete the activated methyl cycle.
Cortisol inhibits protein synthesis.[4]
Regulation by feedback inhibition[edit]
Most of the pathways of amino acid biosynthesis are regulated by feedback inhibition, in which the committed step is allosterically inhibited by the final product. Branched pathways require extensive interaction among the branches that includes both negative and positive regulation. The regulation of glutamine synthetase from E. coli is a striking demonstration of cumulative feedback inhibition and of control by a cascade of reversible covalent modifications.
α-Ketoglutarates[edit]
The α-ketoglutarate family of amino acid synthesis (synthesis of glutamate, glutamine, proline and arginine) begins with α-ketoglutarate, an intermediate in the Citric Acid Cycle. The concentration of α-ketoglutarate is dependent on the activity and metabolism within the cell along with the regulation of enzymatic activity. In E. coli citrate synthase, the enzyme involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP.[5] This is one of the initial regulations of the α-ketoglutarate family of amino acid synthesis.
The regulation of the synthesis of glutamate from α-ketoglutarate is subject to regulatory control of the Citric Acid Cycle as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions.[5]
The conversion of glutamate to glutamine is regulated by glutamine synthetase (GS) and is a highly significant step in nitrogen metabolism.[5] This enzyme is regulated by at least four different mechanisms: 1. Repression and depression due to nitrogen levels; 2. Activation and inactivation due to enzymatic forms (taut and relaxed); 3. Cumulative feedback inhibition through end product metabolites; and 4. Alterations of the enzyme due to adenylation and deadenylation.[5] In rich nitrogenous media or growth conditions containing high quantities of ammonia there is a low level of GS, whereas in limiting quantities of ammonia the specific activity of the enzyme is 20-fold higher.[5] The confirmation of the enzyme plays a role in regulation depending on if GS is in the taut or relaxed form. The taut form of GS is fully active but, the removal of manganese converts the enzyme to the relaxed state. The specific conformational state occurs based on the binding of specific divalent cations and is also related to adenylation.[5] The feedback inhibition of GS is due to a cumulative feedback due to several metabolites including L-tryptophan, L-histidine, AMP, CTP, glucosamine-6-phosphate and carbamyl phosphate, alanine, and glycine.[5] An excess of any one product does not individually inhibit the enzyme but a combination or accumulation of all the end products have a strong inhibitory effect on the synthesis of glutamine.[5] Glutamine synthase activity is also inhibited via adenylation. The adenylation activity is catalyzed by the bifunctional adenylyltransferase/adenylyl removal (AT/AR) enzyme. Glutamine and a regulatory protein called PII act together to stimulate adenylation.[6]
The regulation of proline biosynthesis can be dependent on the initial controlling step through negative feedback inhibition.[7] In E. coli, proline allosterically inhibits Glutamate 5-kinase which catalyzes the reaction from L-glutamate to an unstable intermediate L-γ-Glutamyl phosphate.[7]
Arginine synthesis also utilizes negative feedback as well as repression through a repressor encoded by the gene argR. The gene product of argR, ArgR an aporepressor, and arginine as a corepressor affect the operon of arginine biosynthesis. The degree of repression is determined by the concentrations of the repressor protein and corepressor level.[8]
Erythrose 4-phosphate and phosphoenolpyruvate[edit]
Phenylalanine, tyrosine, and tryptophan are known as the aromatic amino acids. The synthesis of all three share a common beginning to their pathways; the formation of chorismate from phosphoenolpyruvate (PEP) and erythrose 4- phosphate (E4P). The first step, condensation of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) from PEP/E4P, uses three isoenzymes AroF, AroG, and AroH. Each one of these has its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively. These isoenzymes all have the ability to help regulate synthesis of DAHP by the method of feedback inhibition. This acts in the cell by monitoring the concentrations of each of the three aromatic amino acids. When there is too much of any one of them, that one will allosterically control the DAHP synthetase by “turning it off”. With the first step of the common pathway shut off, synthesis of the three amino acids can not proceed. The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, except for shikimate kinase which can be inhibited by shikimate through linear mixed-type inhibition. If too much shikimate has been produced then it can bind to shikimate kinase to stop further production.
Besides the regulations described above, each amino acids terminal pathway can be regulated. These terminal pathways progress from chorismate to the final end product, either tyrosine, phenylalanine, or tryptophan. Each one of these pathways is regulated in a similar fashion to the common pathway; with feedback inhibition on the first committed step of the pathway.
Tyrosine and phenylalanine share the same initial step in their terminal pathways, chorismate converted to prephenate which is converted to an amino acid-specific intermediate. This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. The reason for the amino acid-specific enzymes is because PheA uses a simple dehydrogenase to convert prephenate to phenylpyruvate, while TyrA uses a NAD-dependent dehydrogenase to make 4-hydroxylphenylpyruvate. Both PheA and TyrA are feedback inhibited by their respective amino acids. Tyrosine can also be inhibited at the transcriptional level by the TyrR repressor. TyrR binds to the TyrR boxes on the operon near the promoter of the gene that it wants to repress.
In the terminal-tryptophan synthesis pathway, the initial step converts chorismate to anthranilate using anthranilate synthase. This enzyme requires either ammonia or glutamine as the amino group donor. Anthranilate synthase is regulated by the gene products of trpE and trpG. trpE encodes the first subunit, which binds to chorismate and moves the amino group from the donor to chorismate. trpG encodes the second subunit, which binds glutamine and uses it as the amino group donor so that the amine group can transfer to the chorismate. Anthranilate synthase is also regulated by feedback inhibition. The finished product of tryptophan, once produced in great enough quantities, is able to act as the co-repressor to the TrpR repressor which represses expression of the trp operon.
Oxaloacetate/aspartate[edit]
The oxaloacetate/aspartate family of amino acids is composed of lysine, asparagine, methionine, threonine, and isoleucine. Aspartate can be converted into lysine, asparagine, methionine and threonine. Threonine also gives rise to isoleucine. All of these amino acids contain different mechanisms for their regulation, some being more complex than others. All the enzymes in this biosynthetic pathway are subject to regulation via feedback inhibition and/or repression at the genetic level. As is typical in highly branched metabolic pathways, there is additional regulation at each branch point of the pathway. This type of regulatory scheme allows control over the total flux of the aspartate pathway in addition to the total flux of individual amino acids. The aspartate pathway uses L-aspartic acid as the precursor for the biosynthesis of one fourth of the building block amino acids. Without this pathway, protein synthesis would not be possible.
Aspartate[edit]
The enzyme aspartokinase, which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, can be broken up into 3 isozymes, AK-I, II and III. AK-I is feed-back inhibited by threonine, while AK-II and III are inhibited by lysine. As a sidenote, AK-III catalyzes the phosphorylation of aspartic acid that is the commitment step in this biosynthetic pathway. The higher the concentration of threonine or lysine, the more aspartate kinase becomes downregulated.
Lysine[edit]
Lysine is synthesized from aspartate via the diaminopimelate (DAP) pathway. The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase and play a key role in the biosynthesis of lysine, threonine and methionine. There are two bifunctional aspartokinase/homoserine dehydrogenases, ThrA and MetL, in addition to a monofunctional aspartokinase, LysC. Transcription of aspartokinase genes is regulated by concentrations of the subsequently produced amino acids, lysine, threonine and methionine. The higher these amino acids concentrations, the less the gene is transcribed. ThrA and LysC are also feed-back inhibited by threonine and lysine. Finally, DAP decarboxylase LysA mediates the last step of the lysine synthesis and is common for all studied bacterial species. The formation of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is also inhibited by both lysine and threonine, which prevents the formation of the amino acids derived from aspartate. Additionally, high lysine concentrations inhibit the activity of dihydrodipicolinate synthase (DHPS). So, in addition to inhibiting the first enzyme of the aspartate families biosynthetic pathway, lysine also inhibits the activity of the first enzyme after the branch point, i.e. the enzyme that is specific for lysine’s own synthesis.
Asparagine[edit]
There are two different asparagine synthetases found in bacterial species. These two synthetases, which are both referred to as the AsnC protein, are coded for by two genes: AsnA and AsnB. AsnC is autogenously regulated, which is where the product of a structural gene regulates the expression of the operon in which the genes reside. The stimulating effect of AsnC on AsnA transcription is downregulated by asparagine. However, the autoregulation of AsnC is not affected by asparagine.
Methionine[edit]
Methionine synthesis is under tight regulation. The repressor protein MetJ, in cooperation with the corepressor protein S-adenosyl-methionine, mediates the repression of methionine’s biosynthetic pathway. Recently, a new regulator focus, MetR has been identified. The MetR protein is required for MetE and MetH gene expression and functions as a transactivator of transcription for these genes. MetR transcriptional activity is regulated by homocystein, which is the metabolic precursor of methionine. It is also known that vitamin B12 can repress MetE gene expression, which is mediated by the MetH holoenzyme.
Threonine[edit]
The biosynthesis of threonine is regulated via allosteric regulation of its precursor, homoserine, by structurally altering the enzyme homoserine dehydrogenase. This reaction occurs at a key branch point in the pathway, with the substrate homoserine serving as the precursor for the biosynthesis of lysine, methionine, threonin and isoleucine. High levels of threonine result in low levels of homoserine synthesis. The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate families biosynthetic pathway, threonine also inhibits the activity of the first enzyme after the branch point, i.e. the enzyme that is specific for threonine’s own synthesis.
Isoleucine[edit]
The enzymes threonine deaminase, dihydroxy acid dehydrase and transaminase are controlled by end-product regulation. I.e. the presence of isoleucine will downregulate the formation of all three enzymes, resulting in the downregulation of threonine biosynthesis. High concentrations of isoleucine also result in the downregulation of aspartate’s conversion into the aspartyl-phosphate intermediate, hence halting further biosynthesis of lysine, methionine, threonine, and isoleucine.
Ribose 5-phosphates[edit]
The synthesis of histidine in E. coli is a complex pathway involving 10 reactions and 10 enzymes. Synthesis begins with 5-phosphoribosyl-pyrophosphate (PRPP) and finishes with histidine and occurs through the reactions of the following enzymes:[9]
HisG-> HisE/HisI-> HisA-> HisH-> HisF-> HisB-> HisC-> HisB-> HisD (HisE/I and HisB are both bifunctional enzymes)
All of the enzymes are coded for on the his operon. This operon has a distinct block of the leader sequence, called block 1:
Met-Thr-Arg-Val-Gln-Phe-Lys-His-His-His-His-His-His-His-Pro-Asp
This leader sequence is very important for the regulation of histidine in "E. coli". The his operon operates under a system of coordinated regulation where all the gene products will be repressed or depressed equally. The main factor in the repression or derepression of histidine synthesis is the concentration of histidine charged tRNAs. The regulation of histidine is actually quite simple considering the complexity of its biosynthesis pathway and, it closely resembles regulation of tryptophan. In this system the full leader sequence has 4 blocks of complementary strands that can form hairpin loops structures.[9] Block one, shown above, is the key to regulation. When histidine charged tRNA levels are low in the cell the ribosome will stall at the string of His residues in block 1. This stalling of the ribosome will allow complementary strands 2 and 3 to form a hairpin loop. The loop formed by strands 2 and 3 forms an anti-terminator and translation of the his genes will continue and histidine will be produced. However, when histidine charged tRNA levels are high the ribosome will not stall at block 1, this will not allow strands 2 and 3 to form a hairpin. Instead strands 3 and 4 will form a hairpin loop further downstream of the ribosome. The hairpin loop formed by strands 3 and 4 is a terminating loop, when the ribosome comes into contact with the loop, it will be “knocked off” the transcript. When the ribosome is removed the his genes will not be translated and histidine will not be produced by the cell.[10]
3-Phosphoglycerates[edit]
Serine[edit]
Serine is the first amino acid in this family to be produced; it is then modified to produce both glycine and cysteine (and many other biologically important molecules). Serine is formed from 3-phosphoglycerate in the following pathway:
3-phosphoglycerate-> phosphohydroxyl-pyruvate-> phosphoserine-> serine
The conversion from 3-phosphoglycerate to phosphohydroxyl-pyruvate is achieved by the enzyme phosphoglycerate dehydrogenase. This enzyme is the key regulatory step in this pathway. Phosphoglycerate dehydrogenase is regulated by the concentration of serine in the cell. At high concentrations this enzyme will be inactive and serine will not be produced. At low concentrations of serine the enzyme will be fully active and serine will be produced by the bacterium.[11] Since serine is the first amino acid produced in this family both glycine and cysteine will be regulated by the available concentration of serine in the cell.[12]
Glycine[edit]
Glycine is synthesized from serine using the enzyme serine hydromethyltransferase (SHMT), which is coded by the gene glyA. The enzyme effectively removes a hydroxyl group from serine and replaces it with a methyl group to yield glycine. This reaction is the only way E. coli can produce glycine. The regulation of glyA is very complex and is known to incorporate serine, glycine, methionine, purines, thymine, and folates however, the full mechanism has yet to be elucidated.[13] The methionine gene product MetR and the methionine intermediate homocysteine are known to positively regulate glyA. Homocysteine is a coactivator of glyA and must act in concert with MetR.[13][14] On the other hand, PurR, a protein which plays a role in purine synthesis and S-adeno-sylmethionine are known to down regulate glyA. PurR binds directly to the control region of glyA and effectively turns the gene off so that glycine will not be produced by the bacterium.
Cysteine[edit]
Cysteine is a very important molecule for a bacterium’s survival. This amino acid harbors a sulfur atom and can actively participate in disulfide bond formation. The genes required for the synthesis of cysteine are coded for on the cys regulon. The integration of sulfur into the molecule is positively regulated by CysB. CysB is the main focus of cysteine regulation. Effective inducers of this regulon are N-acetyl-serine (NAS) and very small amounts of reduced sulfur. CysB functions by binding to DNA half sites on the cys regulon. These half sites differ in quantity and arrangement depending on the promoter of interest. There is however one half site that is conserved. It lies just upstream of the -35 site of the promoter. There are also multiple accessory sites depending on the promoter. In the absence of the inducer, NAS, CysB will bind the DNA and cover many of the accessory half sites. Without the accessory half sites the regulon cannot be transcribed and cysteine will not be produced. It is believed that the presence of NAS causes CysB to undergo a conformational change. This conformational change allows CysB to bind properly to all the half sites and causes the recruitment of the RNA polymerase. The RNA polymerase will then transcribe the cys regulon and cysteine will be produced.
Further regulation is required for this pathway, however. CysB can actually down regulate its own transcription by binding to its own DNA sequence and blocking the RNA polymerase. In this case NAS will act to disallow the binding of CysB to its own DNA sequence. OAS is a precursor of NAS, cysteine itself can inhibit CysE which functions to create OAS. Without the necessary OAS, NAS will not be produced and cysteine will not be produced. There are two other negative regulators of cysteine. These are the molecules sulfide and thiosulfate, they act to bind to CysB and they compete with NAS for the binding of CysB.[15]
Pyruvates[edit]
Pyruvate is the end result of glycolysis and can feed into both the TCA cycle and fermentation processes.[16] Reactions beginning with either one or two molecules of pyruvate cause the synthesis of alanine, valine, and leucine. Feedback inhibition of final products is the main method of inhibition, and, in E. coli, the ilvEDA operon also plays a part in this regulation.
Alanine[edit]
Alanine is produced by the transamination of one molecule of pyruvate using two alternate steps: 1) conversion of glutamate to α-ketoglutarate using a glutamate-alanine transaminase, and 2) conversion of valine to α-ketoisovalerate via Transaminase C.
Not much is known about the regulation of alanine synthesis. The only definite method is the bacterium’s ability to repress Transaminase C activity by either valine or leucine (see ilvEDA operon). Other than that, alanine biosynthesis does not seem to be regulated.[17]
Valine[edit]
Valine is produced by a four-enzyme pathway. It begins with the reaction of two pyruvate molecules catalyzed by Acetohydroxy acid synthase yielding α-acetolactate. Step two is the NADPH+ + H+ - dependent reduction of α-acetolactate and migration of the methane groups to produce α, β-dihydroxyisovalerate. This is catalyzed by Acetohydroxy isomeroreductase. The third reaction is the dehydration reaction of α, β-dihydroxyisovalerate catalyzed by Dihydroxy acid dehydrase resulting in α-ketoisovalerate. Finally, a transamination catalyzed either by an alanine-valine transaminase or a glutamate-valine transaminase results in valine.
Valine performs feedback inhibition to inhibit the Acetohydroxy acid synthase used to combine the first two pyruvate molecules.[17]
Leucine[edit]
The leucine synthesis pathway diverges from the valine pathway beginning with α-ketoisovalerate. α-Isopropylmalate synthase reacts with this substrate and Acetyl CoA to produce α-isopropylmalate. An isomerase then isomerizes α-isopropylmalate to β-isopropylmalate. The third step is the NAD+-dependent oxidation of β-isopropylmalate via the action of a dehydrogenase to yield α-ketoisocaproate. Finally is the transamination via the action of a glutamate-leucine transaminase to result in leucine.
Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase.[17] Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its pathway also can inhibit the synthesis of leucine.
ilvEDA operon[edit]
The genes that encode both the Dihydroxy acid dehydrase used in the creation of α-ketoisovalerate and Transaminase E, as well as other enzymes are encoded on the ilvEDA operon. This operon is bound and inactivated by valine, leucine, and isoleucine. (Isoleucine is not a direct derivative of pyruvate, but is produced by the use of many of the same enzymes used to produce valine and, indirectly, leucine.) When one of these amino acids is limited, the gene furthest from the amino-acid binding site of this operon can be transcribed. When a second of these amino acids is limited, the next-closest gene to the binding site can be transcribed, and so forth.[17]
Amino acids as precursors to other biomolecules[edit]
Amino acids are precursors of a variety of biomolecules. Glutathione (γ-Glu-Cys-Gly) serves as a sulfhydryl buffer and detoxifying agent. Glutathione peroxidase, a selenoenzyme, catalyzes the reduction of hydrogen peroxide and organic peroxides by glutathione. Nitric oxide, a short-lived messenger, is formed from arginine. Porphyrins are synthesized from glycine and succinyl CoA, which condense to give δ-aminolevulinate. Two molecules of this intermediate become linked to form porphobilinogen. Four molecules of porphobilinogen combine to form a linear tetrapyrrole, which cyclizes to uroporphyrinogen III. Oxidation and side-chain modifications lead to the synthesis of protoporphyrin IX, which acquires an iron atom to form heme.[18]
References[edit]
Jump up ^ Annigan, Jan. "How Many Amino Acids Does the Body Require?". SFGate. Demand Media. Retrieved 28 July 2015.
Jump up ^ Fürst P, Stehle P (1 June 2004). "What are the essential elements needed for the determination of amino acid requirements in humans?". J. Nutr. 134 (6 Suppl): 1558S–1565S. PMID 15173430.
Jump up ^ Reeds PJ (1 July 2000). "Dispensable and indispensable amino acids for humans". J. Nutr. 130 (7): 1835S–40S. PMID 10867060.
Jump up ^ Manchester KL (1964). "Sites of Hormonal Regulation of Protein Metabolism". In Munro HN, Allison JB. Mammalian protein metabolism. 4. New York: Academic Press. p. 229. ISBN 978-0-12-510604-7.
^ Jump up to: a b c d e f g h Shapiro BM, Stadtman ER (1970). "The Regulation of Glutamine Synthesis in Microorganisms". Annual Review of Microbiology. 24: 501–524. doi:10.1146/annurev.mi.24.100170.002441. PMID 4927139.
Jump up ^ White D (2007). The physiology and biochemistry of prokaryotes (3rd ed.). New York: Oxford Univ. Press. ISBN 0195301684.
^ Jump up to: a b Marco-Marín C, Gil-Ortiz F, Pérez-Arellano I, Cervera J, Fita I, Rubio V (2007). "A Novel Two-domain Architecture Within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia coli Glutamate 5-kinase". Journal of Molecular Biology. 367 (5): 1431–1446. doi:10.1016/j.jmb.2007.01.073. PMID 17321544.
Jump up ^ Maas WK (1991). "The regulation of arginine biosynthesis: its contribution to understanding the control of gene expression". Genetics. 128 (3): 489–94. PMC 1204522  . PMID 1874410.
^ Jump up to: a b Cohen GN (2007). The Biosynthesis of Histidine and Its Regulation. Springer. pp. 399–407.
Jump up ^ "Regulation of Histidine and Hut Operons". Retrieved 29 April 2012.
Jump up ^ Bridgers WF (1970). "The relationship of the metabolic regulation of serine to phospholipids and one-carbon metabolism". International Journal of Biochemistry. 1 (4): 495–505. doi:10.1016/0020-711X(70)90065-0.
Jump up ^ Pilzer LI (December 1963). "The Pathway and Control of Serine Biosynthesis in Escherichia coli". J. Biol. Chem. 238: 3934–44. PMID 14086727.
^ Jump up to: a b Steiert JG, Rolfes RJ, Zalkin H, Stauffer GV (1990). "Regulation of the Escherichia coli glyA gene by the purR gene product". J. Bacteriol. 172 (7): 3799–803. PMC 213358  . PMID 2113912.
Jump up ^ Plamann MD, Stauffer GV (1989). "Regulation of the Escherichia coli glyA gene by the metR gene product and homocysteine". J. Bacteriol. 171 (9): 4958–62. PMC 210303  . PMID 2670901.
Jump up ^ Figge RM (2007). "Methione biosynthesis". In Wendisch VF. Amino acid biosynthesis: pathways, regulation, and metabolic engineering. Berlin: Springer. pp. 206–208. ISBN 3540485953.
Jump up ^ Lehninger AL, Cox MM, Nelson DL (2008). Lehninger principles of biochemistry (5th ed.). New York: W.H. Freeman. p. 528. ISBN 978-0-7167-7108-1.
^ Jump up to: a b c d Umbarger HE (1978). "Amino Acid Biosynthesis and its Regulation". Annual Review of Biochemistry. 47: 533–606. doi:10.1146/annurev.bi.47.070178.002533. PMID 354503.
Jump up ^ Berg JM, Tymoczko JL, Stryer L (2002). Biochemistry (5th ed.). New York, NY: W. H. Freeman. ISBN 0-7167-3051-0.
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Metabolism: Protein metabolism, synthesis and catabolism enzymes
Essential amino acids are in Capitals
K→acetyl-CoA
LYSINE→
Saccharopine dehydrogenase
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(see below)
G
G→pyruvate
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proline→
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PYCR1
arginine→
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glutamate→glutamine: Glutamine synthetase
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succinyl-CoA
VALINE→
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Branched-chain alpha-keto acid dehydrogenase complex
Enoyl-CoA hydratase
3-hydroxyisobutyryl-CoA hydrolase
3-hydroxyisobutyrate dehydrogenase
Methylmalonate semialdehyde dehydrogenase
ISOLEUCINE→
Branched-chain amino acid aminotransferase
Branched-chain alpha-keto acid dehydrogenase complex
3-hydroxy-2-methylbutyryl-CoA dehydrogenase
METHIONINE→
generation of homocysteine: Methionine adenosyltransferase
Adenosylhomocysteinase
regeneration of methionine: Methionine synthase/Homocysteine methyltransferase
Betaine-homocysteine methyltransferase
conversion to cysteine: Cystathionine beta synthase
Cystathionine gamma-lyase
THREONINE→
Threonine aldolase
→succinyl-CoA→TCA
Propionyl-CoA carboxylase
Methylmalonyl CoA epimerase
Methylmalonyl-CoA mutase
G→fumarate
PHENYLALANINE→tyrosine→
Phenylalanine hydroxylase
Tyrosine aminotransferase
4-Hydroxyphenylpyruvate dioxygenase
Homogentisate 1,2-dioxygenase
Fumarylacetoacetate hydrolase
tyrosine→melanin: Tyrosinase
G→oxaloacetate
asparagine→aspartate→
Asparaginase/Asparagine synthetase
Aspartate transaminase
Retrieved from "https://en.wikipedia.org/w/index.php?title=Amino_acid_synthesis&oldid=814794458"
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text:
Magic (B.o.B song)
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
"Magic"
Single by B.o.B featuring Rivers Cuomo
from the album B.o.B Presents: The Adventures of Bobby Ray
Released
July 6, 2010 (2010-07-06)
Format
Digital download
CD single
Recorded
2010
Genre
Hip hop
pop punk[1]
Length
3:16
Label
Grand Hustle
Rebel Rock
Atlantic
Songwriter(s)
Bobby Simmons
Rivers Cuomo
Lukasz Gottwald
Producer(s)
Dr. Luke
B.o.B singles chronology
"Bet I"
(2010) "Magic"
(2010) "So High"
(2010)
"Bet I"
(2010) "Magic"
(2010) "So High"
(2010)
Rivers Cuomo singles chronology
"Magic"
(2010) Magic2010 "Can't Keep My Hands off You"
(2011) Can't Keep My Hands off You2011
"Magic" is a song by American hip hop recording artist B.o.B, released on June 7, 2010 as the fifth single from his debut studio album B.o.B Presents: The Adventures of Bobby Ray (2010). The track features Weezer's lead singer Rivers Cuomo, singing the chorus. It was written by both artists, alongside the song's producer Dr. Luke. In the UK, the track made Radio 1's B-Playlist.[2]
Contents
1 Composition
2 Reception
3 Music video
4 Track listing
5 Charts and certifications
5.1 Weekly charts
5.2 Year-end charts
5.3 Certifications
6 In other media
7 References
8 External links
Composition[edit]
"Magic" is written in the key of B major with a tempo of 82 beats per minute in common time. The song follows a chord progression of B5–E5–G♯5–F♯5, and the vocals in the song span from D♯4 to F♯5.[3][4]
Reception[edit]
Despite mixed reviews, the song progressed up and down the Billboard Hot 100 chart, reaching number 10 at its peak.[5] Billboard.com gave it a positive review, saying, "The song's strongest force is an infectious, throbbing synth-guitar hook from Dr. Luke, who seamlessly fuses B.o.B's verses with a chorus by Weezer frontman Rivers Cuomo that demands a singalong. The result is stellar."[6] The reviewer at TinyMixtapes.com said that "'Magic' is magnificently, triumphantly corny, enough to give Steve Miller and that guy from The Outfield a run for their money. 'Magic' isn't good by any stretch of the imagination, but it is goofily enjoyable."[7] In his album review for Spin, Kenny Herzog wrote, "The Adventures of Bobby Ray is a hip-hop Scary Movie, tossing off references (Vampire Weekend sample, Rivers Cuomo cameo) while struggling to establish a distinctive identity."[8] Pitchfork questioned "the appearance by Weezer's Rivers Cuomo, whose creepily blank vocals on 'Magic' sound like the engineer has a gun to his head".[9] The Guardian's Paul MacInnes wrote that "all the Chris Martinesque piano lines and calibrated guest appearances – from Weezer's River Cuomo to Janelle Monáe – can't obscure an absence of soul throughout."[10]
Music video[edit]
B.o.B (right) in the music video
The music video was released on MTV at midnight on September 3, 2010(www.mtv.com/news/2296301/bob-magic-video-rivers-cuomo/date=April 2011}} The video features B.o.B trying to wake himself up from a dream. He was also performing with Rivers Cuomo in the video on a stage at a wild party. In addition, Paul Iacono from the MTV show The Hard Times of RJ Berger is featured dancing on stage. The video was directed by Sanaa Hamri.[citation needed]
Track listing[edit]
"Magic" - 3:16
"Mellow Fellow" - 2:58
Charts and certifications[edit]
Weekly charts[edit]
Chart (2010)
Peak
position
Australia (ARIA)[11] 5
Canada (Canadian Hot 100)[12] 17
European Hot 100 Singles[13] 47
Ireland (IRMA)[14] 16
Netherlands (Dutch Top 40)[15] 6
New Zealand (Recorded Music NZ)[16] 6
Scotland (Official Charts Company)[17] 17
Sweden (Sverigetopplistan)[18] 53
UK Singles (Official Charts Company)[19] 16
UK R&B (Official Charts Company)[20] 2
US Billboard Hot 100[5] 10
US Hot Rap Songs (Billboard)[21] 25
US Mainstream Top 40 (Billboard)[22] 12
US Rhythmic (Billboard)[23] 30
Year-end charts[edit]
Chart (2010)
Position
Australian Singles Chart[24] 44
US Billboard Hot 100[25] 63
Certifications[edit]
Region
Certification
Certified units/Sales
Canada (Music Canada)[26]
Platinum 80,000^
New Zealand (RMNZ)[27]
Gold 7,500*
United States (RIAA)[28]
2× Platinum 2,000,000^
*sales figures based on certification alone
^shipments figures based on certification alone
In other media[edit]
The Treblemakers, an all-male a cappella group in the musical comedy Pitch Perfect, sang this song in their finale performance.
American female rapper Becky G, recorded a new version of the song for The Smurfs 2 soundtrack called Magik 2.0. Her rendition features singer Austin Mahone singing the hook while Becky raps the verses. It was produced by A.C.
References[edit]
Jump up ^ http://www.slantmagazine.com/music/review/b-o-b-b-o-b-presents-the-adventures-of-bobby-ray
Jump up ^ "BBC - Radio 1 - Playlist". Radio 1.
Jump up ^ Simmons Jr., Bobby Ray. "B.o.B "Magic" Sheet Music in B Major (transposable) - Download & Print". Musicnotes.com. Retrieved 2016-10-14.
Jump up ^ "BPM for 'magic' by bob | songbpm.com". songbpm.com. Retrieved 2016-10-14.
^ Jump up to: a b "B.o.B Chart History (Hot 100)". Billboard.
Jump up ^ "Billboard.com article"
Jump up ^ "B.o.B. - B.o.B Presents: The Adventures of Bobby Ray | Music Review". Tiny Mix Tapes.
Jump up ^ Herzog, Kenny (April 26, 2010). "B.o.B, 'The Adventures of Bobby Ray' (Atlantic)". Spin Magazine Online.
Jump up ^ Greene, Jayson (May 13, 2010). "Pitchfork: Album Reviews: B.o.B: The Adventures of Bobby Ray". Pitchfork Media.
Jump up ^ MacInnes, Paul (May 27, 2010). "B.o.B.: B.o.B. Presents the Adventures of Bobby Ray". guardian.co.uk. Guardian News and Media.
Jump up ^ "Australian-charts.com – B.o.B feat. Rivers Cuomo – Magic". ARIA Top 50 Singles.
Jump up ^ "B.o.B Chart History (Canadian Hot 100)". Billboard.
Jump up ^ " European Hot 100: Week of November 20, 2010". Billboard.com
Jump up ^ "Chart Track: Week 42, 2010". Irish Singles Chart.
Jump up ^ "Nederlandse Top 40 – B.o.B feat. Rivers Cuomo" (in Dutch). Dutch Top 40.
Jump up ^ "Charts.nz – B.o.B feat. Rivers Cuomo – Magic". Top 40 Singles.
Jump up ^ "Official Scottish Singles Sales Chart Top 100". Official Charts Company.
Jump up ^ "Swedishcharts.com – B.o.B feat. Rivers Cuomo – Magic". Singles Top 100.
Jump up ^ "Official Singles Chart Top 100". Official Charts Company.
Jump up ^ "Official R&B Singles Chart Top 40". Official Charts Company.
Jump up ^ "B.o.B Chart History (Hot Rap Songs)". Billboard.
Jump up ^ "B.o.B Chart History (Pop Songs)". Billboard.
Jump up ^ "B.o.B Chart History (Rhythmic)". Billboard.
Jump up ^ "ARIA Charts – End Of Year Charts – Top 100 Singles 2010". Australian Recording Industry Association. Retrieved 2011-01-08.
Jump up ^ "Hot 100 Songs: 2010 Year-End Charts - Billboard". Billboard.
Jump up ^ "Canadian single certifications – B.o.B – Magic". Music Canada.
Jump up ^ THE FIELD id (chart number) MUST BE PROVIDED for NEW ZEALAND CERTIFICATION.
Jump up ^ "American single certifications – B.o.B – Magic". Recording Industry Association of America. If necessary, click Advanced, then click Format, then select Single, then click SEARCH
External links[edit]
Lyrics of this song at MetroLyrics
show
v
t
e
B.o.B
Discography
Production discography
Studio albums
B.o.B Presents: The Adventures of Bobby Ray
Strange Clouds
Underground Luxury
Ether
Compilations
Elements
We Want Smoke (with Hustle Gang)
Mixtapes
G.D.O.D. (Get Dough or Die) (with Hustle Gang)
Psycadelik Thoughtz
Singles
"Nothin' on You"
"Don't Let Me Fall"
"Airplanes"
"Bet I"
"Magic"
"I'll Be in the Sky"
"Strange Clouds"
"Play the Guitar"
"So Good"
"So Hard to Breathe"
"Both of Us"
"Out of My Mind"
"We Still in This Bitch"
"HeadBand"
"Ready"
"John Doe"
"Not for Long"
"Back and Forth"
Featured singles
"Don't Go There"
"So High"
"Price Tag"
"The One That Got Away"
"Am I a Psycho?"
"Memories Back Then"
"Brokenhearted"
"Up Down (Do This All Day)"
"Paranoid"
"Numb"
"Secrets"
"Hood Go Crazy"
Promotional singles
"Blow (Remix)"
"Good Life (Remix)"
"Body Party (Remix)"
Other songs
"Generation Lost"
"I'm On 2.0"
"Double or Nothing"
"Flatline"
Related articles
All City Chess Club
A.K.O.O Clothing
Grand Hustle Records
Jim Jonsin
Label No Genre
T.I.
Rebel Rock Entertainment
show
v
t
e
Rivers Cuomo
Albums
Alone: The Home Recordings of Rivers Cuomo
Alone II: The Home Recordings of Rivers Cuomo
Alone III: The Pinkerton Years
Live albums
Not Alone – Rivers Cuomo and Friends: Live at Fingerprints
Featured singles
"Magic"
"High Maintenance"
"Can't Keep My Hands off You"
"Sober Up"
Member of
Weezer
Homie
Scott & Rivers
Related bands
The Rentals
The Special Goodness
The Relationship
Space Twins
Related articles
Rivers Cuomo discography
Weezer discography
Songs from the Black Hole
The Kitchen Tapes
Foozer
Retrieved from "https://en.wikipedia.org/w/index.php?title=Magic_(B.o.B_song)&oldid=849003357"
Categories:
2010 singles
B.o.B songs
Songs written by B.o.B
Songs written by Rivers Cuomo
Grand Hustle Records singles
Song recordings produced by Dr. Luke
Atlantic Records singles
Songs written by Dr. Luke
2010 songs
Hidden categories:
Cite certification used with missing parameters
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All articles with unsourced statements
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Singlechart usages for Australia
Singlechart usages for Canada
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Singlechart usages for UK
Singlechart usages for UKrandb
Singlechart usages for Billboardhot100
Singlechart usages for Billboardrapsongs
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Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.
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Jack Wild
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Jack Wild
Jack Wild, 1970
Born
(1952-09-30)30 September 1952
Royton, Lancashire, England
Died
1 March 2006(2006-03-01) (aged 53)
Tebworth, Bedfordshire, England
Occupation
Actor, singer
Years active
1964–2006
Spouse(s)
Gaynor Jones (1976–1985)
Claire Harding (2005–2006 his death)
Jack Wild (30 September 1952 – 1 March 2006) was an English actor and singer, known for his teenage performances as the Artful Dodger in Oliver! (film) (1968) and as Jimmy in the NBC children's television series H.R. Pufnstuf (1969) and accompanying 1970 feature film. He played Much the Miller's Son in Robin Hood: Prince of Thieves (1991).
The film of Lionel Bart's musical, Oliver! earned him Golden Globe Award and BAFTA Award nominations, plus a nomination for the Academy Award for Best Supporting Actor. As Jimmy, he was the protagonist of the television series and feature film about a boy befriended by a friendly dragon named H.R. Pufnstuf, produced by Sid and Marty Krofft.
Jack Wild (right) with Oliver! co-star Mark Lester at the 41st Annual Academy Awards, 14 April 1969.
Contents
[hide]
1 Early life
2 Entertainment career
3 Challenges
4 Career restarts
5 Death
6 Autobiography
7 Filmography
8 Discography
8.1 Albums
8.2 Singles
9 See also
10 References
11 Bibliography
12 External links
Early life[edit]
Wild was an English born actor born into a working class family in a small town in Lancashire (now Greater Manchester), called Royton, near Oldham. Wild moved to Bungalow in London, with his parents and his older brother Arthur in 1960 at the age of eight, where he got a job helping the milkman, which paid about five shillings.
He was discovered whilst playing football with his brother in the park by theatrical agent June Collins mother of Phil Collins.
Collins enrolled both Jack and Arthur at the Barbara Speake Stage School, an independent school in Acton in West London.
Entertainment career[edit]
Wild with the title character in the NBC children's series H.R. Pufnstuf, 1969
The Wild brothers sought acting roles to supplement their parents' income and, in the autumn of 1964, both were cast in a West End theatre production of Lionel Bart's Oliver!, Arthur in the title role, and Jack as a member of Fagin's gang, Charley Bates.[1] Although Jack auditioned as The Artful Dodger for several subsequent stage productions of Oliver!, he was always turned down because he was too short.[2] He stayed with the show until the spring of 1966, when he left to make the film serial Danny the Dragon for the Children's Film Foundation.[3] Wild's first speaking roles on TV were an episode of Out of the Unknown, and the third part of the BBC’s version of the Wesker Trilogy, I’m Talking About Jerusalem. By the time Wild was chosen to portray the Artful Dodger for the 1968 movie version of Oliver! he had also appeared in episodes of Z Cars, The Newcomers (TV series), and George and the Dragon (TV series). He received critical acclaim and several nominations for his appearance as the Artful Dodger:
Academy Award for Best Supporting Actor
Golden Globe Award for Most Promising Newcomer
BAFTA Award for Most Promising Newcomer
It was at the 1968 premiere of Oliver! that Wild met brothers Sid and Marty Krofft, who thought he would make a good lead for a show they were developing called H.R. Pufnstuf. Wild starred in this American family television series that launched in 1969. He was to be paid $1,000,000 to play "Jimmy", a boy washed up on "Living Island" (a magic island) with his best friend Freddy, a talking flute, although Jack stated in 2001 that he never received the money. He starred in the movie Pufnstuf (1970). Other roles followed, including the films Melody (1971) (with Oliver! co-star Mark Lester) and Flight of the Doves (1971). The latter film reunited him with Ron Moody, who had played Fagin in Oliver!.
Wild also embarked on a recording career, cutting one album for Capitol Records- containing the single "Some Beautiful" that received a lot of airplay on Radio Luxembourg, but didn't chart very highly - and two for Buddah Records in the early 1970s. The three albums were called The Jack Wild Album, Everything's Coming Up Roses and Beautiful World.[4]
At the height of his acting career, Jack usually acted younger than he was. For H.R. Pufnstuf, Wild was a seventeen-year-old playing a boy who was eleven.
"When I first entered in the show business," Jack said in 1999," Of course I didn't mind playing younger roles. However it did bug me when I would be twenty-one being offered the role of a thirteen-year-old. I'm not saying I didn't enjoy playing these roles; I had barrels of fun, I just wanted more serious and dramatic roles; it's that simple."
During the early 1970s, Wild was considered "one of the world's teen heartthrobs," alongside David Cassidy and Barry Williams. With large hazel eyes, a somewhat pug nose and freckles, Jack was loved and adored by many girls across the globe. "I received roughly 2,000 fan letters a week," he stated in 1989. "I never left any one of them blank. I always answered, even if I was exhausted. I really thought it was one of the most important things."
While Jack and Arthur were at Barbara Speake stage school, Jack met Welsh-born actress Gaynor Jones when they were around twelve years old. After he left the school in 1966, he didn't see her again until Christmas of 1970, when she was hosting a Christmas party. Then, after seeing her for the first time in four years, he got her telephone number and they were soon dating. They married on Valentine's Day 1976, Wild was 23 years old and Jones was 22. Afterwards, they celebrated with a honeymoon to Paris. After they returned, bought a home a few weeks later in the wealthy suburb Richmond, London.
Challenges[edit]
Wild struggled to make the transition to adult stardom. He had begun smoking at the age of 12, and by age 17 was drinking heavily.
At age 21 he was already an alcoholic and a diabetic. This did not help him find acting work, and by 1976 his film career was badly stalled. In 1981 he was supposed to star with Suzi Quatro in a series about a modern-day Bonnie and Clyde for British television, but it was cancelled at the last minute. His alcoholism ruined both his career and marriage to Gaynor, who left him in 1985 because of his excessive drinking.[1]
After exhausting his remaining fortune Wild lived with his retired father for a few years.[5] His alcoholism caused three cardiac arrests and resulted in several hospital stays until he stopped drinking in 1989.[5] Wild later admitted his alcoholism was so debilitating during this period that from the late 1970s until he went sober, he was incapable of doing any kind of work.[6]
Career restarts[edit]
Wild unsuccessfully attempted various alcoholism rehabilitation programmes and finally gave up drinking on 6 March 1989 after joining Alcoholics Victorious.[6] He returned to the big screen in a few minor roles, such as in the 1991 Kevin Costner film Robin Hood: Prince of Thieves and as a peddler in Basil (1998).[2] For the most part, Wild spent the remainder of his career working in theatre. His last major appearance was as the male lead, "Mouse", in Tayla Goodman's rock musical Virus. The show ran for two weeks at the Theatre Royal, Nottingham. For his final film appearance, Wild had a minor role in Moussaka & Chips (2000), where he once again worked with Ron Moody.[2]
Death[edit]
Wild died on 1 March 2006 at age 53 after a long battle with mouth cancer, which he blamed on his drinking and/or smoking.[1][7] Diagnosed with the disease in 2000, he initially underwent chemotherapy, but later had part of his tongue and both vocal cords removed in July 2004.[1] Because of this surgery, he had lost his speech and had to communicate through his wife, Claire Harding, whom he met when they were appearing in Jack and the Beanstalk in Worthing.[1] Wild was reportedly working on his autobiography, but died before it could be completed.[8]
Wild's body was buried in Toddington Parish Cemetery, Bedfordshire.[9]
Autobiography[edit]
At the time of his death, Wild and his widow, Claire Harding, had been working on his autobiography. It was completed by Claire, who explained: 'All the material was there when Jack died, it just needed rearranging, editing, and, in certain sections, writing out from transcripts Jack and I made as we recorded him talking about his life.'[10] In 2016, his autobiography, It's a Dodger's Life was finally published by Fantom Films (ISBN 978-1-78196-266-4) with a foreword by Pufnstuf co-star Billie Hayes, an afterword by Clive Francis, and an epilogue by Claire Harding.[11]
Filmography[edit]
List of acting performances in film and television
Title
Year
Alternate titles
Role
Notes
Oliver!
1968 The Artful Dodger 1st film to co-star with Mark Lester[1] and Ron Moody.
Nominated – Academy Award for Best Supporting Actor
Nominated – BAFTA Award for Most Promising Newcomer
Nominated – Golden Globe Award for Most Promising Newcomer
H.R. Pufnstuf
1969 Jimmy TV series
Pufnstuf
1970 Pufnstuf Zaps the World Jimmy
Melody
1971 S.W.A.L.K. Ornshaw 2nd and last film to co-star with Mark Lester.[1]
Flight of the Doves
1971 Finn Dove 2nd film to co-star with Ron Moody.
Pied Piper, TheThe Pied Piper
1972 Gavin
14, TheThe 14
1973 Existence (USA)
The Wild Little Bunch (USA) Reg
Sigmund and the Sea Monsters
1973 Himself Guest Appearance
Keep It Up Downstairs
1976 Peregrine Cockshute
Alicja
1982 Mock Turtle
Robin Hood: Prince of Thieves
1991 Much the Miller's Son
Basil
1998 Peddler
Moussaka & Chips
2005 Durgen Fleece 3rd and last film to co-star with Ron Moody. Last film
Discography[edit]
Albums[edit]
The Jack Wild Album (1970)
Everything's Coming Up Roses (1971)
A Beautiful World (1972)
Singles[edit]
List of singles, with selected chart positions
Title
Year
Peak chart positions
UK[12]
US
"Some Beautiful"
1970 46 92
"Wait For Summer"
1970 — 115
"(Holy Moses!) Everything's Coming Up Roses"
1971 — 107
"—" denotes releases that did not chart.
See also[edit]
List of oldest and youngest Academy Award winners and nominees
References[edit]
^ Jump up to: a b c d e f g "Jack Wild". The Independent. 3 March 2006.
^ Jump up to: a b c "Jack Wild - Biography". IMDb. Amazon.com. Retrieved 24 December 2013.
Jump up ^ "Official Jack Wild Website - Theatre Work".
Jump up ^ "Jack Wild: Albums". CMT.com. MTV Networks. Retrieved 5 September 2010.
^ Jump up to: a b "Jack Wild". The Daily Telegraph. London. 3 March 2006. ISSN 0307-1235. OCLC 49632006. Retrieved 5 September 2010.
^ Jump up to: a b Ian Wylie (29 December 2004). "Jack's Wild life | Manchester Evening News". menmedia.co.uk. Retrieved 30 April 2012.
Jump up ^ "My lifestyle caused my mouth cancer". BBC News, Health. BBC. 16 November 2005. Retrieved 5 September 2010.
Jump up ^ "Oliver! star Jack Wild dies at 53". BBC. 2006-03-02. Retrieved 2016-04-10.
Jump up ^ "Jack Wild (1952 - 2006)". Find A Grave. 2 March 2006. Retrieved 5 September 2010.
Jump up ^ Wild, Jack (2016). It’s a Dodger’s Life. Fantom Publishing. ISBN 978-1-78196-266-4.
Jump up ^ Published by Fantom Films (ISBN 978-1-78196-266-4)
Jump up ^ Roberts, David (2006). British Hit Singles & Albums (19th ed.). London: Guinness World Records Limited. p. 601. ISBN 1-904994-10-5.
This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. (March 2009) (Learn how and when to remove this template message)
Bibliography[edit]
Wild, Jack. Autobiography: It's A Dodger's Life, Fantom Films 2016. Hardback edition ISBN 978-1-78196-266-4
Holmstrom, John. The Moving Picture Boy: An International Encyclopaedia from 1895 to 1995, Norwich, Michael Russell, 1996, p. 296.
Dye, David. Child and Youth Actors: Filmography of Their Entire Careers, 1914-1985. Jefferson, NC: McFarland & Co., 1988, p. 239.
External links[edit]
Wikimedia Commons has media related to Jack Wild.
Jack Wild on IMDb
Jack Wild at the TCM Movie Database
Jack Wild Official Website New
Authority control
WorldCat Identities
VIAF: 34669634
LCCN: n91086654
ISNI: 0000 0001 2127 5896
GND: 143093649
SUDOC: 14314443X
BNF: cb14239104h (data)
MusicBrainz: 326f9dd2-8cff-4907-afbd-b404326f1594
Retrieved from "https://en.wikipedia.org/w/index.php?title=Jack_Wild&oldid=800637234"
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Take Our Daughters and Sons to Work Day
From Wikipedia, the free encyclopedia
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"Take Your Daughter To Work Day" redirects here. For the episode of The Office, see Take Your Daughter to Work Day (The Office).
Take Our Daughters And Sons To Work Day is a national day that gives children in the United States a glimpse into the working world. [1] Developed by the Take Our Daughters And Sons To Work Foundation, a 501(c)(3) non-profit educational organisation, the day revolves around parents taking their children to work to expose students to future job possibilities and the value of education.[2] It is the successor to Take Our Daughters To Work Day, which was expanded to include boys in 2003. In the U.S., it occurs on the fourth Thursday in April and onward every year.[3]
The last Take Our Daughters And Sons To Work Day occurred on Thursday, April 26, 2018, with more than 37 million Americans at over 3.5 million workplaces participating. [4]
Contents
1 History
2 See also
3 References
4 External links
History[edit]
Take Our Daughters To Work Day was created in New York City in the summer of 1992 by the Ms. Foundation for Women and its president, Marie C. Wilson, the Women's foundation treasurer, Ms. Daren Ball, and with support from foundation founder Gloria Steinem.[5] The first celebration took place on April 22, 1993, and has since been celebrated on the fourth Thursday of April in order for the 37 million children, parents, schools in over 3.5 million workplaces across the country, in addition to participants in over 200 countries around the world, to plan ahead for the annual event.[6] The day has generally been scheduled on a day that is a school day for most children in the United States, and schools are provided with literature and encouraged to promote the program. Educators are provided with materials for incorporating career exploration into school curricula on the day before or after the event.
In 2000, when asked by the Minneapolis Star Tribune which activities he would propose for a national day for boys equivalent to Take Our Daughters to Work day, author Robert Bly suggested that fathers take their sons to the library and show them the books they love. Noting that women have often been excluded from the work world, Bly said, "I think it's just as likely now that men will be shut out of the inward world, the literature world."
The program was officially expanded in 2003 to include boys; however, most companies that participated in the program had, since the beginning, allowed both boys and girls to participate, usually renaming it "Take Our Children to Work Day" or an equivalent.[7] The program's official website states that the program was changed in order to provide both boys and girls with opportunities to explore careers at an age when they are more flexible in terms of gender roles. The Ms. Foundation also states that men who have hosted children have benefited from being seen as parental figures in addition to their roles as professionals, which can contribute to combating gender stereotypes as well.
Prior to the inclusion of boys, the Ms. Foundation contended that the program was designed to specifically address self-esteem issues unique to girls and initially resisted pressure to include boys. Much of this pressure came from educators who did not wish to include the event in their curriculum given that their male students were not encouraged to participate.
In 2007, upon becoming its own separate foundation, the Take Our Daughters And Sons To Work program was turned over to Carolyn McKecuen, a MacArthur Genius Award recipient, who took effective control as its Executive Director before relocated to Elizabeth City, North Carolina where it has remained since. Gloria Steinem continues to maintain a role with the Take Our Daughters And Sons To Work Foundation as a member of its board of directors.
Employees across the United States and around the world typically invite their own children or relatives to join them at work, but the program particularly encourages employees to invite children from residential programs or shelters who may not be exposed to many adults in skilled professions today.
See also[edit]
Job shadow
Take Our Kids to Work Day
References[edit]
Jump up ^ News, A. B. C. (2018-04-26). "Take Our Daughters and Sons to Work Day: Little-known facts". ABC News. Retrieved 2018-07-16.
Jump up ^ "About". daughtersandsonstowork.org. Retrieved 2018-07-16.
Jump up ^ "Frequently Asked Questions". Take Our Daughters and Sons to Work Foundation. Retrieved 2015-02-09. For over 21 years, the Take Our Daughters and Sons to Work® event has been scheduled for the 18th of November...
Jump up ^ "The Dos And Don'ts Of Take Your Kids To Work Day". Forbes. Retrieved 2018-07-16.
Jump up ^ "Find out more about the Ms. Foundation for Women!". Ms. Foundation for Women.
Jump up ^ "Support - National Women's History Museum - NWHM". www.nwhm.org.
Jump up ^ "One Day of 'Take a Child to Work' Is Short on Substance : Boys are now being invited to join the formerly all-girl event. But it's doubtful kids find our jobs worth imitating. It may be better to just share the pride of accomplishment". Los Angeles Times. 1995-04-16. Retrieved 2013-04-27.
External links[edit]
Official homepage
Collection of articles regarding inclusion of boys as well as alternative events held prior to the Ms. Foundation event being expanded to include boys
Form 17, a short film about a bomb squad dad who brings his daughter to work
Retrieved from "https://en.wikipedia.org/w/index.php?title=Take_Our_Daughters_and_Sons_to_Work_Day&oldid=850546882"
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values: A list of edits made from this IP address [ctrl-alt-y]

values: You are encouraged to create an account and log in; however, it is not mandatory

values: You're encouraged to log in; however, it's not mandatory. [ctrl-alt-o]

values: Discussion about the content page [ctrl-alt-t]

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values:
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values: Past revisions of this page [ctrl-alt-h]

values: p-views navigation vectorTabs p-views-label

values:
p-cactions
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values:
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/wiki/Main_Page
Visit the main page

values:
/wiki/Main_Page
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z

values: Featured content – the best of Wikipedia

values: Find background information on current events

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values: A list of recent changes in the wiki [ctrl-alt-r]

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values: List of all English Wikipedia pages containing links to this page [ctrl-alt-j]

values: Recent changes in pages linked from this page [ctrl-alt-k]

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values: A list of all special pages [ctrl-alt-q]

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