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Escherichia coli K-12 substr. MG1655 Pathway: L-valine biosynthesis
Inferred from experiment

Pathway diagram: L-valine biosynthesis

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic

Genetic regulation schematic for L-valine biosynthesis

Superclasses: BiosynthesisAmino Acids BiosynthesisProteinogenic Amino Acids BiosynthesisL-valine Biosynthesis

The pathway of valine biosynthesis is a four-step pathway that shares all of its steps with the parallel pathway of isoleucine biosynthesis. These entwined pathways are part of the superpathway of branched amino acid biosynthesis, that generates not only isoleucine and valine, but also leucine.

As a consequence of having several of its component enzymes involved in the synthesis of three different amino acids, the pathway of isoleucine biosynthesis is subject to regulation by all three amino acids. The first step in the pathway is primarily inhibited by valine, along with inhibition by isoleucine and leucine. The potential disruption this might cause to the parallel isoleucine biosynthesis pathway step using the same enzymes is resolved by upregulation of an earlier step that is unique to isoleucine biosynthesis, as explained in the L-isoleucine biosynthesis I (from threonine) summary. In this way, valine biosynthesis can be regulated independently of isoleucine biosynthesis, despite all four valine biosynthesis enzymes also participating in isoleucine biosynthesis.

Citations: [Neidhardt96 ]

Superpathways: superpathway of branched amino acid biosynthesis

Created 02-Feb-1994 by Riley M, Marine Biological Laboratory
Last-Curated 08-Nov-2007 by Shearer A, SRI International


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Gollop89: Gollop N, Damri B, Barak Z, Chipman DM (1989). "Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli." Biochemistry 28(15);6310-7. PMID: 2675968

LeePeng79: Lee-Peng FC, Hermodson MA, Kohlhaw GB (1979). "Transaminase B from Escherichia coli: quaternary structure, amino-terminal sequence, substrate specificity, and absence of a separate valine-alpha-ketoglutarate activity." J Bacteriol 1979;139(2);339-45. PMID: 378964

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Vinogradov06: Vinogradov V, Vyazmensky M, Engel S, Belenky I, Kaplun A, Kryukov O, Barak Z, Chipman DM (2006). "Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties." Biochim Biophys Acta 1760(3);356-63. PMID: 16326011

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Adelberg53: Adelberg EA, Umbarger HE (1953). "Isoleucine and valine metabolism in Escherichia coli. V. alpha-Ketoisovaleric acid accumulation." J Biol Chem 205(1);475-82. PMID: 13117924

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Aulabaugh90: Aulabaugh A, Schloss JV (1990). "Oxalyl hydroxamates as reaction-intermediate analogues for ketol-acid reductoisomerase." Biochemistry 29(11);2824-30. PMID: 2189496

Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

Barak12: Barak Z, Chipman DM (2012). "Allosteric regulation in Acetohydroxyacid Synthases (AHASs)--different structures and kinetic behavior in isozymes in the same organisms." Arch Biochem Biophys 519(2);167-74. PMID: 22198286

Barak87: Barak Z, Chipman DM, Gollop N (1987). "Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria." J Bacteriol 169(8);3750-6. PMID: 3301814

Barak88: Barak Z, Calvo JM, Schloss JV (1988). "Acetolactate synthase isozyme III from Escherichia coli." Methods Enzymol 1988;166;455-8. PMID: 3071721

Brown78: Brown OR, Yein F (1978). "Dihydroxyacid dehydratase: the site of hyperbaric oxygen poisoning in branch-chain amino acid biosynthesis." Biochem Biophys Res Commun 85(3);1219-24. PMID: 367373

Burns95: Burns DM, Burger MJ, Beacham IR (1995). "Silent genes in bacteria: the previously designated 'cryptic' ilvHI locus of 'Salmonella typhimurium LT2' is active in natural isolates." FEMS Microbiol Lett 131(2);167-72. PMID: 7557326

Dailey86: Dailey FE, Cronan JE (1986). "Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source." J Bacteriol 1986;165(2);453-60. PMID: 3511034

Daniels92: Daniels DL, Plunkett G, Burland V, Blattner FR (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 1992;257(5071);771-8. PMID: 1379743

De74: De Felice M, Guardiola J, Esposito B, Iaccarino M (1974). "Structural genes for a newly recognized acetolactate synthase in Escherichia coli K-12." J Bacteriol 120(3);1068-77. PMID: 4612003

De78: De Felice M, Squires C, Levinthal M (1978). "A comparative study of the acetohydroxy acid synthase isoenzymes of Escherichia coli K-12." Biochim. Biophys. Acta 541;9-17.

deFelice78: de Felice M, Squires C, Levinthal M "A comparative study of the acetohydroxy acid synthase isoenzymes of Escherichia coli K-12." BBA 1978;541:9-17.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Duan09: Duan X, Yang J, Ren B, Tan G, Ding H (2009). "Reactivity of nitric oxide with the [4Fe-4S] cluster of dihydroxyacid dehydratase from Escherichia coli." Biochem J 417(3);783-9. PMID: 18945212

Engel04: Engel S, Vyazmensky M, Berkovich D, Barak Z, Chipman DM (2004). "Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of alpha-hydroxy ketones." Biotechnol Bioeng 88(7);825-31. PMID: 15558598

Eoyang84: Eoyang L, Silverman PM (1984). "Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12." J Bacteriol 157(1);184-9. PMID: 6360995

Eoyang86: Eoyang L, Silverman PM (1986). "Role of small subunit (IlvN polypeptide) of acetohydroxyacid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition." J Bacteriol 166(3);901-4. PMID: 3011751

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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