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Escherichia coli K-12 substr. MG1655 Compound: L-valine

Abbrev Name: val

Synonyms: V, val, valine, L-val

Superclasses: an acidall carboxy acidsa carboxylatean amino acida non-polar amino acid
an acidall carboxy acidsa carboxylatean amino acidan alpha amino acida branched-chain amino acid
an acidall carboxy acidsa carboxylatean amino acidan alpha amino acida standard alpha amino acid
an acidall carboxy acidsa carboxylatean amino acidan L-amino acid
an amino acid or its derivativean amino acida non-polar amino acid
an amino acid or its derivativean amino acidan alpha amino acida branched-chain amino acid
an amino acid or its derivativean amino acidan alpha amino acida standard alpha amino acid
an amino acid or its derivativean amino acidan L-amino acid


Chemical Formula: C5H11NO2

Molecular Weight: 117.15 Daltons

Monoisotopic Molecular Weight: 118.0868036346 Daltons

L-valine compound structure

SMILES: CC(C)C([N+])C([O-])=O

InChI: InChI=1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)/t4-/m0/s1

InChIKey: InChIKey=KZSNJWFQEVHDMF-BYPYZUCNSA-N

Unification Links: CAS:72-18-4, ChEBI:57762, HMDB:HMDB00883, IAF1260:34167, KEGG:C00183, MetaboLights:MTBLC57762, PubChem:6971018

Standard Gibbs Free Energy of Formation (ΔfG in kcal/mol): -85.72

Reactions known to consume the compound:

tRNA charging :
a tRNAval + L-valine + ATP + H+ → an L-valyl-[tRNAval] + AMP + diphosphate

Reactions known to produce the compound:

Not in pathways:
a peptide with an N-terminal X-L-proline + H2O → a standard α amino acid + a peptide with an N-terminal L-proline + H+
a peptide + H2O → a standard α amino acid + a peptide
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a peptide + a standard α amino acid
a protein + H2O → a standard α amino acid + a peptide
β-aspartyl dipeptide + H2O → L-aspartate + a standard α amino acid
a dipetide with an N-terminal L-aspartate + H2O → L-aspartate + a standard α amino acid
a tripeptide + H2O → a dipeptide + a standard α amino acid
a dipeptide with proline at the C-terminal + H2O → L-proline + a standard α amino acid
a dipeptide + H2O → 2 a standard α amino acid

Not in pathways:
a polypeptide + H2O → a polypeptide + an L-amino acid

Not in pathways:
a carboxylic ester + H2O → an alcohol + a carboxylate + H+
an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+
an acyl phosphate + H2O → a carboxylate + phosphate + H+
an acyl-CoA + H2O → a carboxylate + coenzyme A + H+
a 1-acyl 2-lyso-phosphatidylcholine + H2O → a carboxylate + sn-glycero-3-phosphocholine + H+

Reactions known to both consume and produce the compound:

L-alanine biosynthesis I :
L-valine + 2-oxoglutarate ↔ 3-methyl-2-oxobutanoate + L-glutamate
pyruvate + L-valine ↔ L-alanine + 3-methyl-2-oxobutanoate

L-valine biosynthesis :
L-valine + 2-oxoglutarate ↔ 3-methyl-2-oxobutanoate + L-glutamate

In Reactions of unknown directionality:

Not in pathways:
L-methionine + a 2-oxo carboxylate = 2-oxo-4-methylthiobutanoate + a standard α amino acid

Not in pathways:
a 5-L-glutamyl-[peptide][periplasm] + an amino acid[periplasm] = a 5-L-glutamyl-amino acid[periplasm] + a peptide[periplasm]

Not in pathways:
a 2-acyl 1-lyso-phosphatidylcholine + H2O = a carboxylate + sn-glycero-3-phosphocholine + H+
an aldehyde[periplasm] + FAD[periplasm] + H2O[periplasm] = a carboxylate[periplasm] + FADH2[periplasm]

In Transport reactions:
Na+[periplasm] + L-valine[periplasm] → Na+[cytosol] + L-valine[cytosol],
ATP + L-valine[periplasm] + H2O → ADP + L-valine[cytosol] + phosphate + H+,
L-valine[cytosol]L-valine[periplasm],
L-valine[cytosol] + H+[periplasm]L-valine[periplasm] + H+[cytosol],
an amino acid[periplasm]an amino acid[extracellular space]

Enzymes activated by L-valine, sorted by the type of activation, are:

Activator (Mechanism unknown) of: threonine deaminase [Squires81]

Enzymes inhibited by L-valine, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: acetohydroxybutanoate synthase [Grimminger79], 3-methyl-2-oxobutanoate hydroxymethyltransferase [Powers76, Comment 1], acetohydroxybutanoate synthase, acetohydroxybutanoate synthase [Gollop89, Comment 2], acetolactate synthase [Gollop89]

This compound has been characterized as an alternative substrate of the following enzymes: leucine efflux transporter

In Growth Media: Neidhardt EZ rich defined medium, PMA nitrogen source test + val, PMA carbon source test + val


References

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

Grimminger79: Grimminger H, Umbarger HE (1979). "Acetohydroxy acid synthase I of Escherichia coli: purification and properties." J Bacteriol 1979;137(2);846-53. PMID: 370104

Powers76: Powers SG, Snell EE (1976). "Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties." J Biol Chem 1976;251(12);3786-93. PMID: 6463

Squires81: Squires CH, Levinthal M, De Felice M (1981). "A role for threonine deaminase in the regulation of alpha-acetolactate biosynthesis in Escherichia coli K12." J Gen Microbiol 1981;127, pt 1;19-25. PMID: 7040602


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Wed May 4, 2016, biocyc13.