Information on EC 2.6.1.32 - valine-3-methyl-2-oxovalerate transaminase:

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota


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EC NUMBERCOMMENTARY
2.6.1.32-

RECOMMENDED NAMEGeneOntology No.
valine-3-methyl-2-oxovalerate transaminaseGO:0047301

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-oxobutanoate + L-isoleucine
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
amino group transfer----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
L-valine:(S)-3-methyl-2-oxopentanoate aminotransferase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
alanine-valine transaminase----
aminotransferase, valine-3-methyl-2-oxovalerate----
valine-2-keto-methylvalerate aminotransferase----
valine-isoleucine aminotransferase----
valine-isoleucine transaminase----
YfbQEscherichia coliC6UMN8, D2AFZ3a novel aminotransferase721875
YfdZEscherichia coliC6UMN8, D2AFZ3uncharacterized aminotransferase721875

CAS REGISTRY NUMBERCOMMENTARY
9023-14-7-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Escherichia coli-721875C6UMN8, D2AFZ3UniProtManually annotated by BRENDA team
Pisum sativum-639963--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coliC6UMN8, D2AFZ3an alanine auxotroph (mutated in yfdZ) is isolated from a prototrophic double mutant deficient in AvtA and YfbQ, a novel alanine aminotransferase, by chemical mutagenesis; Escherichia coli synthesizes L-alanine by means of three aminotransferases, YfbQ, YfdZ, and AvtA; level of yfdZ expression in minimal medium is higher than in rich medium; an alanine auxotroph (mutated in yfdZ) is isolated from a prototrophic double mutant deficient in AvtA and YfbQ by chemical mutagenesis; Escherichia coli synthesizes L-alanine by means of three aminotransferases, YfbQ, YfdZ, and AvtA; YfbQ contributes to most of the alanine aminotransferase activity in rich medium721875

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-valine + (S)-3-methyl-2-oxopentanoate3-methyl-2-oxobutanoate + L-isoleucine
show the reaction diagram
Pisum sativum--639963-639963?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
No entries in this field

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
sproutPisum sativum--639963Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
partialPisum sativum-639963

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
level of yfdZ expression in minimal medium is higher than in rich mediumEscherichia coliC6UMN8, D2AFZ3721875

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
639963Kagan, Z.S.; Dronov, A.S.; Kretovich, V.L.Separation of valine-glutamic aminotransferase from valine-isoleucine aminotransferase in pea sproutsDokl. Akad. Nauk SSSR1751171-11741967Pisum sativum-
721875Yoneyama, H.; Hori, H.; Lim, S.J.; Murata, T.; Ando, T.; Isogai, E.; Katsumata, R.Isolation of a mutant auxotrophic for L-alanine and identification of three major aminotransferases that synthesize L-alanine in Escherichia coliBiosci. Biotechnol. Biochem.75930-9382011Escherichia coli, Escherichia coli (C6UMN8), Escherichia coli (D2AFZ3) PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.32)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)