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Information on EC 2.6.1.7 - kynurenine-oxoglutarate transaminase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P47039

for references in articles please use BRENDA:EC2.6.1.7
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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.7 kynurenine-oxoglutarate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P47039
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aspartate aminotransferase, mitochondrial aspartate aminotransferase, kat ii, kat i, kynurenine aminotransferase ii, aadat, kat-i, kat-ii, kynurenine aminotransferase i, kynurenine-oxoglutarate transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminotransferase, kynurenine
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kynurenine 2-oxoglutarate transaminase
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kynurenine aminotransferase
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kynurenine transaminase (cyclizing)
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L-kynurenine aminotransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-kynurenine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-38-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate + H2O
show the reaction diagram
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via o-aminobenzoylpyruvic acid which is immediately converted to the intramolecularly dehydrated and cyclized form kynurenic acid
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Bna3 is not an formyl kynurenine formamidase, but kynurenine aminotransferase
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 2.0 A resolution, comparison with crystallization data from Aspergillus fumigatus, Dictyostelium discoideum, Aedes aegypti, Trypanosoma brucei, Rattus norvegicus, and Homo sapiens
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanizawa, K.; Asada, Y.; Soda, K.
L-Kynurenine transaminase from Hansenula schneggii
Methods Enzymol.
113
90-95
1985
Saccharomyces cerevisiae, Debaryomyces hansenii, Kluyveromyces marxianus, Diutina rugosa, Naganishia albida, Torulaspora globosa, Schwanniomyces polymorphus, Hansenula schneggii, Saccharomyces fragilis, Schwanniomyces occidentalis, Cutaneotrichosporon cutaneum
Manually annotated by BRENDA team
Wogulis, M.; Chew, E.R.; Donohoue, P.D.; Wilson, D.K.
Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence
Biochemistry
47
1608-1621
2008
Saccharomyces cerevisiae (P47039)
Manually annotated by BRENDA team