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Information on EC 2.6.1.39 - 2-aminoadipate transaminase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.39 2-aminoadipate transaminase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-aminoadipate aminotransferase, aaa-at, 2-aminoadipate aminotransferase, glutamate-alpha-ketoadipate transaminase, kat ii/aadat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-aminoadipate aminotransferase
-
-
-
-
2-aminoadipic aminotransferase
-
-
-
-
AadAT
alpha-aminoadipate aminotransferase
-
-
-
-
aminoadipate aminotransferase
-
aminoadipate aminotransferase/kynurenine aminotransferase II
-
glutamate-alpha-ketoadipate transaminase
-
-
-
-
glutamic-ketoadipic transaminase
-
-
-
-
KAT II/AADAT
bifunctional enzyme with kynurenine aminotransferase activity and aminoadipate aminotransferase function
kynurenine aminotransferase II
-
additional information
KAT II is identical to AADAT (aminoadipate aminotransferase)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-00-5
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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
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
show the reaction diagram
-
-
-
-
ir
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
show the reaction diagram
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-
-
-
?
additional information
?
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-
2 isoenzymes, AadAT-I and AadAT-II, isoenzyme AadAT-II shows additional activity with tryptophan or kynurenine-2-oxoglutarate reaction, only slight activity with asparagine, alanine, arginine, ornithine, isoleucine, valine, leucine, lysine, serine, threonine, phenylalanine, tyrosine, histidine, glutamine, methionine or aspartate with 2-oxoglutarate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 2.5
2-oxoadipate
1.1 - 3.2
2-oxoglutarate
1.4
glutamate
-
pH 8.0, 37°C
0.25 - 20
L-2-aminoadipate
12.5
L-glutamate
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pH 8.0, 37°C, isoenzyme AadAT-II
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.77
-
isoenzyme AadAT-I
10.68
-
isoenzyme AadAT-II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
-
isoenzyme AadAT-II
9.5
-
isoenzyme AadAT-I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AADAT_HUMAN
425
0
47352
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
-
isoenzyme AadAT-I, sucrose density gradient centrifugation
46000
-
2 * 46000, SDS-PAGE
50800
cDNA analysis
98000
-
isoenzyme AadAT-II, sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 46000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
-
isoenzyme AadAT-I, sensitive to pH changes, activity is quickly lost at a higher pH, isoenzyme AadAT-II is less sensitive to pH changes
639983
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes, AadAT-I and AadAT-II
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AADAT sequenced
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
L-alpha-aminoadipate is a component of the precursor to penicillin and cephalosporin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuno, E.; Tsujimoto, M.; Nakamura, M.; Kido, R.
2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human liver: a plausible physiological role in lysine and tryptophan metabolism
Enzyme Protein
47
136-148
1993
Homo sapiens
Manually annotated by BRENDA team
Goh, D.L.; Patel, A.; Thomas, G.H.; Salomons, G.S.; Schor, D.S.; Jakobs, C.; Geraghty, M.T.
Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)
Mol. Genet. Metab.
76
172-180
2002
Homo sapiens, Homo sapiens (Q8N5Z0)
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.A.; Robinson, H.; Li, J.
Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
Biosci. Rep.
28
205-215
2008
Homo sapiens (Q8N5Z0), Homo sapiens
Manually annotated by BRENDA team
Han, Q.; Cai, T.; Tagle, D.A.; Li, J.
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
Cell. Mol. Life Sci.
67
353-368
2010
Homo sapiens (Q8N5Z0), Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team