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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,
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aminoadipate aminotransferase
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aminoadipate aminotransferase/kynurenine aminotransferase II
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KAT II/AADAT
bifunctional enzyme with kynurenine aminotransferase activity and aminoadipate aminotransferase function
kynurenine aminotransferase II
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2-aminoadipate aminotransferase
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2-aminoadipic aminotransferase
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alpha-aminoadipate aminotransferase
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glutamate-alpha-ketoadipate transaminase
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glutamic-ketoadipic transaminase
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additional information
KAT II is identical to AADAT (aminoadipate aminotransferase)
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amino group transfer
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L-2-aminoadipate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
kynurenine + 2-oxoglutarate
kynurenic acid + L-glutamate
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ir
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
L-tryptophan + 2-oxoglutarate
3-indole-2-oxopropanoate + L-glutamate
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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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?
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
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?
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
also transamination of methionine, 2-oxocaproic acid, phenylpyruvate and 2-oxo-4-methylthiobutyrate
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?
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
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r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
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r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
lysine catabolic pathway
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r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
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lysine and tryptophan metabolism
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r
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L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
lysine catabolic pathway
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r
L-2-aminoadipate + 2-oxoglutarate
2-oxoadipate + L-glutamate
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lysine and tryptophan metabolism
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r
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1.4
glutamate
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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
1
2-oxoadipate
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pH 8.0, 37°C isoenzyme AadAT-II
2.5
2-oxoadipate
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pH 8.0, 37°C isoenzyme AadAT-I
1.1
2-oxoglutarate
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pH 8.0, 37°C isoenzyme AadAT-I
3.2
2-oxoglutarate
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pH 8.0, 37°C isoenzyme AadAT-II
0.25
L-2-aminoadipate
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pH 8.0, 37°C isoenzyme AadAT-II
20
L-2-aminoadipate
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pH 8.0, 37°C
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10.68
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isoenzyme AadAT-II
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9 - 9.5
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isoenzyme AadAT-II
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SwissProt
brenda
human
SwissProt
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brenda
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brenda
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isoenzyme AadAT-I
brenda
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brenda
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isoenzyme AadAT-II
brenda
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AADAT_HUMAN
425
0
47352
Swiss-Prot
Mitochondrion (Reliability: 3)
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104000
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isoenzyme AadAT-I, sucrose density gradient centrifugation
46000
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2 * 46000, SDS-PAGE
98000
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isoenzyme AadAT-II, sucrose density gradient centrifugation
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dimer
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2 * 46000, SDS-PAGE
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9 - 9.5
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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
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2 isoenzymes, AadAT-I and AadAT-II
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pharmacology
L-alpha-aminoadipate is a component of the precursor to penicillin and cephalosporin
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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
brenda
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)
brenda
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
brenda
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
brenda
2.6.1.39 2-aminoadipate transaminase
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The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
