AADAT - Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial - human protein (Function)
 
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AADAT »  Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial  (KAT/AadAT)
 
Protein also known as:  Kynurenine--oxoglutarate aminotransferase II.
Gene name:  AADAT
Entry whose protein(s) existence is based on evidence at protein level
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GENE REF ISO

Function

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Overview 
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).  
2
  • UniProtKB
GO molecular function 
2-aminoadipate transaminase activitydefinition[GO:0047536]  
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  • UniProtKB
Kynurenine-oxoglutarate transaminase activitydefinition[GO:0016212]  
1
  • UniProtKB
Protein homodimerization activitydefinition[GO:0042803]  
1
  • UniProtKB
Pyridoxal phosphate bindingdefinition[GO:0030170] silver  
1
  • InterPro 2 GO
GO biological process 
2-oxoglutarate metabolic processdefinition[GO:0006103]  
1
  • UniProtKB
Biosynthetic processdefinition[GO:0009058] silver  
1
  • InterPro 2 GO
Glutamate metabolic processdefinition[GO:0006536]  
1
  • UniProtKB
Kynurenine metabolic processdefinition[GO:0070189]  
1
  • UniProtKB
L-kynurenine metabolic processdefinition[GO:0097052]  
2
  • GOC
  • EC 2 GO
L-lysine catabolic process to acetyl-CoA via saccharopinedefinition[GO:0033512]  
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  • UniPathway
Tryptophan catabolic process to kynureninedefinition[GO:0019441] silver  
1
  • Ortholog Compara
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reactions
EC 2.6.1.7: L-kynurenine + 2-oxoglutarate 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.  
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  • UniProtKB
EC 2.6.1.39: L-2-aminoadipate + 2-oxoglutarate 2-oxoadipate + L-glutamate.  
1
  • UniProtKB
It requires the following cofactor
 pyridoxal 5'-phosphate  
4
  • UniProtKB
It is regulated in the following manner
Kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine and phenylalanine.  
2
  • UniProtKB
 
More information is available from:
Pathways 
This protein is involved in the following pathway
Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6  
1
  • UniProtKB
According to KEGG, this protein belongs to the following pathways:
Lysine biosynthesis  hsa00300+51166  
Lysine degradation  hsa00310+51166  
Metabolic pathways  hsa01100+51166  
Tryptophan metabolism  hsa00380+51166  
According to Reactome, this protein belongs to the following pathways:
Lysine catabolism  REACT_1298  
Tryptophan catabolism  REACT_916  
 
More information is available from:
 

Biophysicochemical properties

Kinetic parameters
KM 1.7 mM for methionine
KM 1.2 mM for 2-oxoglutarate
KM 1.4 mM for ino-3-pyruvate
KM 4.7 mM for kynurenine
KM 1.8 mM for tyrosine
KM 1.8 mM for phenylpyruvate
KM 0.9 mM for aminoadipate
KM 1.5 mM for 2-oxocaproic acid
KM 1.6 mM for glutamate
Dependence
pH Optimum pH is 7-9.
Temperature Optimum temperature is 50 degrees Celsius.

Keywords

Molecular function 
Aminotransferase  definition   [KW-0032]
Transferase  definition   [KW-0808]
Technical term 
Reference proteome  definition   [KW-1185]
 

Further external links

GenomeRNAi: 51166
PRO: PR:Q8N5Z0