kynurenine/alpha-aminoadipate aminotransferase, mitochondrial; KAT/AadAT; 2-aminoadipate aminotransferase; 2-aminoadipate transaminase; alpha-aminoadipate aminotransferase; AadAT; kynurenine aminotransferase 2; kynurenine-oxoglutarate transaminase 2 (AADAT, KAT2)
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Function
- lysine degradation via saccharopine pathway
- glutaryl-CoA from L-lysine: step 4/6
- converts L-kynurenine to 4-(2-aminophenyl)-2,4-dioxobutanoate
- converts L-2-aminoadipate to 2-oxoadipate
- also shows activity also towards tryptophan, aspartate & hydroxykinurenine
- homodimer
,L-kynurenine + 2-oxoglutarate <--> 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-2-aminoadipate + 2-oxoglutarate <--> 2-oxoadipate + L-glutamate
Inhibition:
- kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine & phenylalanine
- KM=0.9 mM for aminoadipate
- KM=4.7 mM for kynurenine
- KM=1.7 mM for methionine
- KM=1.6 mM for glutamate
- KM=1.8 mM for tyrosine
- KM=1.2 mM for 2-oxoglutarate
- KM=1.5 mM for 2-oxocaproic acid
- KM=1.8 mM for phenylpyruvate
- KM=1.4 mM for ino-3-pyruvate
- pH dependence: optimum pH is 7-9
- temperature dependence:
- optimum temperature is 50 degrees celsius
Structure
- homodimer
- belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family
Compartment
Alternative splicing
named isoforms=2