Function and Biology

The crystal structure of human kynurenine aminotransferase II

Source organism: Homo sapiens
Biochemical function: methionine-glyoxylate transaminase activity
Biological process: alpha-amino acid metabolic process
Cellular component: mitochondrial matrix

EC 2.6.1.63: Kynurenine--glyoxylate transaminase

Reaction catalysed:
(1a) L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
Systematic name:
L-kynurenine:glyoxylate aminotransferase (cyclizing)
Alternative Name(s):
  • Kynurenine--glyoxylate aminotransferase

EC 2.6.1.7: Kynurenine--oxoglutarate transaminase

Reaction catalysed:
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
Systematic name:
L-kynurenine:2-oxoglutarate aminotransferase
Alternative Name(s):
  • Kynurenine 2-oxoglutarate transaminase
  • Kynurenine aminotransferase
  • Kynurenine transaminase (cyclizing)
  • Kynurenine--oxoglutarate aminotransferase
  • L-kynurenine aminotransferase

EC 2.6.1.73: Methionine--glyoxylate transaminase

Reaction catalysed:
L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine
Systematic name:
L-methionine:glyoxylate aminotransferase
Alternative Name(s):
  • MGAT
  • Methionine--glyoxylate aminotransferase

EC 2.6.1.4: Glycine transaminase

Reaction catalysed:
Glycine + 2-oxoglutarate = glyoxylate + L-glutamate
Systematic name:
Glycine:2-oxoglutarate aminotransferase
Alternative Name(s):
  • Glutamic--glyoxylic transaminase
  • Glycine aminotransferase
  • Glyoxylate--glutamate aminotransferase
  • Glyoxylate--glutamic transaminase
  • L-glutamate:glyoxylate aminotransferase

EC 2.6.1.39: 2-aminoadipate transaminase

Reaction catalysed:
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Systematic name:
L-2-aminoadipate:2-oxoglutarate aminotransferase
Alternative Name(s):
  • 2-aminoadipate aminotransferase
  • 2-aminoadipic aminotransferase
  • Alpha-aminoadipate aminotransferase
  • Glutamate--alpha-ketoadipate transaminase
  • Glutamic--ketoadipic transaminase

Sequence family

Pfam Protein family (Pfam)
PF00155
Domain description: Aminotransferase class I and II
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
The deposited structure of PDB entry 5efs contains 1 copy of Pfam domain PF00155 (Aminotransferase class I and II) in Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR004839
Domain description: Aminotransferase, class I/classII
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
IPR015424
Domain description: Pyridoxal phosphate-dependent transferase
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
IPR015421
Domain description: Pyridoxal phosphate-dependent transferase, major domain
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Structure domains

CATH CATH domains
3.90.1150.10
Class: Alpha Beta
Architecture: Alpha-Beta Complex
Topology: Aspartate Aminotransferase, domain 1
Homology: Aspartate Aminotransferase, domain 1
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
The deposited structure of PDB entry 5efs contains 1 copy of CATH domain 3.90.1150.10 (Aspartate Aminotransferase, domain 1) in Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial. Showing 1 copy in chain A.
3.40.640.10
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Aspartate Aminotransferase; domain 2
Homology: Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Occurring in:
  1. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
The deposited structure of PDB entry 5efs contains 1 copy of CATH domain 3.40.640.10 (Aspartate Aminotransferase; domain 2) in Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial. Showing 1 copy in chain A.