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2.6.1.1 |
| Description |
Aspartate aminotransferase |
| Alternative names |
Transaminase A;
Glutamic--oxaloacetic transaminase;
Glutamic--aspartic transaminase;
AspAT;
GOT. |
| Catalyzed reaction |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. This activity can be formed from EC 2.6.1.57 by controlled proteolysis. |
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Subfamily a includes eukariotic enzymes (both cytosolic and organellar).
Subfamily b encompasses proteins from gram-positive bacteria and from archaea.
Subfamily c is a compact subgroup including the E. coli AAT and other enzymes from proteobacteria.
Subfamily d represents a very distinct subgroup of bacterial enzymes based on the functionally validated sequence from Corynebacterium glutamicum.
Subfamily e is yet another very distinct group, including enzymes from thermophilic Archaea and from Eubacteria.
Subfamily f (distantly related to subfamily b) is based on a very divergent sequence from Bacillus. |
| Prosite |
PROSITE; PDOC00098; |
| PDB |
1AAT; 1AAW; 1ASL; 1ARG; 1ARS; 1CQ6; 7AAT; 1J32; 1YAA; 3MEB; 5IWQ; 5C6U; 3HLM; 2X5F; |
| Organisms |
-Eubacteria -Archea -Plants -Fungi -Metazoa -Human |
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| Links |
Enzyme (activities) 2.6.1.1
BRENDA (activities) 2.6.1.1
KEGG (pathways) 2.6.1.1
PLPMDB (PLP mutants) 2.6.1.1
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| References |
Articles on 2.6.1.1 |
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| last changed |
2020/03/01 19:52 |
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