pyridoxamine-phosphate transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.54 | ||||||||
CAS no. | 9074-84-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a pyridoxamine-phosphate transaminase (EC 2.6.1.54) is an enzyme that catalyzes the chemical reaction
- pyridoxamine 5'-phosphate + 2-oxoglutarate pyridoxal 5'-phosphate + D-glutamate
Thus, the two substrates of this enzyme are pyridoxamine 5'-phosphate and 2-oxoglutarate, whereas its two products are pyridoxal 5'-phosphate and D-glutamate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is pyridoxamine-5'-phosphate:2-oxoglutarate aminotransferase (D-glutamate-forming). Other names in common use include pyridoxamine phosphate aminotransferase, pyridoxamine 5'-phosphate-alpha-ketoglutarate transaminase, and pyridoxamine 5'-phosphate transaminase. This enzyme participates in vitamin B6 metabolism.
References
- Tani Y, Ukita M, Ogata K (1972). "Studies on vitamin B6 metabolism in microorganisms. Part X. Further purification and characterization of pyridoxamine 5'-phosphate-alpha-ketoglutarate transaminase from Clostridium kainantoi". Agric. Biol. Chem. 36: 181–188. doi:10.1080/00021369.1972.10860239.
Transferase: nitrogenous groups (EC 2.6) | |
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2.6.1: Transaminases | |
2.6.3: Oximinotransferases | |
2.6.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
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