Biology:Pyridoxamine-phosphate transaminase
| Pyridoxamine-phosphate transaminase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.6.1.54 | ||||||||
| CAS number | 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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Pyridoxamine-phosphate transaminase (EC 2.6.1.54) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme characterised from Clostridium kainantoi are pyridoxamine phosphate and α-ketoglutaric acid. Its products are pyridoxal phosphate and D-glutamic acid. This is the final step in the biosynthesis of the cofactor, pyridoxal phosphate, in this bacterium.[1]
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.[2]
References
- ↑ "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. 1972. doi:10.1080/00021369.1972.10860239.
- ↑ Enzyme 2.6.1.54 at KEGG Pathway Database.
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