Aminolevulinate transaminase
aminolevulinate transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.43 | ||||||||
CAS no. | 9012-46-8 | ||||||||
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, an aminolevulinate transaminase (EC 2.6.1.43) is an enzyme that catalyzes the chemical reaction
- 5-aminolevulinate + pyruvate 4,5-dioxopentanoate + L-alanine
Thus, the two substrates of this enzyme are 5-aminolevulinate and pyruvate, whereas its two products are 4,5-dioxopentanoate and L-alanine.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 5-aminolevulinate:pyruvate aminotransferase. Other names in common use include aminolevulinate aminotransferase, gamma,delta-dioxovalerate, aminotransferase, gamma,delta-dioxovaleric acid transaminase, 4,5-dioxovalerate aminotransferase, 4,5-dioxovaleric acid transaminase, 4,5-dioxovaleric transaminase, 5-aminolevulinic acid transaminase, alanine-gamma,delta-dioxovalerate aminotransferase, alanine-dioxovalerate aminotransferase, alanine:4,5-dioxovalerate aminotransferase, aminolevulinic acid transaminase, dioxovalerate transaminase, L-alanine-4,5-dioxovalerate aminotransferase, L-alanine:4,5-dioxovaleric acid transaminase, L-alanine:dioxovalerate transaminase, DOVA transaminase, and 4,5-dioxovaleric acid aminotransferase. This enzyme participates in porphyrin and chlorophyll metabolism. It employs one cofactor, pyridoxal phosphate.
References
- Gibson KD, Matthew M, Neuberger A (1961). "Biosynthesis of porphyrins and chlorophylls". Nature. 192 (4799): 204–208. Bibcode:1961Natur.192..204G. doi:10.1038/192204a0. PMID 13898421. S2CID 41389926.
- Neuberger A, Turner JM (1963). "gamma,delta-Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides". Biochimica et Biophysica Acta. 67: 342–5. doi:10.1016/0006-3002(63)91839-0. PMID 13938132.