Methionine transaminase
| Methionine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.88 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Methionine transaminase (EC 2.6.1.88, methionine-oxo-acid transaminase) is an enzyme with systematic name L-methionine:2-oxo-acid aminotransferase.[1][2][3] This enzyme catalyses the following chemical reaction
- L-methionine + 2-oxo carboxylate 2-oxo-4-methylthiobutanoate + L-amino acid
The enzyme is most active with L-methionine.
References
- ↑ Heilbronn, J.; Wilson, J.; Berger, B.J. (1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae". J. Bacteriol. 181: 1739–1747. PMID 10074065.
- ↑ Dolzan, M.; Johansson, K.; Roig-Zamboni, V.; Campanacci, V.; Tegoni, M.; Schneider, G.; Cambillau, C. (2004). "Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function". FEBS Lett. 571: 141–146. doi:10.1016/j.febslet.2004.06.075. PMID 15280032.
- ↑ Schuster, J.; Knill, T.; Reichelt, M.; Gershenzon, J.; Binder, S. (2006). "Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis". Plant Cell. 18: 2664–2679. doi:10.1105/tpc.105.039339. PMID 17056707.
External links
- Methionine transaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
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