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
| Methionine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
- L-methionine + 2-oxo carboxylate 2-oxo-4-methylthiobutanoate + L-amino acid
The enzyme is most active with L-methionine.
References
edit- ^ Heilbronn J, Wilson J, Berger BJ (March 1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae". Journal of Bacteriology. 181 (6): 1739–47. PMC 93571. PMID 10074065.
- ^ Dolzan M, Johansson K, Roig-Zamboni V, Campanacci V, Tegoni M, Schneider G, Cambillau C (July 2004). "Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function". FEBS Letters. 571 (1–3): 141–6. doi:10.1016/j.febslet.2004.06.075. PMID 15280032.
- ^ Schuster J, Knill T, Reichelt M, Gershenzon J, Binder S (October 2006). "Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis". The Plant Cell. 18 (10): 2664–79. doi:10.1105/tpc.105.039339. PMC 1626624. PMID 17056707.
External links
edit- Methionine+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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