|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: methionine transaminase
Enzyme Commission Synonyms: methionine-oxo-acid transaminase
Enzyme Commission Summary:
The enzyme is most active with L-methionine. It participates in the L-methionine salvage pathway from S-methyl-5'-thioadenosine, a by-product of polyamine biosynthesis. The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective [Heilbronn99]. The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates [Schuster06].
Dolzan04: 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(1-3);141-6. PMID: 15280032
Heilbronn99: Heilbronn J, Wilson J, Berger BJ (1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae." J Bacteriol 1999;181(6);1739-47. PMID: 10074065
Schuster06: 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(10);2664-79. PMID: 17056707
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493