Methionine transaminase explained

Methionine transaminase
Ec Number:2.6.1.88

Methionine transaminase (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

\rightleftharpoons

2-oxo-4-methylthiobutanoate + L-amino acid

The enzyme is most active with L-methionine.

Notes and References

  1. Heilbronn J, Wilson J, Berger BJ . Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae . Journal of Bacteriology . 181 . 6 . 1739–47 . March 1999 . 10074065 . 93571 .
  2. Dolzan M, Johansson K, Roig-Zamboni V, Campanacci V, Tegoni M, Schneider G, Cambillau C . Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function . FEBS Letters . 571 . 1-3 . 141–6 . July 2004 . 15280032 . 10.1016/j.febslet.2004.06.075 . free .
  3. Schuster J, Knill T, Reichelt M, Gershenzon J, Binder S . 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 . October 2006 . 17056707 . 1626624 . 10.1105/tpc.105.039339 .