4oma

Publication Abstract from PubMed

MGL catalyzes the gamma-elimination of L-methionine and its derivatives as well as the beta-elimination of L-cysteine and its analogs. These reactions yield alpha-keto acids and thiols. The mechanism of chemical conversion of amino acids includes numerous reaction intermediates. The detailed analysis of MGL interaction with glycine, L-alanine, L-norvaline and L-cycloserine was performed by pre-steady-state stopped-flow kinetics. The structure of side chains of the amino acids is important both for their binding with enzyme and for the stability of the external aldimine and ketimine intermediates. X-ray structure of MGL-L-cycloserine complex has been solved at 1.6 A resolution. The structure models ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediates interconversion at the stages of external aldimine and ketimine formation.

Pre-Steady-State Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.,Kuznetsov NA, Faleev NG, Kuznetsova AA, Morozova EA, Revtovich SV, Anufrieva NV, Nikulin AD, Fedorova OS, Demidkina TV J Biol Chem. 2014 Nov 14. pii: jbc.M114.586511. PMID:25398880^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.