Download MendeleyPre-steady-state Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.
Kuznetsov, N.A., Faleev, N.G., Kuznetsova, A.A., Morozova, E.A., Revtovich, S.V., Anufrieva, N.V., Nikulin, A.D., Fedorova, O.S., Demidkina, T.V.(2015) J Biological Chem 290: 671-681
- PubMed: 25398880
- DOI: https://doi.org/10.1074/jbc.M114.586511
- Primary Citation of Related Structures:
4OMA - PubMed Abstract:
Methionine γ-lyase (MGL) catalyzes the γ-elimination of l-methionine and its derivatives as well as the β-elimination of l-cysteine and its analogs. These reactions yield α-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 the MGL·l-cycloserine complex has been solved at 1.6 Å resolution. The structure models the ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediate interconversion at the stages of external aldimine and ketimine formation.
- From the Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk 630090, the Department of Natural Sciences, Novosibirsk State University, Novosibirsk 630090.
Organizational Affiliation:
