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Publication Abstract from PubMed

The interaction of Citrobacter freundii methionine gamma-lyase (MGL) and the mutant form in which Cys115 is replaced by Ala (MGL C115A) with the nonprotein amino acid (2R)-2-amino-3-[(S)-prop-2-enylsulfinyl]propanoic acid (alliin) was investigated. It was found that MGL catalyzes the beta-elimination reaction of alliin to form 2-propenethiosulfinate (allicin), pyruvate and ammonia. The beta-elimination reaction of alliin is followed by the inactivation and modification of SH groups of the wild-type and mutant enzymes. Three-dimensional structures of inactivated wild-type MGL (iMGL wild type) and a C115A mutant form (iMGL C115A) were determined at 1.85 and 1.45 A resolution and allowed the identification of the SH groups that were oxidized by allicin. On this basis, the mechanism of the inactivation of MGL by alliin, a new suicide substrate of MGL, is proposed.

Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.,Morozova EA, Revtovich SV, Anufrieva NV, Kulikova VV, Nikulin AD, Demidkina TV Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3034-42. doi:, 10.1107/S1399004714020938. Epub 2014 Oct 29. PMID:25372692^[1]

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