@article{ref1,
title="Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine γ-lyase. Structural bases of the enzyme inactivation",
journal="Biochimie",
year="2020",
author="Revtovich, Svetlana and Morozova, Elena and Kulikova, Vitalia and Koval, Vasiliy and Anufrieva, Natalya and Nikulin, Alexei and Demidkina, Tatyana",
volume="168",
number="",
pages="190-197",
abstract="Interactions of Citrobacter freundii methionine γ-lyase (MGL) with sulfoxides of typical substrates were investigated. It was found that sulfoxides are suicide substrates of the enzyme. The products of the β- and γ-elimination reactions of sulfoxides, thiosulfinates, oxidize three cysteine residues of the enzyme. Three-dimensional structures of MGL inactivated by dimethyl thiosulfinate and diethyl thiosulfinate were determined at 1.46 Å and 1.59 Å resolution. Analysis of the structures identified SH groups oxidized by thiosulfinates and revealed the structural bases of MGL inactivation. The extent of inactivation of MGL in the catalysis of the β-elimination reaction depends on the length of the &quot;tail&quot; at oxidized Cys115. Oxidation of Cys115 results in MGL incapable to catalyze the stage of methyl mercaptan elimination of the physiological reaction.<p /><p>Language: en</p>",
language="en",
issn="0300-9084",
doi="10.1016/j.biochi.2019.11.004",
url="http://dx.doi.org/10.1016/j.biochi.2019.11.004"
}