Alliin is a suicide substrate of Citrobacter freundii methionine γ-lyase: structural bases of inactivation of the enzyme

被引：21

作者：

Morozova, Elena A. ^{[1
]}

Revtovich, Svetlana V. ^{[1
]}

Anufrieva, Natalya V. ^{[1
]}

Kulikova, Vitalia V. ^{[1
]}

Nikulin, Alexey D. ^{[2
]}

Demidkina, Tatyana V. ^{[1
]}

机构：

[1] Russian Acad Sci, VA Engelhardt Mol Biol Inst, Moscow 119991, Russia

[2] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Russia

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2014年 / 70卷

基金：

俄罗斯基础研究基金会;

关键词：

CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; ACTIVE-SITE; ALLICIN; IDENTIFICATION; PRINCIPLE; GENE; ELIMINATION; METABOLISM; PARAMETERS;

D O I：

10.1107/S1399004714020938

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom 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.

引用

页码：3034 / 3042

页数：9

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