Oxidation of Cysteine 645 of Cobalamin-Independent Methionine Synthase Causes a Methionine Limitation in Escherichia coli | Zendy

Elise R. Hondorp | Zendy; Rowena G. Matthews | Zendy

Open Access

Oxidation of Cysteine 645 of Cobalamin-Independent Methionine Synthase Causes a Methionine Limitation in Escherichia coli

Author(s) -

Elise R. Hondorp,

Rowena G. Matthews

Publication year - 2009

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.01722-08

Subject(s) - methionine , methionine synthase , cysteine , auxotrophy , biology , cobalamin , escherichia coli , biochemistry , alanine , biosynthesis , amino acid , enzyme , gene , vitamin b12

Cobalamin-independent methionine synthase (MetE) catalyzes the final step in Escherichia coli methionine biosynthesis but is inactivated under oxidative conditions, triggering a methionine deficiency. This study demonstrates that the mutation of MetE cysteine 645 to alanine completely eliminates the methionine auxotrophy imposed by diamide treatment, suggesting that modulation of MetE activity via cysteine 645 oxidation has significant physiological consequences for oxidatively stressed cells.

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