The methionine sulfoxide reductases: Catalysis and substrate specificities

Oxidation of Met residues in proteins leads to the formation of methionine sulfoxides (MetSO). Methionine sulfoxide reductases (Msr) are ubiquitous enzymes, which catalyze the reduction of the sulfoxide function of the oxidized methionine residues. In vivo, the role of Msrs is described as essential...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2008-06, Vol.474 (2), p.266-273
Main Authors: Boschi-Muller, Sandrine, Gand, Adeline, Branlant, Guy
Format: Article
Language:English
Subjects:
Acid/base catalyst
Animals
Biochemistry
Biochemistry, Molecular Biology
Catalysis
Cattle
Chemical catalysis
Cysteine - metabolism
DsbE
Escherichia coli - enzymology
Hydrophobic pocket
Kinetics
Life Sciences
Methionine - analogs & derivatives
Methionine - metabolism
Methionine Sulfoxide Reductases
Msr
Mycobacterium tuberculosis - enzymology
Neisseria - enzymology
Oxidoreductases - chemistry
Oxidoreductases - metabolism
Populus - enzymology
Substrate Specificity
Sulfenic acid
Sulfhydryl Compounds - metabolism
Sulfoxide
Thiol activation
Thioredoxin
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Summary:Oxidation of Met residues in proteins leads to the formation of methionine sulfoxides (MetSO). Methionine sulfoxide reductases (Msr) are ubiquitous enzymes, which catalyze the reduction of the sulfoxide function of the oxidized methionine residues. In vivo, the role of Msrs is described as essential in protecting cells against oxidative damages and to play a role in infection of cells by pathogenic bacteria. There exist two structurally-unrelated classes of Msrs, called MsrA and MsrB, with opposite stereoselectivity towards the S and R isomers of the sulfoxide function, respectively. Both Msrs present a similar three-step catalytic mechanism. The first step, called the reductase step, leads to the formation of a sulfenic acid on the catalytic Cys with the concomitant release of Met. In recent years, significant efforts have been made to characterize structural and molecular factors involved in the catalysis, in particular of the reductase step, and in structural specificities.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2008.02.007