Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function.
Reactive oxygen and nitrogen intermediates can cause damage to many cellular components and have been implicated in a number of diseases. Cells have developed a variety of mechanisms to destroy these reactive molecules or repair the damage once it occurs. In proteins one of the amino acids most easily oxidized is methionine, which is converted to methionine sulfoxide. An enzyme, peptide methionine sulfoxide reductase (MsrA), catalyzes the reduction of methionine sulfoxide in proteins back to methionine. There is growing evidence that MsrA plays an important role in protecting cells against oxidative damage. This paper reviews the biochemical properties and biological role of MsrA.
Weissbach
Herbert
H
Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, Florida 33431, USA. hweissba@fau.edu
Etienne
Frantzy
F
Hoshi
Toshinori
T
Heinemann
Stefan H
SH
Lowther
W Todd
WT
Matthews
Brian
B
St  John
Gregory
G
Nathan
Carl
C
Brot
Nathan
N
D000595:Amino Acid Sequence; D008715:Methionine / Q000031:analogs & derivatives* / Q000378:metabolism*; D051150:Methionine Sulfoxide Reductases; D008956:Models, Chemical; D008969:Molecular Sequence Data; D018384:Oxidative Stress / Q000502:physiology*; D010088:Oxidoreductases / Q000378:metabolism*
D008715:Methionine; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; C013111:methionine sulfoxide