E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide

Protein Science

Volumn 10, Issue 11, 2001, Pages 2272-2279

  Boschi Muller, Sandrine ^a   Azza, Saïd ^a   Branlant, Guy ^a  

^a Biopôle de l Université de Lorraine   (France)

Author keywords

Methionine sulfoxide reductase; Sulfenic acid reduction; Thioredoxin; Truncated enzymes

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; CYSTEINE; DISULFIDE; DITHIOTHREITOL; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; MONOMER; OXIDOREDUCTASE; SULFENIC ACID DERIVATIVE; THIOL; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CATALYST; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ESCHERICHIA COLI; KINETICS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN FOLDING; REACTION ANALYSIS; REDUCTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; KINETICS; METHIONINE; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); BOS TAURUS; ESCHERICHIA COLI;

EID: 0034775194     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.10701     Document Type: Article

References (23)

1. Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity
2. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
3. Analysis of the kinetic and redox properties of the NADH peroxidase R303M mutant: Correlation with the crystal structure
4. The minimal gene set member msrA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi
5. In vitro and in vivo oxidation of methionine residues in small, acid-soluble spore proteins from Bacillus species
6. Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)
7. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
8. Reductive half-reaction of thioredoxin reductase from Escherichia coli
9. G33D mutant thioredoxin primarily affects the kinetics of reaction with thioredoxin reductase. Probing the structure of the mutant protein
10. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase
11. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme
12. The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
13. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
14. Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues
15. Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
16. Purification and analysis of streptococcal NADH peroxidase expressed in Escherichia coli
17. The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins
18. Identification of a peptide methionine sulphoxide reductase gene in an oleosin promoter from Brassica napus
19. Measurement of protein by spectrophotometry at 205 nm
20. Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase
21. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 Å resolution
22. Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens
23. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations