Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis.
about
Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductasesStructural and kinetic analysis of an MsrA-MsrB fusion protein fromStreptococcus pneumoniaeStructural and Biochemical Characterization of Free Methionine-R-sulfoxide Reductase from Neisseria meningitidisPostischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acidsEssential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzaeMethionine sulfoxide reductase from the hyperthermophilic archaeon Thermococcus kodakaraensis, an enzyme designed to function at suboptimal growth temperatures.Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B.Selenocysteine in thiol/disulfide-like exchange reactions.Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensisThe selenoproteome of Clostridium sp. OhILAs: characterization of anaerobic bacterial selenoprotein methionine sulfoxide reductase ABiochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability.Kinetic analysis of the interactions between plant thioredoxin and target proteins.Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases.Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin.Characterization of the amino acids from Neisseria meningitidis MsrA involved in the chemical catalysis of the methionine sulfoxide reduction step.The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases.Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes.Molecular Mechanisms of the Methionine Sulfoxide Reductase System from
P2860
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P2860
Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
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2003年学术文章
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2003年學術文章
@zh-hant
name
Kinetic characterization of th ...... A from Neisseria meningitidis.
@en
Kinetic characterization of th ...... A from Neisseria meningitidis.
@nl
type
label
Kinetic characterization of th ...... A from Neisseria meningitidis.
@en
Kinetic characterization of th ...... A from Neisseria meningitidis.
@nl
prefLabel
Kinetic characterization of th ...... A from Neisseria meningitidis.
@en
Kinetic characterization of th ...... A from Neisseria meningitidis.
@nl
P2093
P2860
P356
P1476
Kinetic characterization of th ...... A from Neisseria meningitidis.
@en
P2093
Guy Branlant
Mathias Antoine
Sandrine Boschi-Muller
P2860
P304
45352-45357
P356
10.1074/JBC.M307471200
P407
P577
2003-09-03T00:00:00Z