MG_408_MONOMER – methionine-S-sulfoxide reductase

Name
WID MG_408_MONOMER View in model
Name methionine-S-sulfoxide reductase View in model
Cross references PDB: 2IEM
 
Genetics
Gene MG_408 View in model
 
Structure
Sequence
1
51
101
151
MKEIYFGGGCFWGIEKYFQLIKGVKKTSVGYLNSRIRNPSYEQVCSGYTN
AVEAVKVEYEEKEISLSELIEALFEVIDPTIRNRQGNDIGTQYRTGIYWT
DSSDEKIINDKFLKLQKNYSKPIVTENKKVENYYLAEEYHQDYLKKNPNG
YCHIKFD*
50
100
150
158
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H1271C835N212O251S4
Molecular weight (pH 7.5; Da) 18423.51 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
32235
Instability index 26.19
Is stable True
Aliphatic index 75.82
GRAVY (25C, pH 7.0) -0.694
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Function
Enzyme L-methionine-S-sulfoxide reductase
[c]: H2O + MET + MG_124_MONOMER_oxMETSOXSL + MG_124_MONOMER
View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0130, PUB_0131]. Coenzymes Monomer interacts with thioredoxin with unknown stoichiometry as coenzyme [131].
References
  1. Boschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, Branlant G. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem 275, 35908-13 (2000). WholeCell: PUB_0130, PubMed: 10964927

  2. Boschi-Muller S, Olry A, Antoine M, Branlant G. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim Biophys Acta 1703, 231-8 (2005). WholeCell: PUB_0131, PubMed: 15680231

 
Metadata
Created 2012-10-01 15:08:02
Last updated 2012-10-01 15:14:48