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Information on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase and Organism(s) Neisseria gonorrhoeae and UniProt Accession P14930
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1.8.4.11 peptide-methionine (S)-S-oxide reductaseIUBMB Comments
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid . On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].
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The taxonomic range for the selected organisms is: Neisseria gonorrhoeae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
methionine sulfoxide reductase a, msra1, msra2, methionine sulfoxide reductases a, msra-1, methionine-s-sulfoxide reductase, peptide methionine sulphoxide reductase, methionine sulphoxide reductase a, peptide methionine sulfoxide reductase a, protein-methionine-s-oxide reductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methionine S-oxide reductase (S-form oxidizing)
-
-
-
-
MsrA/B
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved
SYSTEMATIC NAME
IUBMB Comments
peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (S)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid [9]. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly [9]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrA activity of the tandem domains of PilB, the MsrA domain alone does very poorly utilize the R-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
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enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
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-
?
additional information
?
-
the tandem domains of PilB also posesses MsrB activity utilizing L-methionine (R)-sulfoxide as substrate, the MsrB domain alone does not utilize the S-isomer
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-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
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-
?
additional information
?
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-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
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-
?
additional information
?
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-
the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
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-
?
additional information
?
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the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.083
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (S)-sulfoxide
0.15
purified recombinant MsrA domain alone, substrate L-methionine (S)-sulfoxide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
posesses MsrA and MsrB domains; PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MSRAB_NEIGO
522
0
57959
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
enzyme domain and active site structure, MsrA domain comprises residues 181-362, overview
additional information
-
the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
additional information
-
mutant strains produce a truncated version of fused MsrA/MsrB with increased sensitivity to H2O2 and superoxide anions
additional information
-
mutation of pilB affects the adherence of gonococci to epithelial cells, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wizemann, T.M.; Moskovitz, J.; Pearce, B.J.; Cundell, D.; Arvidson, C.G.; So, M.; Weissbach, H.; Brot, N.; Masure, H.R.
Peptide methionine-sulfoxide reductase contributes to the maintenance of adhesions in three major pathogens
Proc. Natl. Acad. Sci. USA
93
7985-7990
1996
Streptococcus pneumoniae, Escherichia coli, Neisseria gonorrhoeae, Neisseria gonorrhoeae MS11A, Streptococcus pneumoniae R6x
Weissbach, H.; Resnick, L.; Brot, N.
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Biochim. Biophys. Acta
1703
203-212
2005
Bos taurus, Dickeya chrysanthemi, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Neisseria gonorrhoeae, Neisseria meningitidis, Saccharomyces cerevisiae, Streptococcus gordonii, Streptococcus pneumoniae
Ezraty, B.; Aussel, L.; Barras, F.
Methionine sulfoxide reductases in prokaryotes
Biochim. Biophys. Acta
1703
221-229
2005
Aggregatibacter actinomycetemcomitans, Bacillus subtilis, Dickeya chrysanthemi, Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Mycoplasma genitalium, Neisseria gonorrhoeae, Neisseria meningitidis, no activity in Aquifex aeolicus, no activity in Thermotoga maritima, Sinorhizobium meliloti, Staphylococcus aureus, Vibrio cholerae serotype O1
Kauffmann, B.; Aubry, A.; Favier, F.
The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions
Biochim. Biophys. Acta
1703
249-260
2005
Bacillus subtilis, Bos taurus (P54149), Deinococcus radiodurans, Escherichia coli (P0A744), Mycobacterium tuberculosis (P9WJM5), Mycobacterium tuberculosis H37Rv (P9WJM5), Neisseria gonorrhoeae (P14930), Neisseria meningitidis, Solanum lycopersicum
Lowther, W.T.; Weissbach, H.; Etienne, F.; Brot, N.; Matthews, B.W.
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
Nat. Struct. Biol.
9
348-352
2002
Neisseria gonorrhoeae (P14930)
Skaar, E.P.; Tobiason, D.M.; Quick, J.; Judd, R.C.; Weissbach, H.; Etienne, F.; Brot, N.; Seifert, H.S.
The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species
Proc. Natl. Acad. Sci. USA
99
10108-10113
2002
Neisseria gonorrhoeae, Neisseria gonorrhoeae MS11
Kim, H.Y.; Gladyshev, V.N.
Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
Biochem. J.
407
321-329
2007
Bos taurus, Escherichia coli, Homo sapiens, Mycobacterium tuberculosis, Neisseria gonorrhoeae, Neisseria meningitidis, Populus trichocarpa, Mus musculus (Q9D6Y7)
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