Literature summary for 1.8.4.11 extracted from

Olry, A.; Boschi-Muller, S.; Marraud, M.; Sanglier-Cianferani, S.; Van Dorsselear, A.; Branlant, G.
Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis (2002), J. Biol. Chem., 277, 12016-12022.

Search for more literature for 1.8.4.11

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutant enzymes in Escherichia coli	Neisseria meningitidis

Protein Variants

Protein Variants	Comment	Organism
C206S	site-directed mutagenesis, MsrA domain of PILB, inactive mutant	Neisseria meningitidis
C348S	site-directed mutagenesis, MsrA domain of PILB, mutant is inactive with thioredoxin, but about 10fold more active than the wild-type enzyme MsrA domain	Neisseria meningitidis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Neisseria meningitidis
0.075	-	thioredoxin	MsrA activity of PILB, pH 8.0, 25°C	Neisseria meningitidis
9	-	L-methionine (R,S)-sulfoxide	MsrB activity of PILB, pH 8.0, 25°C	Neisseria meningitidis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview	Neisseria meningitidis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
21898	-	x * 21898, about, recombinant MsrA domain, mass spectrometry	Neisseria meningitidis

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	-	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	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	reaction mechanism	Neisseria meningitidis	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3	-	recombinant wild-type MsrA domain, cosubstrate dithiothreitol	Neisseria meningitidis
4.2	-	recombinant wild-type MsrA/MsrB, cosubstrate dithiothreitol	Neisseria meningitidis
170	-	recombinant wild-type MsrA/MsrB, cosubstrate thioredoxin	Neisseria meningitidis
220	-	recombinant wild-type MsrA domain, cosubstrate thioredoxin	Neisseria meningitidis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-methionine (R,S)-sulfoxide + thioredoxin	-	Neisseria meningitidis	L-methionine + thioredoxin disulfide	-	?
L-methionine (S)-sulfoxide + thioredoxin	MsrA activity of the tandem domains of PilB, the MsrA domain alone does not utilize the R-isomer	Neisseria meningitidis	L-methionine + thioredoxin disulfide + H2O	-	?
additional information	substrate specificity of MsrA activity, diverse substrates, overview	Neisseria meningitidis	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 21898, about, recombinant MsrA domain, mass spectrometry	Neisseria meningitidis
More	MsrA activity is located on the central domain of PILB, the fused domains are folded entities	Neisseria meningitidis

Synonyms

Synonyms	Comment	Organism
methionine sulfoxide reductase	-	Neisseria meningitidis
MsrA	-	Neisseria meningitidis
PilB	-	Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
3.7	-	L-methionine (S,R)-sulfoxide	MsrB activity of PILB, pH 8.0, 25°C	Neisseria meningitidis

Cofactor

Cofactor	Comment	Organism	Structure
dithiothreitol	-	Neisseria meningitidis
thioredoxin	-	Neisseria meningitidis

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Release 2023.1 (January 2023)