Literature summary for 1.8.4.12 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 1.8.4.12

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
C439S	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
C494S	site-directed mutagenesis, MsrA domain of PILB, inactive mutant	Neisseria meningitidis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Neisseria meningitidis
0.034	-	thioredoxin	MsrB activity of PILB, pH 8.0, 25°C	Neisseria meningitidis
56	-	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
16374	-	x * 16374, about, recombinant wild-type MsrB 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 (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	reaction mechanism, Cys494 and Cys439 are involved	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 MsrB domain, cosubstrate dithiothreitol	Neisseria meningitidis
4.2	-	recombinant wild-type MsrA/MsrB, cosubstrate dithiothreitol	Neisseria meningitidis
12	-	recombinant wild-type MsrB domain, cosubstrate thioredoxin	Neisseria meningitidis
170	-	recombinant wild-type MsrA/MsrB, cosubstrate thioredoxin	Neisseria meningitidis

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
?	x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry	Neisseria meningitidis
More	MsrB activity is located on the C-terminal domain of PILB, the fused domains are folded entities	Neisseria meningitidis

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.8	-	L-methionine (R,S)-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)