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Enzyme Nomenclature
Information on EC 1.8.4.B3 - thioredoxin-independent methionine sulfoxide reductases B
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.8.4.B3
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
thioredoxin-independent methionine sulfoxide reductases B
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine-(R)-S-sulfoxide + thionein = peptide-L-methionine + thionein disulfide + H2O
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
dabsyl-L-methionine (R)-S-sulfoxide + bovine liver thionein
dabsyl-L-methionine + bovine liver thionein + H2O
NtMsrB1
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-
?
dabsyl-L-methionine (R)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
NtMsrB1
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-
?
dabsyl-L-methionine (R)-S-sulfoxide + plant Trx-like protein CDSP32
dabsyl-L-methionine + ?
NtMsrB1
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-
?
dabsyl-L-methionine (R)-S-sulfoxide + selenocysteamine
dabsyl-L-methionine + 2,2'-disulfanediyldiethanamine + H2O
NtMsrB1
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-
?
L-methionine (R)-S-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
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-
-
?
L-methionine (R)-S-sulfoxide + thionein
L-methionine + thionein disulfide + H2O
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-
-
?
L-methionine (R)-S-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
reduced thioredoxin is not an efficient reducing agent for hMsrB3. Less than 5% of the activity with dithiothreitol
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-
?
L-methionine (R)-S-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
reduced thioredoxin is not an efficient reducing agent for hMsrB2. Less than 5% of the activity with dithiothreitol
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-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
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-
-
?
peptide-L-methionine-(R)-S-sulfoxide + thionein
peptide-L-methionine + thionein disulfide + H2O
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-
-
?
additional information
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zinc-containing metallothionein in the presence of EDTA can serve as a reducing agent. Thioredoxin can reduce oxidized thionein
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additional information
?
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zinc-containing metallothionein in the presence of EDTA can serve as a reducing agent. Thioredoxin can reduce oxidized thionein
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additional information
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NtMsrB1 shows very little activity towards L-methionine (R)-sulfoxide. Escherichia coli thioredoxin can not serve as a reducing agent for NtMsrB1. The Trx-independent MsrB enzyme lacks an additional cysteine (resolving cysteine) that is capable of forming a disulfide bond on the enzyme during the catalytic reaction
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additional information
?
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NtMsrB1 shows very little activity towards L-methionine (R)-sulfoxide. Escherichia coli thioredoxin can not serve as a reducing agent for NtMsrB1. The Trx-independent MsrB enzyme lacks an additional cysteine (resolving cysteine) that is capable of forming a disulfide bond on the enzyme during the catalytic reaction
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
peptide-L-methionine-(R)-S-sulfoxide + thionein
peptide-L-methionine + thionein disulfide + H2O
A7U630
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?
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.4.B3)
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