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Information on EC 1.8.4.B3 - thioredoxin-independent methionine sulfoxide reductases B for references in articles please use BRENDA:EC1.8.4.B3
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
hmsrb2, hmsrb3, ntmsrb1,
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thioredoxin-independent methionine sulfoxide reductases B
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peptide-L-methionine-(R)-S-sulfoxide + thionein = peptide-L-methionine + thionein disulfide + H2O
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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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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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peptide-L-methionine-(R)-S-sulfoxide + thionein
peptide-L-methionine + thionein disulfide + H2O
A7U630
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SwissProt
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precursor, fragment
SwissProt
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brenda
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brenda
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MSRB3_HUMAN
192
0
20702
Swiss-Prot
MSRB2_HUMAN
182
0
19536
Swiss-Prot
A7U630_TOBAC
195
0
21413
TrEMBL
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15200
x * 15200, calculated from sequence
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?
x * 15200, calculated from sequence
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expression in Escherichia coli BL21
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Sagher, D.; Brunell, D.; Hejtmancik, J.F.; Kantorow, M.; Brot, N.; Weissbach, H.
Thionein can serve as a reducing agent for the methionine sulfoxide reductases
Proc. Natl. Acad. Sci. USA
103
8656-8661
2006
Homo sapiens, Homo sapiens (Q8IXL7), Homo sapiens (Q9Y3D2)
brenda
Ding, D.; Sagher, D.; Laugier, E.; Rey, P.; Weissbach, H.; Zhang, X.H.
Studies on the reducing systems for plant and animal thioredoxin-independent methionine sulfoxide reductases B
Biochem. Biophys. Res. Commun.
361
629-633
2007
Nicotiana tabacum (A7U630), Nicotiana tabacum
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1.8.4.B3 thioredoxin-independent methionine sulfoxide reductases B
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