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The expected taxonomic range for this enzyme is: Methanosarcina acetivorans
Synonyms MA_1658 , methanoredoxin, more
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MA_1658
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methanoredoxin
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protein-disulfide + reduced coenzyme M = protein-dithiol + oxidized coenzyme M
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protein-dithiol:coenzyme M oxidoreductase
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insulin disulfide + reduced coenzyme M
insulin dithiol + oxidized coenzyme M
insulin disulfide + reduced glutathione
insulin dithiol + oxidized glutathione
additional information
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insulin disulfide + reduced coenzyme M
insulin dithiol + oxidized coenzyme M
Substrates: - Products: -
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insulin disulfide + reduced coenzyme M
insulin dithiol + oxidized coenzyme M
Substrates: - Products: -
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insulin disulfide + reduced glutathione
insulin dithiol + oxidized glutathione
Substrates: - Products: -
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insulin disulfide + reduced glutathione
insulin dithiol + oxidized glutathione
Substrates: - Products: -
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additional information
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Substrates: no betahydroxyethyl disulfide reductase activity, no dehydroascorbate reductase activity Products: -
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additional information
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Substrates: no betahydroxyethyl disulfide reductase activity, no dehydroascorbate reductase activity Products: -
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coenzyme M
coenzyme M-SH and glutathione bind to the active site
glutathione
coenzyme M-SH and glutathione bind to the active site
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Cd2+
a cadmium ion is found within the active site of each monomer, crystallization data
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2.2
reduced coenzyme M
pH 6.8, temperature not specified in the publication
8.9
reduced glutathione
pH 6.8, temperature not specified in the publication
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Q8TQ93_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
101
0
11465
TrEMBL
Mitochondrion (Reliability: 2 )
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11500
1 * 11500, SDS-PAGE
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monomer
1 * 11500, SDS-PAGE
monomer
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1 * 11500, SDS-PAGE
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structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to glutaredoxins. Active site modeling of coenzyme M shows the sulfate moiety hydrogen-bonded to the backbone amide and carbonyl oxygen of residue Phe 76
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Yenugudhati, D.; Prakash, D.; Kumar, A.K.; Kumar, R.S.; Yennawar, N.H.; Yennawar, H.P.; Ferry, J.G.
Structural and biochemical characterizations of methanoredoxin from Methanosarcina acetivorans, a glutaredoxin-like enzyme with coenzyme M-dependent protein disulfide reductase activity
Biochemistry
55
313-321
2016
Methanosarcina acetivorans (Q8TQ93), Methanosarcina acetivorans DSM 2834 (Q8TQ93)
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