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Literature summary extracted from

  • Tang, H.; Rothery, R.A.; Voss, J.E.; Weiner, J.H.
    Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion (2011), J. Biol. Chem., 286, 15147-15154.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.8.5.3 DELTAN21 mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled Escherichia coli
1.8.5.3 R61K molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity Escherichia coli
1.8.5.3 V20Y/DELTAN21/P27G introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR Escherichia coli
1.8.5.3 V20Y/DELTAN21/P27G/R61K addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.8.5.3 Escherichia coli P18775
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.5.3 0.07
-
 mutant DELTAN21, cosubstrate lapachol, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 0.14
-
 mutant V20Y/DELTAN21/P27G, cosubstrate lapachol, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 0.33
-
 mutant V20Y/DELTAN21/P27G/R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 2.63
-
 mutant R61K, cosubstrate lapachol, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 5.22
-
 mutant V20Y/DELTAN21/P27G, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 5.91
-
 mutant DELTAN21, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 7.72
-
 wild-type, cosubstrate lapachol, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 7.97
-
 mutant V20Y/DELTAN21/P27G/R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 125
-
 mutant R61K, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication Escherichia coli
1.8.5.3 141
-
 wild-type, cosubstrate benzyl viologen, pH 7.0, temperature not specified in the publication Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.5.3 trimethylamine N-oxide + reduced benzyl viologen
-
 Escherichia coli trimethylamine + oxidized benzyl viologen
-
 ?
1.8.5.3 trimethylamine N-oxide + reduced lapachol
-
 Escherichia coli trimethylamine + oxidized lapachol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.5.3 DmsABC
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.5.3 [4Fe-4S]-center role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. The cluster is predicted to be in close proximity to the molybdo-bis(pyranopterin guanine dinucleotide) cofactor, which provides the site of dimethyl sulfoxide reduction Escherichia coli