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Literature summary for 1.8.5.3 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

Protein Variants Comment Organism
DELTAN21 mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled Escherichia coli
R61K molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity Escherichia coli
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
V20Y/DELTAN21/P27G/R61K addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P18775
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DmsABC
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
[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