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Literature summary for 2.8.1.11 extracted from

  • Matthies, A.; Rajagopalan, K.; Mendel, R.; Leimkühler, S.
    Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans (2004), Proc. Natl. Acad. Sci. USA, 101, 5946-5951.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
MOCS3 is encoded by an intronless gene located on chromosome 20, expression of wild-type and mutant tagged MOCS3 rhodanese-like domain, MOCS3-RLD, in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
C316A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Homo sapiens
C324A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Homo sapiens
C365A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Homo sapiens
C412A site-directed mutagenesis, exchange of the conserved active site loop residue, inactive mutant Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O95396
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant tagged wild-type and mutant MOCS3 rhodanese-like domain, MOCS3-RLD, from Escherichia coli strain BL21(DE3) by affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide. Recombinant MOCS3 can activate MOCS2A but not endogenous Escherichia coli MoaD. MOCS3 exhibits sulfurtransferase activity only with thiosulfate, clearly identifying the enzyme as thiosulfate sulfurtransferase. The thiosulfate sulfurtransferase activity of the separated MOCS3-RLD protein is comparable to that of intact MOCS3 Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More the 158 C-terminal amino acids form the MOCS3 rhodanese-like domain, MOCS3-RLD Homo sapiens

Synonyms

Synonyms Comment Organism
MOCS3
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction mutation of the putative persulfide-forming active-site cysteine residue C412 abolishes the sulfurtransferase activity of MOCS3-RLD completely Homo sapiens
physiological function the MOCS3 protein is believed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C terminus of the smaller subunit of molybdopterin (MPT) synthase, the C-terminal segment of MOCS3 displays similarities to the sulfurtransferase rhodanese. The MOCS3 rhodanese-like domain provides the sulfur for the thiocarboxylation of MOCS2A, the small MPT synthase subunit in humans. C412 is important for catalysis. The MoeB domain of MOCS3 is not involved in sulfur transfer in vitro Homo sapiens