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Literature summary for 2.8.1.11 extracted from
- Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs (2007), FEBS J., 274, 2778-2787.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| phylogenetic analysis | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D417R | site-directed mutagenesis, the kcat of the mutant variant is increased 83fold when dithiothreitol is used as reductant, or 470fold when cyanide is used as sulfur acceptor | Homo sapiens |
| D417T | site-directed mutagenesis, the mutant shows a 17fold increased dithiothreitol:thiosulfate oxidoreductase activity or a 90fold increased thiosulfate:cyanide sulfurtransferase activity | Homo sapiens |
| G415A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
| K413R | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
| L414K | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
| additional information | when the six amino acid active site loop of MOCS3 rhodanese-like domain is exchanged with the loop found in bovine rhodanese, thiosulfate:cyanide sulfurtransferase activity is increased 165fold. By site-directed mutagenesis also the whole loop is exchanged with the one found in bovine rhodanese, which results in a 36fold increase in the kcat with dithiothreitol in the assay mixture and a 165fold increased kcat with cyanide as sulfur acceptor | Homo sapiens |
| N416V | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
| P458G | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
| Y460A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of dithiothreitol:thiosulfate oxidoreductase activity and thiosulfate:cyanide sulfurtransferase activity | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3 | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O95396 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of MOCS2A during Moco biosynthesis in humans. In humans and most eukaryotes thiosulfate is not the physiologic sulfur donor for MOCS3 | Homo sapiens | ? | - |
? | |
| additional information | the MOCS3 rhodanese-like domain, MOCS3-RLD, is also capable to catalyze the transfer of sulfur from thiosulfate to cyanide and shows dithiothreitol:thiosulfate oxidoreductase activity, kinetics, overview | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MOCS3 | - |
Homo sapiens |
| MOCS3 rhodanese-like domain | - |
Homo sapiens |
| MOCS3-RLD | - |
Homo sapiens |
| molybdopterin synthase sulfurase | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | MOCS3 belongs to the class of rhodaneses that is found in combination with another protein domain, and contains one rhodanese domain of 158 amino acids at the C-terminus with a sequence identity of less than 20% with the classic two-domain rhodaneses, phylogenetic analysis of MoeB homologues, overview | Homo sapiens |
| metabolism | the enzyme is involved in the biosynthesis of the molybdenum cofactor divided into three steps: conversion of GTP to precursor, transformation of the precursor to molybdopterin, and insertion of molybdenum into MPT to form the molybdenum cofactor | Homo sapiens |
| additional information | the MOCS3 C-terminal domain is homologous to rhodanese-like proteins. The last amino acid must be either polar or positively charged to increase the thiosulfate sulfurtransferase activity of MOCS3-RLD | Homo sapiens |
| physiological function | molybdopterin synthase sulfurase is involved in sulfur transfer to the C-terminus of the molybdopterin synthase, which synthesizes the molybdenum cofactor, that play a central role in several enzymes, role of specific conserved residues in the six amino acid active site loop of MOCS3-RLD in thiosulfate sulfurtransferase activity | Homo sapiens |
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