Any feedback?
Literature summary for 2.7.7.80 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the MOCS3 MoeB-like domain MOCS3-MoeBD in a Esccherichia coli MoeB-deficient strain moeB- (DE3) | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C239A | the MOCS3 N-terminal domain mutant shows 81% reduced MoeB-like activity compared to wild-type MOCS3, the cysteine 293 residue in the MOCS3-MoeB domain is involved in the sulfur transfer reaction of MOCS3, EC 2.8.1.11 | Homo sapiens |
| additional information | the human MOCS3-MoeB domain can be functionally substituted by Escherichia coli MoeB protein | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O95396 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MOCS3 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 N-terminal MOCS3 MoeB-like domain, i.e. MOCS3-MoeBD, is similar to the Escherichia coli MoeB protein | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
