EC Tree |
2. Transferases |
2.8 Transferring sulfur-containing groups |
2.8.1 Sulfurtransferases |
ID: | 2.8.1.9 |
---|---|
Description: | Molybdenum cofactor sulfurtransferase. |
Alternative Name: |
Molybdenum cofactor sulfurase. MoCo sulfurtransferase. MoCo sulfurase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.8.1.9 |
BRENDA Enzyme Link: | BRENDA 2.8.1.9 |
KEGG Enzyme Link: | KEGG2.8.1.9 |
BioCyc Enzyme Link: | BioCyc 2.8.1.9 |
ExPASy Enzyme Link: | ExPASy2.8.1.9 |
EC2PDB Enzyme Link: | EC2PDB 2.8.1.9 |
ExplorEnz Enzyme Link: | ExplorEnz 2.8.1.9 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.8.1.9 |
IntEnz Enzyme Link: | IntEnz 2.8.1.9 |
MEDLINE Enzyme Link: | MEDLINE 2.8.1.9 |
RHEA:42636 | AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + thio-Mo-molybdotperin |
RULE(radius=1) | [*:1]-[CH2;+0:2]-[SH;+0:3].[*:4]-[Mo;H0;+0:5](=[*:6])(-[*:7])=[O;H0;+0:8]>>[*:1]-[CH3;+0:2].[*:4]-[Mo;H0;+0:5](=[*:6])(-[*:7])=[S;H0;+0:3].[OH2;+0:8] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases. | Wahl RC, Warner CK, Finnerty V, Rajagopalan KV | 1982 Apr 10 | 6801056 |
Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. | Wollers S, Heidenreich T, Zarepour M, Zachmann D, Kraft C, Zhao Y, Mendel RR, Bittner F | 2008 Apr 11 | 18258600 |
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. | Heidenreich T, Wollers S, Mendel RR, Bittner F | 2005 Feb 11 | 15561708 |
ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. | Bittner F, Oreb M, Mendel RR | 2001 Nov 2 | 11553608 |