EC number:1.8.4.9
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.4 With a disulfide as acceptor |
| ID: | 1.8.4.9 |
|---|---|
| Description: | Adenylyl-sulfate reductase (glutathione). |
| Alternative Name: |
Plant-type 5'-adenylylsulfate reductase. 5'-phosphosulfate-forming). AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine- 5'-adenylylsulfate reductase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.4.9 |
| BRENDA Enzyme Link: | BRENDA 1.8.4.9 |
| KEGG Enzyme Link: | KEGG1.8.4.9 |
| BioCyc Enzyme Link: | BioCyc 1.8.4.9 |
| ExPASy Enzyme Link: | ExPASy1.8.4.9 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.4.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.4.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.4.9 |
| IntEnz Enzyme Link: | IntEnz 1.8.4.9 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.4.9 |
| RHEA:14141 | AMP + glutathione disulfide + 2 H(+) + sulfite = adenosine 5'-phosphosulfate + 2 glutathione |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S;H0;+0:4]-[S;H0;+0:5]-[*:6].[*:7]=[S;H0;+0:8](-[*:9])-[OH;+0:10].[H+;H0:11].[H+;H0:12]>>[*:1]-[O;H0;+0:2]-[S;H0;+0:8](=[*:7])(-[*:9])=[O;H0;+0:10].[*:3]-[SH;+0:4].[*:6]-[SH;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase. | Bick JA, Aslund F, Chen Y, Leustek T | 1998 Jul 7 | 9653199 |
| Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase. | Setya A, Murillo M, Leustek T | 1996 Nov 12 | 8917600 |
| Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity. | Gutierrez-Marcos JF, Roberts MA, Campbell EI, Wray JL | 1996 Nov 12 | 8917599 |