| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.4 With a disulfide as acceptor |
| ID: | 1.8.4.8 |
|---|---|
| Description: | Phosphoadenylyl-sulfate reductase (thioredoxin). |
| Alternative Name: |
Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase. Thioredoxin:3'-phospho-adenylylsulfate reductase. Phosphoadenosine-phosphosulfate reductase. PAPS sulfotransferase. PAPS reductase, thioredoxin-dependent. PAPS reductase. PAdoPS reductase. 3'-phosphoadenylylsulfate reductase. |
| Cath: | 3.40.50.620; |
Click one PDB to see exact 3D structure provided by NGL.
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 1.8.4.8 |
| BRENDA Enzyme Link: | BRENDA 1.8.4.8 |
| KEGG Enzyme Link: | KEGG1.8.4.8 |
| BioCyc Enzyme Link: | BioCyc 1.8.4.8 |
| ExPASy Enzyme Link: | ExPASy1.8.4.8 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.4.8 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.4.8 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.4.8 |
| IntEnz Enzyme Link: | IntEnz 1.8.4.8 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.4.8 |
| RHEA:11724 | [thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2 H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. | Berendt U, Haverkamp T, Prior A, Schwenn JD | 1995 Oct 1 | 7588765 |