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 |
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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 |
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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 |