| EC |
1.8.4.8 |
| Accepted name: |
phosphoadenylyl-sulfate reductase (thioredoxin) |
| Reaction: |
adenosine 3′,5′-bisphosphate + sulfite + thioredoxin disulfide = 3′-phosphoadenylyl sulfate + thioredoxin |
| Glossary: |
3′-phosphoadenylyl sulfate = PAPS |
| Other name(s): |
PAPS reductase, thioredoxin-dependent; PAPS reductase; thioredoxin:adenosine 3′-phosphate 5′-phosphosulfate reductase; 3′-phosphoadenylylsulfate reductase; thioredoxin:3′-phospho-adenylylsulfate reductase; phosphoadenosine-phosphosulfate reductase; adenosine 3′,5′-bisphosphate,sulfite:oxidized-thioredoxin oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming) |
| Systematic name: |
adenosine 3′,5′-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3′-phosphoadenosine-5′-phosphosulfate-forming) |
| Comments: |
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-63-7 |
| References: |
| 1. |
Berendt, U., Haverkamp, T., Prior, A., Schwenn, J.D. Reaction mechanism of thioredoxin: 3′-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 (1995) 347–356. [DOI] [PMID: 7588765] |
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| [EC 1.8.4.8 created 1999 as EC 1.8.99.4, transferred 2000 to EC 1.8.4.8] |
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