Adenylyl-sulfate reductase (thioredoxin)
Adenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.10) is an enzyme that catalyzes the chemical reaction
- AMP + sulfite + thioredoxin disulfide 5'-adenylyl sulfate + thioredoxin
| adenylyl-sulfate reductase (thioredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.4.10 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and thioredoxin disulfide, whereas its two products are 5'-adenylyl sulfate and thioredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is AMP, sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). This enzyme is also called thioredoxin-dependent 5'-adenylylsulfate reductase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GOY.
References
- Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T (2000). "Identification of a New Class of 5′-Adenylylsulfate (APS) Reductases from Sulfate-Assimilating Bacteria". J. Bacteriol. 182 (1): 135–42. doi:10.1128/JB.182.1.135-142.2000. PMC 94249. PMID 10613872.
- Abola AP, Willits MG, Wang RC, Long SR (1999). "Reduction of Adenosine-5′-Phosphosulfate Instead of 3′-Phosphoadenosine-5′-Phosphosulfate in Cysteine Biosynthesis by Rhizobium meliloti and Other Members of the Family Rhizobiaceae". J. Bacteriol. 181 (17): 5280–7. doi:10.1128/JB.181.17.5280-5287.1999. PMC 94033. PMID 10464198.
- Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR (2002). "5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria". J. Biol. Chem. 277 (36): 32606–15. doi:10.1074/jbc.M204613200. PMID 12072441.
- Neumann S, Wynen A, Truper HG, Dahl C (2000). "Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway". Mol. Biol. Rep. 27 (1): 27–33. doi:10.1023/A:1007058421714. PMID 10939523. S2CID 6026693.
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