Adenylyl-sulfate reductase (thioredoxin)

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In enzymology, an adenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.10) is an enzyme that catalyzes the chemical reaction

AMP + sulfite + thioredoxin disulfide $\rightleftharpoons$ 5'-adenylyl sulfate + thioredoxin

The 3 substrates of this enzyme are AMP, 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GOY.

[edit] References

IUBMB entry for 1.8.4.10
BRENDA references for 1.8.4.10 (Recommended.)
PubMed references for 1.8.4.10
PubMed Central references for 1.8.4.10
Google Scholar references for 1.8.4.10
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: 135–42. 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: 5280–7. 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: 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: 27–33. doi:10.1023/A:1007058421714. PMID 10939523.