Adenylyl-sulfate reductase (glutathione)

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In enzymology, an adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction

AMP + sulfite + glutathione disulfide $\rightleftharpoons$ adenylyl sulfate + 2 glutathione

The 3 substrates of this enzyme are AMP, sulfite, and glutathione disulfide, whereas its two products are adenylyl sulfate and glutathione.

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:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). Other names in common use include 5'-adenylylsulfate reductase (also used for, internal_xref(ec_num(1,8,99,2))), AMP,sulfite:oxidized-glutathione oxidoreductase, (adenosine-5'-phosphosulfate-forming), and plant-type 5'-adenylylsulfate reductase.

[edit] References

IUBMB entry for 1.8.4.9
BRENDA references for 1.8.4.9 (Recommended.)
PubMed references for 1.8.4.9
PubMed Central references for 1.8.4.9
Google Scholar references for 1.8.4.9
Gutierrez-Marcos JF, Roberts MA, Campbell EI, Wray JL (1996). "Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity". Proc. Natl. Acad. Sci. U. S. A. 93: 13377–82. doi:10.1073/pnas.93.23.13377. PMID 8917599.
Setya A, Murillo M, Leustek T (1996). "Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase". Proc. Natl. Acad. Sci. U. S. A. 93: 13383–8. doi:10.1073/pnas.93.23.13383. PMID 8917600.
Bick JA, Aslund F, Chen Y, Leustek T (1998). "Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase". Proc. Natl. Acad. Sci. U. S. A. 95: 8404–9. doi:10.1073/pnas.95.14.8404. PMID 9653199.