Adenylyl-sulfate reductase (glutathione)

Adenylyl-sulfate reductase (glutathione)^[1] (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction

AMP + sulfite + glutathione disulfide ${\displaystyle \rightleftharpoons }$ adenylyl sulfate + 2 glutathione

Adenylyl-sulfate reductase (glutathione)
Identifiers
EC no.	1.8.4.9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

The 3 substrates of this enzyme are adenosine monophosphate, 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. In plants, APS is reduced by the plastidic enzyme APS reductase (APR; EC 1.8.4.9) in the presence of physiological concentrations of reduced glutathione (GSH), which acts as an electron donor.^[1][2]

References

1. Brychkova, Galina; Yarmolinsky, Dmitry; Sagi, Moshe (September 2012). "Kinetic assays for determining in vitro APS reductase activity in plants without the use of radioactive substances". Plant & Cell Physiology. 53 (9): 1648–1658. doi:10.1093/pcp/pcs091. ISSN 1471-9053. PMID 22833665.
2. Bick, J. A.; Leustek, T. (June 1998). "Plant sulfur metabolism--the reduction of sulfate to sulfite". Current Opinion in Plant Biology. 1 (3): 240–244. doi:10.1016/s1369-5266(98)80111-8. ISSN 1369-5266. PMID 10066588.

• 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 (23): 13377–82. Bibcode:1996PNAS...9313377G. doi:10.1073/pnas.93.23.13377. PMC 24101. 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 (23): 13383–8. Bibcode:1996PNAS...9313383S. doi:10.1073/pnas.93.23.13383. PMC 24102. 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 (14): 8404–9. Bibcode:1998PNAS...95.8404B. doi:10.1073/pnas.95.14.8404. PMC 20988. PMID 9653199.