Adenylyl-sulfate reductase (glutathione)
Adenylyl-sulfate reductase (glutathione) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 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 | ||||||||
|
Adenylyl-sulfate reductase (glutathione) (EC 1.8.4.9) is an enzyme that catalyzes the chemical reaction
- AMP + sulfite + glutathione disulfide adenylyl sulfate + 2 glutathione
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.
References
- 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. 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. 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. doi:10.1073/pnas.95.14.8404. PMC 20988. PMID 9653199.