EC - Adenylyl-sulfate reductase (glutathione)

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IntEnz Enzyme Nomenclature


Accepted name:
adenylyl-sulfate reductase (glutathione)
Other names:
5'-adenylylsulfate reductase
AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming)
plant-type 5'-adenylylsulfate reductase
Systematic name:
AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)



This enzyme differs from EC, adenylyl-sulfate reductase (acceptor), in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033741


  1. Gutierrez-Marcos, J.F., Roberts, M.A., Campbell, E.I. and Wray, J.L.
    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. USA 93: 13377-13382 (1996). [PMID: 8917599]
  2. Setya, A., Murillo, M. and Leustek, T.
    Sulfate reduction in higher plants: Molecular evidence for a novel 5-adenylylphosphosulfate (APS) reductase.
    Proc. Natl. Acad. Sci. USA 93: 13383-13388 (1996). [PMID: 8917600]
  3. Bick, J.A., Aslund, F., Cen, Y. and Leustek, T.
    Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase.
    Proc. Natl. Acad. Sci. USA 95: 8404-8409 (1998). [PMID: 9653199]

[EC created 2000, modified 2002]