IUBMB Enzyme Nomenclature


Accepted name: adenylyl-sulfate reductase (glutathione)

Reaction: AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione

Other name(s): 5'-adenylylsulfate reductase (also used for EC; 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)

Comments: This enzyme differs from EC, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or 2-sulfanylethan-1-ol (2-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: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 355840-27-6


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 (1996) 13377-13382. [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 (1996) 13383-13388. [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 (1998) 8404-8409. [PMID: 9653199]

[EC created 2000, modified 2002]

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