ExplorEnz: EC 1.8.4.9

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1.8.4.9

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 1.8.99.2); 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 1.8.99.2, 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, Ulva intestinalis.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 355840-27-6

References:

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 9653199]

[EC 1.8.4.9 created 2000, modified 2002]