The Enzyme Database

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EC 1.8.4.10     
Accepted name: adenylyl-sulfate reductase (thioredoxin)
Reaction: AMP + sulfite + thioredoxin disulfide = 5′-adenylyl sulfate + thioredoxin
Other name(s): thioredoxin-dependent 5′-adenylylsulfate reductase
Systematic name: AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5′-phosphosulfate-forming)
Comments: Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bick, J.A., Dennis, J.J., Zylstra, G.J., Nowack, J. and Leustek, T. Identification of a new class of 5-adenylylsulfate (APS) reductase from sulfate-assimilating bacteria. J. Bacteriol. 182 (2000) 135–142. [PMID: 10613872]
2.  Abola, A.P., Willits, M.G., Wang, R.C. and Long, S.R. Reduction of adenosine-5′-phosphosulfate instead of 3′-phosphoadenosine-5′-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae. J. Bacteriol. 181 (1999) 5280–5287. [PMID: 10464198]
3.  Williams, S.J., Senaratne, R.H., Mougous, J.D., Riley, L.W. and Bertozzi, C.R. 5′-Adenosinephosphosulfate lies at a metabolic branchpoint in mycobacteria. J. Biol. Chem. 277 (2002) 32606–32615. [PMID: 12072441]
4.  Neumann, S., Wynen, A., Truper, H.G. and Dahl, C. Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. Mol. Biol. Rep. 27 (2000) 27–33. [PMID: 10939523]
[EC 1.8.4.10 created 2003]
 
 


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