EC 1.8.4.10 - Adenylyl-sulfate reductase (thioredoxin)

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IntEnz Enzyme Nomenclature
EC 1.8.4.10

Names

Accepted name:
adenylyl-sulfate reductase (thioredoxin)
Other name:
thioredoxin-dependent 5'-adenylylsulfate reductase
Systematic name:
AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043866
UniProtKB/Swiss-Prot:

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: 135-142 (2000). [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: 5280-5287 (1999). [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: 32606-32615 (2002). [PMID: 12072441]
  4. Neumann, S., Wynen, A., Trüper, H.G. and Dahl, C.
    Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway.
    Mol. Biol. Rep. 27: 27-33 (2000). [PMID: 10939523]

[EC 1.8.4.10 created 2003]