Adenylyl-sulfate reductase (thioredoxin)

The 3 substrates of this enzyme are adenosine monophosphate, sulfite, and thioredoxin disulfide, whereas its two products are 5'-adenylyl sulfate and thioredoxin.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming). This enzyme is also called thioredoxin-dependent 5'-adenylylsulfate reductase.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2GOY.

References

Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T (2000). "Identification of a New Class of 5′-Adenylylsulfate (APS) Reductases from Sulfate-Assimilating Bacteria". J. Bacteriol. 182 (1): 135–42. doi:10.1128/JB.182.1.135-142.2000. PMC 94249. PMID 10613872.
Abola AP, Willits MG, Wang RC, Long SR (1999). "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 (17): 5280–7. PMC 94033. PMID 10464198.
Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR (2002). "5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria". J. Biol. Chem. 277 (36): 32606–15. doi:10.1074/jbc.M204613200. PMID 12072441.
Neumann S, Wynen A, Truper HG, Dahl C (2000). "Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway". Mol. Biol. Rep. 27 (1): 27–33. doi:10.1023/A:1007058421714. PMID 10939523.

Oxidoreductases: sulfur oxidoreductases (EC 1.8)

1.8.1: NAD or NADP	Dihydrolipoamide dehydrogenase Glutathione reductase Thioredoxin reductase

1.8.2: cytochrome	Sulfite dehydrogenase Thiosulfate dehydrogenase

1.8.3: oxygen	Sulfite oxidase

1.8.4: disulfide	Glutathione—homocystine transhydrogenase

1.8.5: quinone	Glutathione dehydrogenase (ascorbate)

1.8.98: Other, known	CoB—CoM heterodisulfide reductase

1.8.99: Other	Sulfite reductase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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