Phosphoadenylyl-sulfate reductase (thioredoxin)

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phosphoadenylyl-sulfate reductase (thioredoxin)
EC no.
CAS no.9068-63-7
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a phosphoadenylyl-sulfate reductase (thioredoxin) (EC is an enzyme that catalyzes the chemical reaction

adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide 3'-phosphoadenylyl sulfate + thioredoxin

The 3 substrates of this enzyme are adenosine 3',5'-bisphosphate, sulfite, and thioredoxin disulfide, whereas its two products are 3'-phosphoadenylyl 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 adenosine 3',5'-bisphosphate,sulfite:thioredoxin-disulfide oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). Other names in common use include PAPS reductase, thioredoxin-dependent, PAPS reductase, thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase, 3'-phosphoadenylylsulfate reductase, thioredoxin:3'-phospho-adenylylsulfate reductase, phosphoadenosine-phosphosulfate reductase, adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin, and oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming). This enzyme participates in sulfur metabolism.

Structural studies[edit]

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1ILO, 1WMJ, and 2O8V.


  • Berendt U, Haverkamp T, Prior A, Schwenn JD (1995). "Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis". Eur. J. Biochem. 233 (1): 347–56. doi:10.1111/j.1432-1033.1995.347_1.x. PMID 7588765.