Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:
3'-phospho-adenylylsulfate reductaseInferred from experiment: cysH

In Pathway: sulfate reduction I (assimilatory)

Supersedes EC number:

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: phosphoadenylyl-sulfate reductase (thioredoxin)

Enzyme Commission Synonyms: 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 oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)

The third reaction in converting sulfate to sulfide. The first reaction in the reduction of sulfate to sulfite in the pathway leading to cysteine synthesis.

Note: Reaction E.C. was transferred to E.C in 2000.

Enzyme Commission Summary:
Specific for PAPS. The enzyme from Escherichia coli will use thioredoxins from other species.

Citations: [Berendt95]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Berendt95: 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 1995;233(1);347-56. PMID: 7588765

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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