MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:

Allochromatium vinosum :
Arabidopsis thaliana col :
Archaeoglobus fulgidus : sulfate adenylyltransferase Inferred from experiment : sat
Desulfocapsa sulfexigens : sulfate adenylyltransferase Inferred from experiment
Desulfovibrio gigas : sulfate adenylyltransferase Inferred from experiment
Desulfovibrio sulfodismutans : sulfate adenylyltransferase Inferred from experiment
endosymbiont of Riftia pachyptila : dissimilatory sulfate adenylyltransferase Inferred from experiment : sat
Escherichia coli K-12 substr. MG1655 : sulfate adenylyltransferase Inferred from experiment : cysD , cysN
Homo sapiens :
Saccharomyces cerevisiae : sulfate adenylyltransferase Inferred from experiment : met3
Sinorhizobium meliloti : sulfate adenylyltransferase Inferred from experiment : cysD , cysN

In Pathway: sulfite oxidation III , sulfate activation for sulfonation , sulfate reduction II (assimilatory) , sulfate reduction III (assimilatory) , sulfate reduction IV (dissimilatory) , sulfate reduction V (dissimilatory)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: sulfate adenylyltransferase

Enzyme Commission Synonyms: adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate pyrophosphorylase, ATP sulfurylase, ATP-sulfurylase, sulfurylase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -20.452515 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5′-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC and adenylyl-sulfate kinase (EC

Citations: [Hilz55, Venkatachalam98]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: KEGG:R00529 , Rhea:18133

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , UniProt:RELATED-TO:O23324 , UniProt:RELATED-TO:O33581 , UniProt:RELATED-TO:O34764 , UniProt:RELATED-TO:O43252 , UniProt:RELATED-TO:O48888 , UniProt:RELATED-TO:O67174 , UniProt:RELATED-TO:P08536 , UniProt:RELATED-TO:P13441 , UniProt:RELATED-TO:P13442 , UniProt:RELATED-TO:P21156 , UniProt:RELATED-TO:P23845 , UniProt:RELATED-TO:P28604 , UniProt:RELATED-TO:P74241 , UniProt:RELATED-TO:Q9JUD6 , UniProt:RELATED-TO:Q9JUD7 , UniProt:RELATED-TO:Q9PM66 , UniProt:RELATED-TO:Q10600 , UniProt:RELATED-TO:Q12555 , UniProt:RELATED-TO:Q12650 , UniProt:RELATED-TO:Q27128 , UniProt:RELATED-TO:Q39595 , UniProt:RELATED-TO:Q43170 , UniProt:RELATED-TO:Q43183 , UniProt:RELATED-TO:Q43870 , UniProt:RELATED-TO:Q96349 , UniProt:RELATED-TO:Q96541 , UniProt:RELATED-TO:Q9S7D8


Hilz55: Hilz H, Lipmann F (1955). "THE ENZYMATIC ACTIVATION OF SULFATE." Proc Natl Acad Sci U S A 41(11);880-90. PMID: 16589765

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Venkatachalam98: Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains." J Biol Chem 273(30);19311-20. PMID: 9668121

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed Oct 7, 2015, biocyc12.