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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 2.7.7.4

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

EC Number: 2.7.7.4

Enzymes and Genes:
sulfate adenylyltransferase Inferred from experiment : cysD , cysN ( Escherichia coli K-12 substr. MG1655 )
assimilatory sulfate adenylyltransferase Inferred by computational analysis : cysN , cysD ( Allochromatium vinosum )
3'-phosphoadenosine 5'-phosphosulfate synthase 1 Inferred from experiment : PAPSS1 ( Homo sapiens )
3'-phosphoadenosine 5'-phosphosulfate synthase 2 Inferred from experiment : PAPSS2 ( Homo sapiens )
sulfate adenylyltransferase Inferred from experiment : cysD , cysN ( Sinorhizobium meliloti )
dissimilatory sulfate adenylyltransferase Inferred from experiment : sat ( Allochromatium vinosum )
sulfate adenylyltransferase Inferred from experiment : sat ( Archaeoglobus fulgidus )
dissimilatory sulfate adenylyltransferase Inferred from experiment : sat ( endosymbiont of Riftia pachyptila )
sulfate adenylyltransferase Inferred from experiment ( Desulfocapsa sulfexigens )
sulfate adenylyltransferase Inferred from experiment ( Desulfovibrio sulfodismutans )
ATP sulfurylase Inferred from experiment : APS2 ( Arabidopsis thaliana col )
sulfate adenylyltransferase Inferred from experiment : APS4 ( Arabidopsis thaliana col )
sulfate adenylyltransferase Inferred from experiment : APS3 ( Arabidopsis thaliana col )
ATP sulfurylase Inferred from experiment : APS1 ( Arabidopsis thaliana col )
sulfate adenylyltransferase Inferred from experiment : met3 ( Saccharomyces cerevisiae )
sulfate adenylyltransferase Inferred from experiment ( Desulfovibrio gigas )

In Pathway: sulfite oxidation III , sulfate activation for sulfonation , sulfate reduction II (assimilatory) , sulfate reduction V (dissimilatory) , sulfate reduction III (assimilatory) , sulfate reduction IV (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 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).

Citations: [Hilz55, Venkatachalam98]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R00529 , Rhea:18133

Relationship Links: BRENDA:EC:2.7.7.4 , ENZYME:EC:2.7.7.4 , IUBMB-ExplorEnz:EC:2.7.7.4 , 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


References

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 18.5 on Fri Dec 19, 2014, BIOCYC14A.