Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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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 Thu Nov 27, 2014, BIOCYC13B.