Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

MetaCyc Reaction: 2.7.7.4

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 2.7.7.4

Enzymes and Genes:

Allochromatium vinosum:
Arabidopsis thaliana col:
Archaeoglobus fulgidus: sulfate adenylyltransferaseInferred from experiment: sat
Desulfocapsa sulfexigens: sulfate adenylyltransferaseInferred from experiment
Desulfovibrio gigas: sulfate adenylyltransferaseInferred from experiment
Desulfovibrio sulfodismutans: sulfate adenylyltransferaseInferred from experiment
endosymbiont of Riftia pachyptila: dissimilatory sulfate adenylyltransferaseInferred from experiment: sat
Escherichia coli K-12 substr. MG1655: sulfate adenylyltransferaseInferred from experiment: cysD, cysN
Homo sapiens:
Saccharomyces cerevisiae: sulfate adenylyltransferaseInferred from experiment: met3
Sinorhizobium meliloti: sulfate adenylyltransferaseInferred 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 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: 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): -20.452515Inferred 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

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 Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc13.