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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Pathway: sulfate activation for sulfonation

Enzyme View:

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Synonyms: sulfation pathway

Superclasses: Activation/Inactivation/Interconversion Activation
Degradation/Utilization/Assimilation Inorganic Nutrients Metabolism Sulfur Compounds Metabolism

Some taxa known to possess this pathway include ? : Arabidopsis thaliana col , Escherichia coli K-12 substr. MG1655 , Glycine max , Homo sapiens , Saccharomyces cerevisiae

Expected Taxonomic Range: Bacteria , Eukaryota

Summary:
General Background

The sulfonation of biological compounds (sulfoconjugation) is a fundamental metabolic process, in which a sulfate group is added to an oxygen moiety to form a sulfate ester bond. The sulfonation of biomolecules occurs widely and results in a dramatic change in the physicochemical property of the sulfonated compounds [Huxtable86]. Sulfonated macromolecules such as a glycosaminoglycan, heparin or a glucosinolate are involved in many important processes, such as cell adhesion, hemostasis, the viscoelastic properties of connective tissue, and plant defense mechanisms. The sulfonation of tyrosine residues has been established as a post-translational modification for many secretory and membrane proteins (see protein-tyrosine sulfotransferase 1) and sulfated versions of lipids such as sphingolipids and galactoglycerolipids are found in the brain, peripheral nerves, and reproductive tissues of mammals. In addition, sulfoconjugation is important in the biotransformation of many low molecular weight compounds such as neurotransmitters and hormones, including catecholamines, iodothyronines, and steroids, and in the production of plant secondary metabolites, such as glucosinolates. Another role for sulfonation is the detoxification and removal of drugs and xenobiotics compounds [Venkatachalam98].

About This Pathway

In the course of sulfonation, inorganic sulfate must be activated prior to being transferred to an acceptor molecule [Gregory60]. In many organisms, including plants and mammals, 3'-phosphoadenylyl-sulfate (PAPS) is used as the universal sulfonate donor for all sulfotransferase reactions [Robbins58, Farooqui80].

The activation of inorganic sulfate to form PAPS is achieved by the concerted action of two enzymes. The first step is catalyzed by EC 2.7.7.4, sulfate adenylyltransferase (also known as ATP-sulfurylase) and involves the reaction of inorganic sulfate with ATP to form adenosine 5'-phosphosulfate (APS) and inorganic pyrophosphate (PPi). This enzyme has an unfavorable equilibrium (Keq ~ 10-7 M) in the direction of APS formation, and it has been postulated that the reaction is driven by the hydrolysis of PPi by a ubiquitous inorganic pyrophosphatase [Segel87]. In Escherichia coli K-12 it was found that the enzymes couples the formation of APS to hydrolysis of GTP [Liu94a].

The second step is catalyzed by EC 2.7.1.25, adenylyl-sulfate kinase, and involves the reaction of APS with ATP to form PAPS and ADP.

It should be mentioned that in plants most of the APS is used for biosynthesis of L-cysteine and L-methionine via the further reduction of APS to sulfide (see sulfate reduction II (assimilatory)). In mammals, however, all of the APS is converted to PAPS and used for sulfonation.

In bacteria, fungi, yeast and plants the two enzymes are found as separate polypeptide chains. In mammals the enzymes are physically linked on a single bifunctional protein [Lyle94].

For an extensive list of sulfonation reactions using 3'-phosphoadenylyl-sulfate, please look at that compound's page.

Superpathways: sulfate reduction I (assimilatory) , superpathway of methionine biosynthesis (by sulfhydrylation) , superpathway of sulfate assimilation and cysteine biosynthesis , superpathway of sulfur amino acid biosynthesis (Saccharomyces cerevisiae)

Unification Links: AraCyc:PWY-5340 , EcoCyc:PWY-5340

Credits:
Created 19-Sep-2006 by Caspi R , SRI International


References

Casu89: Casu, B. (1989). "in Heparin: Chemical and Biological Properties, Clinical Applications." Lane, D. A., and Lindahl, U., Eds, pp 25-49, CRC Press, Boca Raton, FL.

Farooqui80: Farooqui AA (1980). "3'-phosphoadenosine 5'-phosphosulphate metabolism in mammalian tissues." Int J Biochem 12(4);529-36. PMID: 6107250

Gatti79: Gatti, G., Casu, B., Hamer, G. K., Pelin, A. S. (1979). Macromolecules 12:1001-1007.

Gregory60: Gregory JD, Robbins PW (1960). "Metabolism of sulfur compounds (sulfate metabolism)." Annu Rev Biochem 29;347-64. PMID: 13851709

Hayes08: Hayes JD, Kelleher MO, Eggleston IM (2008). "The cancer chemopreventive actions of phytochemicals derived from glucosinolates." Eur J Nutr 47 Suppl 2;73-88. PMID: 18458837

Huxtable86: Huxtable, R.J. (1986). "Biochemistry of Sulfur, pp. 293-358." Plenum Publishing Corp., New York.

Leustek02: Leustek, Thomas (2002). "Sulfate metabolism." The Arabidopsis Book, American Society of Plant Biologists.

Liu94a: Liu C, Martin E, Leyh TS (1994). "GTPase activation of ATP sulfurylase: the mechanism." Biochemistry 33(8);2042-7. PMID: 8117661

Lyle94: Lyle S, Stanczak J, Ng K, Schwartz NB (1994). "Rat chondrosarcoma ATP sulfurylase and adenosine 5'-phosphosulfate kinase reside on a single bifunctional protein." Biochemistry 33(19);5920-5. PMID: 8180221

Robbins58: Robbins, P.W., Lipmann, F. (1958). "Separation of the two enzymatic phases in active sulfate synthesis." J Biol Chem 233(3):681-5. PMID: 13575436

Segel87: Segel IH, Renosto F, Seubert PA (1987). "Sulfate-activating enzymes." Methods Enzymol 143;334-49. PMID: 2821345

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

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Abola99: Abola AP, Willits MG, Wang RC, Long SR (1999). "Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae." J Bacteriol 181(17);5280-7. PMID: 10464198

Bairoch93a: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Dahl90: Dahl, C., Koch, H., Keuken, O., Trueper, H.G. (1990). "Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate-reducer, Archaeoglobus fulgidus." FEMS Microbiol. Let. 67: 27-32.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Frederiksen03: Frederiksen TM, Finster K (2003). "Sulfite-oxido-reductase is involved in the oxidation of sulfite in Desulfocapsa sulfoexigens during disproportionation of thiosulfate and elemental sulfur." Biodegradation 14(3);189-98. PMID: 12889609

Gavel98: Gavel OY, Bursakov SA, Calvete JJ, George GN, Moura JJ, Moura I (1998). "ATP sulfurylases from sulfate-reducing bacteria of the genus Desulfovibrio. A novel metalloprotein containing cobalt and zinc." Biochemistry 1998;37(46);16225-32. PMID: 9819214

Girard98: Girard JP, Baekkevold ES, Amalric F (1998). "Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase." FASEB J 12(7);603-12. PMID: 9576487

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hansen94a: Hansen TA (1994). "Metabolism of sulfate-reducing prokaryotes." Antonie Van Leeuwenhoek 1994;66(1-3);165-85. PMID: 7747930

Hatzfeld00: Hatzfeld Y, Lee S, Lee M, Leustek T, Saito K (2000). "Functional characterization of a gene encoding a fourth ATP sulfurylase isoform from Arabidopsis thaliana." Gene 2000;248(1-2);51-8. PMID: 10806350

Hawes73: Hawes CS, Nicholas DJ (1973). "Adenosine 5'-triphosphate sulphurylase from Saccharomyces cerevisiae." Biochem J 1973;133(3);541-50. PMID: 4582048

Kraemer89: Kraemer, M., Cypionka, H. (1989). "Sulfate formation via ATP sulfurylase in thiosulfate- and sulfite-disproportionating bacteria." Arch. Microbiol. 151:232-237.

Krisko14: Kri Ko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

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

Leustek94: Leustek T, Murillo M, Cervantes M (1994). "Cloning of a cDNA encoding ATP sulfurylase from Arabidopsis thaliana by functional expression in Saccharomyces cerevisiae." Plant Physiol 1994;105(3);897-902. PMID: 8058839

Leyh88: Leyh TS, Taylor JC, Markham GD (1988). "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization." J Biol Chem 263(5);2409-16. PMID: 2828368

Leyh92: Leyh TS, Suo Y (1992). "GTPase-mediated activation of ATP sulfurylase." J Biol Chem 1992;267(1);542-5. PMID: 1730615

Showing only 20 references. To show more, press the button "Show all references".


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 Sun Dec 21, 2014, biocyc14.