Biology:Sulfate adenylyltransferase
| sulfate adenylyltransferase (ATP) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Sulfate adenylyltransferase (bifunctional) homohexamer, Thiobacillus denitrificans | |||||||||
| Identifiers | |||||||||
| EC number | 2.7.7.4 | ||||||||
| CAS number | 9012-39-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| ATP-sulfurylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps, seb.e is the best | |||||||||
| Identifiers | |||||||||
| Symbol | ATP-sulfurylase | ||||||||
| Pfam | PF01747 | ||||||||
| InterPro | IPR002650 | ||||||||
| SCOP2 | 1i2d / SCOPe / SUPFAM | ||||||||
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In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction
- ATP + sulfate [math]\displaystyle{ \rightleftharpoons }[/math]pyrophosphate + adenylyl sulfate
Thus, the two substrates of this enzyme are ATP and sulfate, whereas its two products are pyrophosphate and adenylyl sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:sulfate adenylyltransferase. Other names in common use include adenosine-5'-triphosphate sulfurylase, adenosinetriphosphate sulfurylase, adenylylsulfate pyrophosphorylase, ATP sulfurylase, ATP-sulfurylase, and sulfurylase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.
Some sulfate adenylyltransferases are part of a bifunctional polypeptide chain associated with adenosyl phosphosulfate (APS) kinase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate.[1][2]
Within the cell Sulfate adenylyltransferase plays a key role in both assimilatory sulfur reduction and dissimilatory sulfur oxidation and reduction (DSR) and participates in the biogeochemically relevant sulfur cycle.[3][4] In dissimilatory sulfate reduction the SAT enzyme, acts as the first priming step in the reduction converting sulfate(+6) to Adenosine 5'-phosphosulfate (APS) via adenylation at the cost of an ATP. If the organisms participating in the DSR pathway possess the full suite of genes necessary, APS can then be further stepwise reduced to sulfite(+4) and then sulfide (-2). Conversely in the process of dissimilatory sulfate oxidation, pyrophosphate combines with APS in a sulfate adenylyltransferase catalyzed reaction to form sulfate.[3] In either direction in which the Sulfate adenylyltransferase (reduction or oxidation) proceeds along DSR in bacterial cells, the associated pathways are participating in cellular respiration necessary for the growth of the organism.[5]
Structural studies
As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes 1G8F, 1G8G, 1G8H, 1I2D, 1J70, 1JEC, 1JED, 1JEE, 1JHD, 1M8P, 1R6X, 1TV6, 1V47, 1X6V, 1XJQ, 1XNJ, 1ZUN, and 2GKS.
In yeast other fungi and bacteria participating in assimilatory sulfate reduction, the sulfate adenylyltransferase is in the form a of a homohexamer.[3][6] Its shape is that of a homotetramer in plants.[7] In Saccharomyces cerevisiae sulfate adenylyltransferase is composed of four domains. Domain I features the N-terminus with beta-barrels similar to pyruvate kinase. A right handed alpha/beta fold makes of the shape of Domain II, and it also contains the active site and substrate-binding pocket. Domain III is composed of a region linking the terminal domain to Domain I & II. Domain IV contains the C-terminus of the protein and forms a typical alpha/beta-fold.[6] The active site of Sulfate adenylyltransferase is composed mostly of portions of the Domain II specifically, H9, S9, S10, S12, and the conserved RNP-Loop and GRD-Loop.[8] The active site is located in the center of the Sulfate adenylyltransferase above the Domain II between the other domains I & II. The core of the groove in which the active site is located is mostly composed of hydrophobic residues, but towards the outside of the groove are positive and hydrophilic residues necessary for substrate binding.[8]
Applications
ATP sulfurylase is one of the enzymes used in pyrosequencing.
References
- ↑ "A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities". Gene 165 (2): 243–8. November 1995. doi:10.1016/0378-1119(95)00450-K. PMID 8522184.
- ↑ "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–5. July 1998. doi:10.1073/pnas.95.15.8681. PMID 9671738. Bibcode: 1998PNAS...95.8681K.
- ↑ 3.0 3.1 3.2 Parey, Kristian; Demmer, Ulrike; Warkentin, Eberhard; Wynen, Astrid; Ermler, Ulrich; Dahl, Christiane (2013-09-20). "Structural, Biochemical and Genetic Characterization of Dissimilatory ATP Sulfurylase from Allochromatium vinosum" (in en). PLOS ONE 8 (9): e74707. doi:10.1371/journal.pone.0074707. ISSN 1932-6203. PMID 24073218. Bibcode: 2013PLoSO...874707P.
- ↑ Herrmann, Jonathan; Ravilious, Geoffrey E.; McKinney, Samuel E.; Westfall, Corey S.; Lee, Soon Goo; Baraniecka, Patrycja; Giovannetti, Marco; Kopriva, Stanislav et al. (April 2014). "Structure and Mechanism of Soybean ATP Sulfurylase and the Committed Step in Plant Sulfur Assimilation". Journal of Biological Chemistry 289 (15): 10919–10929. doi:10.1074/jbc.m113.540401. ISSN 0021-9258. PMID 24584934.
- ↑ Gibson, G. R. (1990). "Physiology and ecology of the sulphate-reducing bacteria" (in en). Journal of Applied Bacteriology 69 (6): 769–797. doi:10.1111/j.1365-2672.1990.tb01575.x. ISSN 1365-2672. PMID 2286579. https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1365-2672.1990.tb01575.x.
- ↑ 6.0 6.1 Ullrich, T. C.; Huber, R. (2001-11-09). "The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle". Journal of Molecular Biology 313 (5): 1117–1125. doi:10.1006/jmbi.2001.5098. ISSN 0022-2836. PMID 11700067. https://pubmed.ncbi.nlm.nih.gov/11700067.
- ↑ Logan, Helen M.; Cathala, Nicole; Grignon, Claude; Davidian, Jean-Claude (May 1996). "Cloning of a cDNA Encoded by a Member of the Arabidopsis thaliana ATP Sulfurylase Multigene Family". Journal of Biological Chemistry 271 (21): 12227–12233. doi:10.1074/jbc.271.21.12227. ISSN 0021-9258. PMID 8647819.
- ↑ 8.0 8.1 Ullrich, T. C.; Blaesse, M.; Huber, R. (2001-02-01). "Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation". The EMBO Journal 20 (3): 316–329. doi:10.1093/emboj/20.3.316. ISSN 0261-4189. PMID 11157739. PMC 133462. https://www.embopress.org/doi/full/10.1093/emboj/20.3.316.
Further reading
- "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. 1956. doi:10.1021/ja01605a028.
- Hilz H; Lipmann F (1955). "The enzymatic activation of sulfate". Proc. Natl. Acad. Sci. USA 41 (11): 880–890. doi:10.1073/pnas.41.11.880. PMID 16589765. Bibcode: 1955PNAS...41..880H.
- "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. 1998. doi:10.1074/jbc.273.30.19311. PMID 9668121.
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