| sulfate adenylyltransferase (ATP) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Sulfate adenylyltransferase (bifunctional) homohexamer, Thiobacillus denitrificans | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.7.4 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction
- ATP + sulfate ⇌ 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 sulfur 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]
- ^ Rosenthal E, Leustek T (November 1995). "A multifunctional Urechis caupo protein, PAPS synthetase, has both ATP sulfurylase and APS kinase activities". Gene. 165 (2): 243–8. doi:10.1016/0378-1119(95)00450-K. PMID 8522184.
- ^ Kurima K, Warman ML, Krishnan S, Domowicz M, Krueger RC, Deyrup A, Schwartz NB (July 1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–8685. Bibcode:1998PNAS...95.8681K. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.
- ^ a b 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". PLOS ONE. 8 (9): e74707. Bibcode:2013PLoSO...874707P. doi:10.1371/journal.pone.0074707. ISSN 1932-6203. PMC 3779200. PMID 24073218.
- ^ Herrmann, Jonathan; Ravilious, Geoffrey E.; McKinney, Samuel E.; Westfall, Corey S.; Lee, Soon Goo; Baraniecka, Patrycja; Giovannetti, Marco; Kopriva, Stanislav; Krishnan, Hari B.; Jez, Joseph M. (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. PMC 4036203. PMID 24584934.
- ^ Gibson, G. R. (1990). "Physiology and ecology of the sulphate-reducing bacteria". Journal of Applied Bacteriology. 69 (6): 769–797. doi:10.1111/j.1365-2672.1990.tb01575.x. ISSN 1365-2672. PMID 2286579.