Sulfate adenylyltransferase

Sulfate adenylyltransferase (ATP)
Sulfate adenylyltransferase (bifunctional) homohexamer, Thiobacillus denitrificans
Identifiers
EC no.2.7.7.4
CAS no.9012-39-9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
ATP-sulfurylase
crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps, seb.e is the best
Identifiers
SymbolATP-sulfurylase
PfamPF01747
InterProIPR002650
SCOP21i2d / SCOPe / SUPFAM
Available protein structures:
PDB  IPR002650 PF01747 (ECOD; PDBsum)  
AlphaFold

Sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the first of two chemical reactions that convert adenosine triphosphate to 3'-phosphoadenosine-5'-phosphosulfate, a coenzyme in sulfotransferase reactions.[1] The product is adenosine 5′-phosphosulfate, which is the substrate for the final enzyme, adenylyl-sulfate kinase.[2]

Function

In bacteria, yeast, fungi and plants the enzyme sulfate adenylyltransferase converts adenosine triphosphate to adenosine 5′-phosphosulfate by reaction with sulfate ion, giving pyrophosphate (PPi) as a byproduct:[1]

2D representation of the chemical structure of adenosine triphosphate .
adenosine triphosphate
+ SO2−4
 
 
 
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
PPi
 
2D representation of the chemical structure of Q356138.
adenosine 5′-phosphosulfate

In these organisms, adenosine 5′-phosphosulfate is subsequently converted to 3'-phosphoadenosine-5'-phosphosulfate (PAPS) by adenylyl-sulfate kinase.[3] Some sulfate adenylyltransferases including the human form are part of a bifunctional polypeptide associated with both activities.[2][4][5]

Within the cell, sulfate adenylyltransferase plays a key role in both assimilatory sulfate reduction and dissimilatory sulfur oxidation and reduction (DSR) and participates in the biogeochemically relevant sulfur cycle.[6][7] In dissimilatory sulfate reduction the enzyme acts as the first priming step in the reduction converting sulfate 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 and then sulfide. Conversely, in the process of dissimilatory sulfur oxidation, pyrophosphate combines with APS in the reverse reaction to form sulfate.[6] In either direction in which the sulfate adenylyltransferase acts, (reduction or oxidation) proceeds along DSR in bacterial cells, the associated pathways are participating in cellular respiration necessary for the growth of the organism.[8]

Nomenclature

The enzyme is a family of transferase, specifically one 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.[9]

Structural studies

As of late 2007, 18 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1G8F​, PDB: 1G8G​, PDB: 1G8H​, PDB: 1I2D​, PDB: 1J70​, PDB: 1JEC​, PDB: 1JED​, PDB: 1JEE​, PDB: 1JHD​, PDB: 1M8P​, PDB: 1R6X​, PDB: 1TV6​, PDB: 1V47​, PDB: 1X6V​, PDB: 1XJQ​, PDB: 1XNJ​, PDB: 1ZUN​, and PDB: 2GKS​.

In yeast other fungi and bacteria participating in assimilatory sulfate reduction, the sulfate adenylyltransferase is in the form a of a homohexamer.[6][10] Its shape is that of a homotetramer in plants.[11] 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.[10] 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.[12] The active site is located in the center of the sulfate adenylyltransferase above the Domain II between the other domains I and 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.[12]

Applications

ATP sulfurylase is one of the enzymes used in pyrosequencing.[13]

References

  1. 1 2 Günal S; Hardman R; Kopriva S; Mueller JW (2019). "Sulfation pathways from red to green". J. Biol. Chem. 294 (33): 12293–12312. doi:10.1074/jbc.REV119.007422. PMC 6699852. PMID 31270211.
  2. 1 2 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. doi:10.1074/jbc.273.30.19311. PMID 9668121.
  3. ↑ MacRae IJ, Rose AB, Segel IH (October 1998). "Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues". J. Biol. Chem. 273 (44): 28583–9. doi:10.1074/jbc.273.44.28583. PMID 9786849.
  4. ↑ 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.
  5. ↑ 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.
  6. 1 2 3 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ Enzyme 2.7.7.4 at KEGG Pathway Database.
  10. 1 2 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.
  11. ↑ 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.
  12. 1 2 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. PMC 133462. PMID 11157739.
  13. ↑ Metzker M. (2005). "Emerging Technologies in DNA Sequencing". Genome Research. 15 (12): 1767–76. doi:10.1101/gr.3770505. PMID 16339375.
This article incorporates text from the public domain Pfam and InterPro: IPR002650
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