Sulfate adenylyltransferase

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sulfate adenylyltransferase (ATP)
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Sulfate adenylyltransferase (bifunctional) homohexamer, Thiobacillus denitrificans
Identifiers
EC no. 2.7.7.4
CAS no. 9012-39-9
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MetaCyc metabolic pathway
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ATP-sulfurylase
PDB 1v47 EBI.jpg
crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps, seb.e is the best
Identifiers
SymbolATP-sulfurylase
Pfam PF01747
InterPro IPR002650
SCOP2 1i2d / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction

Contents

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 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.

Related Research Articles

Pyrosequencing is a method of DNA sequencing based on the "sequencing by synthesis" principle, in which the sequencing is performed by detecting the nucleotide incorporated by a DNA polymerase. Pyrosequencing relies on light detection based on a chain reaction when pyrophosphate is released. Hence, the name pyrosequencing.

<span class="mw-page-title-main">Sulfate-reducing microorganism</span> Microorganisms that "breathe" sulfates

Sulfate-reducing microorganisms (SRM) or sulfate-reducing prokaryotes (SRP) are a group composed of sulfate-reducing bacteria (SRB) and sulfate-reducing archaea (SRA), both of which can perform anaerobic respiration utilizing sulfate (SO2−
4
) as terminal electron acceptor, reducing it to hydrogen sulfide (H2S). Therefore, these sulfidogenic microorganisms "breathe" sulfate rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration.

<span class="mw-page-title-main">3'-Phosphoadenosine-5'-phosphosulfate</span> Chemical compound

3′-Phosphoadenosine-5′-phosphosulfate (PAPS) is a derivative of adenosine monophosphate (AMP) that is phosphorylated at the 3′ position and has a sulfate group attached to the 5′ phosphate. It is the most common coenzyme in sulfotransferase reactions and hence part of sulfation pathways. It is endogenously synthesized by organisms via the phosphorylation of adenosine 5′-phosphosulfate (APS), an intermediary metabolite. In humans such reaction is performed by bifunctional 3′-phosphoadenosine 5′-phosphosulfate synthases using ATP as the phosphate donor.

<span class="mw-page-title-main">Adenylyl-sulfate reductase</span> Class of enzymes

Adenylyl-sulfate reductase is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate (APS) to sulfite through the use of an electron donor cofactor. The products of the reaction are AMP and sulfite, as well as an oxidized electron donor cofactor.

Adenylyl-sulfate reductase (glutathione) is an enzyme that catalyzes the chemical reaction

Adenylyl-sulfate reductase (thioredoxin) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Sulfite reductase</span> Enzyme family

Sulfite reductases (EC 1.8.99.1) are enzymes that participate in sulfur metabolism. They catalyze the reduction of sulfite to hydrogen sulfide and water. Electrons for the reaction are provided by a dissociable molecule of either NADPH, bound flavins, or ferredoxins.

<span class="mw-page-title-main">Phosphatidate phosphatase</span>

The enzyme phosphatidate phosphatase (PAP, EC 3.1.3.4) is a key regulatory enzyme in lipid metabolism, catalyzing the conversion of phosphatidate to diacylglycerol:

<span class="mw-page-title-main">Adenylyl-sulfate kinase</span>

In enzymology, an adenylyl-sulfate kinase is an enzyme that catalyzes the chemical reaction

In enzymology, a sulfate adenylyltransferase (ADP) (EC 2.7.7.5) is an enzyme that catalyzes the chemical reaction

CCA tRNA nucleotidyltransferase is an enzyme with systematic name CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">PAPSS1</span> Protein-coding gene in the species Homo sapiens

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.

<span class="mw-page-title-main">PAPSS2</span> Protein-coding gene in the species Homo sapiens

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 is an enzyme that in humans is encoded by the PAPSS2 gene.

Sulfur is metabolized by all organisms, from bacteria and archaea to plants and animals. Sulfur can have an oxidation state from -2 to +6 and is reduced or oxidized by a diverse range of organisms. The element is present in proteins, sulfate esters of polysaccharides, steroids, phenols, and sulfur-containing coenzymes.

Sulfate conjugates are a heterogeneous class of polar, anionic organosulfate compounds containing an ester of sulfuric acid. Sulfate conjugates commonly result from the metabolic conjugation of endogenous and exogenous compounds with sulfate (-OSO3).

<span class="mw-page-title-main">Carbohydrate sulfotransferase</span> Class of enzymes which transfer an –SO3 group to glycoproteins and lipids

In biochemistry, carbohydrate sulfotransferases are enzymes within the class of sulfotransferases which catalyze the transfer of the sulfate functional group to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.

Sulfur carrier protein ThiS adenylyltransferase is an enzyme with systematic name ATP:(ThiS) adenylyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Dissimilatory sulfate reduction</span>

Dissimilatory sulfate reduction is a form of anaerobic respiration that uses sulfate as the terminal electron acceptor to produce hydrogen sulfide. This metabolism is found in some types of bacteria and archaea which are often termed sulfate-reducing organisms. The term "dissimilatory" is used when hydrogen sulfide is produced in an anaerobic respiration process. By contrast, the term "assimilatory" would be used in relation to the biosynthesis of organosulfur compounds, even though hydrogen sulfide may be an intermediate.

<span class="mw-page-title-main">Microbial oxidation of sulfur</span>

Microbial oxidation of sulfur is the oxidation of sulfur by microorganisms to build their structural components. The oxidation of inorganic compounds is the strategy primarily used by chemolithotrophic microorganisms to obtain energy to survive, grow and reproduce. Some inorganic forms of reduced sulfur, mainly sulfide (H2S/HS) and elemental sulfur (S0), can be oxidized by chemolithotrophic sulfur-oxidizing prokaryotes, usually coupled to the reduction of oxygen (O2) or nitrate (NO3). Anaerobic sulfur oxidizers include photolithoautotrophs that obtain their energy from sunlight, hydrogen from sulfide, and carbon from carbon dioxide (CO2).

Dissimilatory sulfite reductase is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction.

References

  1. 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.
  2. 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): 8681–5. Bibcode:1998PNAS...95.8681K. doi: 10.1073/pnas.95.15.8681 . PMC   21136 . PMID   9671738.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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. 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.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR002650