Sulfate adenylyltransferase

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sulfate adenylyltransferase (ATP)
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
ATP-sulfurylase
PDB 1v47 EBI.jpg
crystal structure of atp sulfurylase from thermus thermophillus hb8 in complex with aps
Identifiers
Symbol ATP-sulfurylase
Pfam PF01747
InterPro IPR002650
SCOP 1i2d
SUPERFAMILY 1i2d

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

ATP + sulfate diphosphate + adenylyl sulfate

Thus, the two substrates of this enzyme are ATP and sulfate, whereas its two products are diphosphate 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]

Structural studier[edit]

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.

Applications[edit]

ATP sulfurylase is one of the enzymes used in pyrosequencing.

References[edit]

  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. PMID 8522184. doi:10.1016/0378-1119(95)00450-K. 
  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. PMC 21136Freely accessible. PMID 9671738. doi:10.1073/pnas.95.15.8681. 

Further reading[edit]

  • Bandurski RS, Wilson LG, Squires CL (1956). "The mechanism of "active sulfate" formation". J. Am. Chem. Soc. 78 (24): 6408–6409. 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. 
  • 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. doi:10.1074/jbc.273.30.19311. 

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