Nucleoside-diphosphatase

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nucleoside-diphosphatase
Nucleoside-diphosphatase dimer, Human
Identifiers
EC no.3.6.1.6
CAS no.9027-69-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a nucleoside-diphosphatase (EC 3.6.1.6) is an enzyme that catalyzes the chemical reaction

a nucleoside diphosphate + H2O a nucleotide + phosphate

Thus, the two substrates of this enzyme are nucleoside diphosphate and H2O, whereas its two products are nucleotide and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside-diphosphate phosphohydrolase. Other names in common use include thiamine pyrophosphatase, UDPase, inosine diphosphatase, adenosine diphosphatase, IDPase, ADPase, adenosinepyrophosphatase, guanosine diphosphatase, guanosine 5'-diphosphatase, inosine 5'-diphosphatase, uridine diphosphatase, uridine 5'-diphosphatase, nucleoside diphosphate phosphatase, type B nucleoside diphosphatase, GDPase, CDPase, nucleoside 5'-diphosphatase, type L nucleoside diphosphatase, NDPase, and nucleoside diphosphate phosphohydrolase. This enzyme participates in purine metabolism and pyrimidine metabolism.

Structural studies[edit]

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2H2N and 2H2U.

References[edit]

  • GIBSON DM, AYENGAR P, SANADI DR (1955). "A phosphatase specific for nucleoside diphosphates". Biochim. Biophys. Acta. 16 (4): 536–8. doi:10.1016/0006-3002(55)90275-4. PMID 14389272.
  • Horecker BL, Hurwitz J, Heppel LA (1957). "The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate". J. Am. Chem. Soc. 79 (3): 701–702. doi:10.1021/ja01560a054.
  • Sano S, Matsuda Y, Nakagawa H (1988). "Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase". J Biochem. 103 (4): 678–81. doi:10.1093/oxfordjournals.jbchem.a122328. PMID 2844741.

External links[edit]