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nucleoside-diphosphatase
Nucleoside-diphosphatase dimer, Human
Identifiers
EC no.	3.6.1.6
CAS no.	9027-69-4
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
Search PMC articles PubMed articles NCBI proteins

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

a nucleoside diphosphate + H₂O ${\displaystyle \rightleftharpoons }$ 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

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

References

• 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

• Thiamine+pyrophosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

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• EC 3.6.1
• Enzymes of known structure
• EC 3.6 stubs