Nucleotide diphosphatase
In enzymology, a nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction
- a dinucleotide + H2O 2 mononucleotides
| nucleotide diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.9 | ||||||||
| CAS number | 9032-64-8 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are dinucleotide and H2O, whereas its product is mononucleotide.
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 dinucleotide nucleotidohydrolase. Other names in common use include nucleotide pyrophosphatase, and nucleotide-sugar pyrophosphatase. This enzyme participates in 5 metabolic pathways: purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1NQY, 1NQZ, 2GSN, 2GSO, and 2GSU.
References
- Jacobson JB; Kaplan NO (1957). "A reduced pyridine nucleotide pyrophosphatase". J. Biol. Chem. 226: 427–437. PMID 13428775.
- Kornberg A; Pricer WE (1950). "Nucleotide pyrophosphatase". J. Biol. Chem. 182: 763–778.
- Kumar SA, Rao NA, Vaidyanathan CS (1965). "Nucleotidases in plants. I. Partial purification and properties of the enzyme hydrolyzing flavine adenine dinucleotide from mung bean seedlings (Phaseolus radiatus)". Arch. Biochem. Biophys. 111 (3): 646–52. doi:10.1016/0003-9861(65)90246-8. PMID 5862212.
- Swartz MN, Kaplan NO, Lamborg MF (1958). "A "heat-activated" diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris". J. Biol. Chem. 232: 1051–1063. PMID 13549486.