Short description: Group of proteins having nucleoside-diphosphatase activity
| nucleoside-diphosphatase |
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 Nucleoside-diphosphatase dimer, Human |
| Identifiers |
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| EC number | 3.6.1.6 |
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| CAS number | 9027-69-4 |
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| Databases |
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| IntEnz | IntEnz view |
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| BRENDA | BRENDA entry |
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| ExPASy | NiceZyme view |
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| KEGG | KEGG entry |
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| MetaCyc | metabolic pathway |
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| PRIAM | profile |
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| PDB structures | RCSB PDB PDBe PDBsum |
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| Gene Ontology | AmiGO / QuickGO |
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| Search |
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| PMC | articles |
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| PubMed | articles |
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| NCBI | proteins |
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In enzymology, a nucleoside-diphosphatase (EC 3.6.1.6) is an enzyme that catalyzes the chemical reaction
- a nucleoside diphosphate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "A phosphatase specific for nucleoside diphosphates". Biochim. Biophys. Acta 16 (4): 536–8. 1955. doi:10.1016/0006-3002(55)90275-4. PMID 14389272.
- "The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate". J. Am. Chem. Soc. 79 (3): 701–702. 1957. doi:10.1021/ja01560a054.
- "Thiamine pyrophosphatase (nucleoside diphosphatase) in the Golgi apparatus is distinct from microsomal nucleoside diphosphatase". J Biochem 103 (4): 678–81. 1988. doi:10.1093/oxfordjournals.jbchem.a122328. PMID 2844741.
External links
- Thiamine+pyrophosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolases: acid anhydride hydrolases (EC 3.6) |
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| 3.6.1 |
- Pyrophosphatase
- Apyrase
- Thiamine-triphosphatase
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| 3.6.2 |
- Adenylylsulfatase
- Phosphoadenylylsulfatase
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| 3.6.3-4: ATPase | | 3.6.3 | | Cu++ (3.6.3.4) |
- Menkes/ATP7A
- Wilson/ATP7B
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| Ca+ (3.6.3.8) |
- SERCA
- Plasma membrane
- ATP2B1
- ATP2B2
- ATP2B3
- ATP2B4
- SPCA
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| Na+/K+ (3.6.3.9) |
- ATP1A1
- ATP1A2
- ATP1A3
- ATP1A4
- ATP1B1
- ATP1B2
- ATP1B3
- ATP1B4
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| H+/K+ (3.6.3.10) | |
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| Other P-type ATPase |
- ATP8B1
- ATP10A
- ATP11B
- ATP12A
- ATP13A2
- ATP13A3
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| 3.6.4 |
- Dynein
- Kinesin
- Myosin
- Katanin
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| 3.6.5: GTPase | | 3.6.5.1: Heterotrimeric G protein |
- Gαs
- Gαi
- GNAI1
- GNAI2
- GNAI3
- Transducin
- Gustducin
- Gαq/11
- Gα12/13
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| 3.6.5.2: Small GTPase > Ras superfamily |
- Rho family of GTPases: Cdc42
- RhoUV
- Rac
- RhoBTB
- RhoH
- Rho
- Rnd
- RhoDF
- other: Ras
- Rab
- Arf
- Ran
- Rheb
- Rap
- RGK
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| 3.6.5.3: Protein-synthesizing GTPase | |
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| 3.6.5.5-6: Polymerization motors | |
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Enzymes |
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
- Enzyme activator
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
- EC7 Translocases (list)
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 | Original source: https://en.wikipedia.org/wiki/Nucleoside-diphosphatase. Read more |