EC Tree |
3. Hydrolases |
3.6 Acting on acid anhydrides |
3.6.1 In phosphorus-containing anhydrides |
ID: | 3.6.1.5 | ||||||||||||||||||||||||||||||||||||||||||||
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Description: | Apyrase. | ||||||||||||||||||||||||||||||||||||||||||||
Alternative Name: |
ATP-diphosphohydrolase. ATP-diphosphatase. ADPase. Adenosine diphosphatase. | ||||||||||||||||||||||||||||||||||||||||||||
Prosite: | PDOC00952; | ||||||||||||||||||||||||||||||||||||||||||||
PDB: |
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Cath: | 3.30.420.150; 3.30.420.40; 3.40.50.720; 3.90.176.10; 1.20.82.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.6.1.5 |
BRENDA Enzyme Link: | BRENDA 3.6.1.5 |
KEGG Enzyme Link: | KEGG3.6.1.5 |
BioCyc Enzyme Link: | BioCyc 3.6.1.5 |
ExPASy Enzyme Link: | ExPASy3.6.1.5 |
EC2PDB Enzyme Link: | EC2PDB 3.6.1.5 |
ExplorEnz Enzyme Link: | ExplorEnz 3.6.1.5 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.6.1.5 |
IntEnz Enzyme Link: | IntEnz 3.6.1.5 |
MEDLINE Enzyme Link: | MEDLINE 3.6.1.5 |
RHEA:36795 | a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate |
RULE(radius=1) | [*:1]=[P;H0;+0:2](-[*:3])(-[O;H0;+0:4]-[*:5])-[O;H0;+0:6]-[P;H0;+0:7](=[*:8])(-[*:9])-[*:10].[OH2;+0:11].[OH2;+0:12]>>[*:5]-[OH;+0:4].[*:8]=[P;H0;+0:7](-[*:9])(-[*:10])-[OH;+0:12].[*:1]=[P;H0;+0:2](-[*:3])(-[OH;+0:6])-[OH;+0:11] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily. | Xu W, Jones CR, Dunn CA, Bessman MJ | 2004 Dec | 15576788 |
YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae. | Gao XD, Kaigorodov V, Jigami Y | 1999 Jul 23 | 10409709 |