EC Tree |
3. Hydrolases |
3.1 Acting on ester bonds |
3.1.7 Diphosphoric-monoester hydrolases |
ID: | 3.1.7.8 |
---|---|
Description: | Tuberculosinol synthase. |
Cath: | 3.40.1180.10; |
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 3.1.7.8 |
BRENDA Enzyme Link: | BRENDA 3.1.7.8 |
KEGG Enzyme Link: | KEGG3.1.7.8 |
BioCyc Enzyme Link: | BioCyc 3.1.7.8 |
ExPASy Enzyme Link: | ExPASy3.1.7.8 |
EC2PDB Enzyme Link: | EC2PDB 3.1.7.8 |
ExplorEnz Enzyme Link: | ExplorEnz 3.1.7.8 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.1.7.8 |
IntEnz Enzyme Link: | IntEnz 3.1.7.8 |
MEDLINE Enzyme Link: | MEDLINE 3.1.7.8 |
RHEA:31783 | H2O + tuberculosinyl diphosphate = diphosphate + tuberculosinol |
RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]-[P;H0;+0:3](=[*:5])(-[*:6])-[OH;+0:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structure and inhibition of tuberculosinol synthase and decaprenyl diphosphate synthase from Mycobacterium tuberculosis. | Chan HC, Feng X, Ko TP, Huang CH, Hu Y, Zheng Y, Bogue S, Nakano C, Hoshino T, Zhang L, Lv P, Liu W, Crick DC, Liang PH, Wang AH, Oldfield E, Guo RT | 2014 Feb 19 | 24475925 |
Substrate specificity of Rv3378c, an enzyme from Mycobacterium tuberculosis, and the inhibitory activity of the bicyclic diterpenoids against macrophage phagocytosis. | Hoshino T, Nakano C, Ootsuka T, Shinohara Y, Hara T | 2011 Apr 7 | 21290071 |
Characterization of the Rv3378c gene product, a new diterpene synthase for producing tuberculosinol and (13R, S)-isotuberculosinol (nosyberkol), from the Mycobacterium tuberculosis H37Rv genome. | Nakano C, Ootsuka T, Takayama K, Mitsui T, Sato T, Hoshino T | 2011 | 21228491 |