Enzyme

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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;

3D structure

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References

External Links

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
MSA:

3.1.7.8;

Phylogenetic Tree:

3.1.7.8;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed 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 RT2014 Feb 1924475925
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 T2011 Apr 721290071
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 T201121228491