Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.3 Acting on phosphates
ID:4.2.3.38
Description:Alpha-bisabolene synthase.
Cath: 1.10.600.10; 1.50.10.130; 1.50.10.160;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.3.38
BRENDA Enzyme Link: BRENDA 4.2.3.38
KEGG Enzyme Link: KEGG4.2.3.38
BioCyc Enzyme Link: BioCyc 4.2.3.38
ExPASy Enzyme Link: ExPASy4.2.3.38
EC2PDB Enzyme Link: EC2PDB 4.2.3.38
ExplorEnz Enzyme Link: ExplorEnz 4.2.3.38
PRIAM enzyme-specific profiles Link: PRIAM 4.2.3.38
IntEnz Enzyme Link: IntEnz 4.2.3.38
MEDLINE Enzyme Link: MEDLINE 4.2.3.38
MSA:

4.2.3.38;

Phylogenetic Tree:

4.2.3.38;

Uniprot:
M-CSA:
RHEA:25436 (2E,6E)-farnesyl diphosphate = (E,R)-alpha-bisabolene + diphosphate
RULE(radius=1) ([*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[*:5]-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[CH2;+0:9]-[*:10])>>[*:1]-[CH2;+0:2]-[CH;+0:6](-[*:5])-[C;H0;+0:7](-[*:8])=[CH;+0:9]-[*:10].[*:4]-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Terpenoid-based defenses in conifers: cDNA cloning, characterization, and functional expression of wound-inducible (E)-alpha-bisabolene synthase from grand fir (Abies grandis).Bohlmann J, Crock J, Jetter R, Croteau R1998 Jun 99618485