EC number:4.2.3.55

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.3 Acting on phosphates
ID:4.2.3.55
Description:(S)-beta-bisabolene synthase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.3.55
BRENDA Enzyme Link: BRENDA 4.2.3.55
KEGG Enzyme Link: KEGG4.2.3.55
BioCyc Enzyme Link: BioCyc 4.2.3.55
ExPASy Enzyme Link: ExPASy4.2.3.55
EC2PDB Enzyme Link: EC2PDB 4.2.3.55
ExplorEnz Enzyme Link: ExplorEnz 4.2.3.55
PRIAM enzyme-specific profiles Link: PRIAM 4.2.3.55
IntEnz Enzyme Link: IntEnz 4.2.3.55
MEDLINE Enzyme Link: MEDLINE 4.2.3.55

EC number:4.2.3.55

MSA:

4.2.3.55;
Phylogenetic Tree:

4.2.3.55;
Uniprot:
M-CSA:
RHEA:28266 (2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene + diphosphate
RULE(radius=1) ([*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[*:5]-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[CH3;+0:9])>>[*:1]-[CH2;+0:2]-[CH;+0:6](-[*:5])-[C;H0;+0:7](-[*:8])=[CH2;+0:9].[*:4]-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Protonation of a neutral (S)-beta-bisabolene intermediate is involved in (S)-beta-macrocarpene formation by the maize sesquiterpene synthases TPS6 and TPS11.Köllner TG, Schnee C, Li S, Svatos A, Schneider B, Gershenzon J, Degenhardt J2008 Jul 2518524777