ID: | 4.2.3.138 |
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Description: | (+)-epi-alpha-bisabolol synthase. |
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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 4.2.3.138 |
BRENDA Enzyme Link: | BRENDA 4.2.3.138 |
KEGG Enzyme Link: | KEGG4.2.3.138 |
BioCyc Enzyme Link: | BioCyc 4.2.3.138 |
ExPASy Enzyme Link: | ExPASy4.2.3.138 |
EC2PDB Enzyme Link: | EC2PDB 4.2.3.138 |
ExplorEnz Enzyme Link: | ExplorEnz 4.2.3.138 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.2.3.138 |
IntEnz Enzyme Link: | IntEnz 4.2.3.138 |
MEDLINE Enzyme Link: | MEDLINE 4.2.3.138 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:34503 | (2E,6E)-farnesyl diphosphate + H2O = (+)-epi-alpha-bisabolol + diphosphate |
RULE(radius=1) | ([*:1]-[CH2;+0:2]-[O;H0;+0:3]-[*:4].[*:5]-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[*:9]).[OH2;+0:10]>>[*:1]-[CH2;+0:2]-[CH;+0:6](-[*:5])-[C;H0;+0:7](-[*:8])(-[*:9])-[OH;+0:10].[*:4]-[OH;+0:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Molecular cloning and characterization of (+)-epi-α-bisabolol synthase, catalyzing the first step in the biosynthesis of the natural sweetener, hernandulcin, in Lippia dulcis. | Attia M, Kim SU, Ro DK | 2012 Nov 1 | 22867794 |