Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline (S)-2,3-epoxysqualene Identifier CHEBI:15441 Charge 0 Formula C30H50O InChIKeyhelp_outline QYIMSPSDBYKPPY-RSKUXYSASA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C=C(/C)CC\C=C(/C)CC[C@@H]1OC1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 31 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline camelliol C Identifier CHEBI:62452 Charge 0 Formula C30H50O InChIKeyhelp_outline CIDHBCQEXDUWEB-HJSIMFEZSA-N SMILEShelp_outline CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C=C(/C)CC[C@@H]1C(C)=CC[C@H](O)C1(C)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:31011 | RHEA:31012 | RHEA:31013 | RHEA:31014 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Arabidopsis camelliol C synthase evolved from enzymes that make pentacycles.
Kolesnikova M.D., Wilson W.K., Lynch D.A., Obermeyer A.C., Matsuda S.P.T.
We establish by heterologous expression that the Arabidopsis thaliana oxidosqualene cyclase At1g78955 (CAMS1) makes camelliol C (98%), achilleol A (2%), and beta-amyrin (0.2%). CAMS1 is the first characterized cyclase that generates predominantly a monocyclic triterpene alcohol. Phylogenetic analy ... >> More
We establish by heterologous expression that the Arabidopsis thaliana oxidosqualene cyclase At1g78955 (CAMS1) makes camelliol C (98%), achilleol A (2%), and beta-amyrin (0.2%). CAMS1 is the first characterized cyclase that generates predominantly a monocyclic triterpene alcohol. Phylogenetic analysis shows that CAMS1 evolved from enzymes that make pentacycles, thus revealing that its pentacyclic beta-amyrin byproduct is an evolutionary relic. Sequence alignments support prior suggestions that decreased steric bulk at a key active-site residue promotes monocycle formation. << Less