Camelliol C synthase

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Camelliol C synthase
Camelliol C synthase
Identifiers
EC no.	5.4.99.38
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PubMed	articles
NCBI	proteins

Last updated September 22, 2024

Camelliol C synthase (EC 5.4.99.38, CAMS1, LUP3 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, camelliol-C-forming).^[1] This enzyme catalyses the following chemical reaction

(3S)-2,3-epoxy-2,3-dihydrosqualene

\rightleftharpoons

camelliol C

The product is mainly camelliol.

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Lupan-3β,20-diol synthase (EC 4.2.1.128, LUP1 (gene)) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene hydro-lyase (lupan-3beta,20-diol forming). This enzyme catalyses the following chemical reaction

Thalianol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

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Taraxerol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Isomultiflorenol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualenee mutase . It catalyses the chemical reaction:

α-Amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Parkeol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Achilleol B synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Glutinol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Friedelin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Baccharis oxide synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

α-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Marneral synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase. This enzyme catalyses the following chemical reaction

β-seco-amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

δ-Amyrin synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

Baruol synthase is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase . This enzyme catalyses the following chemical reaction

References

↑ Kolesnikova MD, Wilson WK, Lynch DA, Obermeyer AC, Matsuda SP (December 2007). "Arabidopsis camelliol C synthase evolved from enzymes that make pentacycles". Organic Letters. 9 (25): 5223–6. doi:10.1021/ol702399g. PMID 17985917.

External links

Camelliol+C+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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[1] Kolesnikova MD, Wilson WK, Lynch DA, Obermeyer AC, Matsuda SP (December 2007). "Arabidopsis camelliol C synthase evolved from enzymes that make pentacycles". Organic Letters. 9 (25): 5223–6. doi:10.1021/ol702399g. PMID 17985917.

[1]

v t e Isomerase: mutases (EC 5.4)
5.4.1 Acyl Groups	Lysolecithin acylmutase Precorrin-8X methylmutase
5.4.2 Phosphomutases	Phosphoglycerate mutase Bisphosphoglycerate mutase Phosphoglucomutase Phosphomannomutase PMM1 PMM2 Phosphoenolpyruvate mutase
5.4.99 Other groups	Cycloartenol synthase Lanosterol synthase Lupeol synthase Methylmalonyl-CoA mutase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)