Baruol synthase

Baruol synthase (EC 5.4.99.57, BARS1) is an enzyme with systematic name (3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, baruol-forming).^[1] This enzyme catalyses the following chemical reaction

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

\rightleftharpoons

baruol

The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids.

References[]

^ Lodeiro S, Xiong Q, Wilson WK, Kolesnikova MD, Onak CS, Matsuda SP (September 2007). "An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis". Journal of the American Chemical Society. 129 (36): 11213–22. doi:10.1021/ja073133u. PMID 17705488.

Baruol+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)

v t 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	Methylmalonyl-CoA mutase Lanosterol synthase Lupeol synthase

v t Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme 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)