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

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baruol

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

References

↑ Lodeiro, S.; Xiong, Q.; Wilson, W.K.; Kolesnikova, M.D.; Onak, C.S.; Matsuda, S.P. (2007). "An oxidosqualene cyclase makes numerous products by diverse mechanisms: a challenge to prevailing concepts of triterpene biosynthesis". J. Am. Chem. Soc. 129: 11213–11222. doi:10.1021/ja073133u. PMID 17705488.

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

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

5.4.99 Other groups	Methylmalonyl-CoA mutase Lanosterol synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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