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Partial purification and characterization of oxidosqualene-lanosterol cyclase from bakers yeast

โœ Scribed by Tsutomo Hoshino; Howard J. Williams; Yongseog Chung; A.Ian Scott

Publisher
Elsevier Science
Year
1991
Tongue
French
Weight
493 KB
Volume
47
Category
Article
ISSN
0040-4020

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โœฆ Synopsis

Partial (120-fdd) purification of oxidosqualene-lanosterol cyclase from yeast is described. The enzyme derived from the microsomal fraction converts 1 mM S-squafene oxide to lanosterd in 5 h and has a pH optimum of 6.2, lower than that (pH 7.2) of the hog-liver cyclase catalyzing the same reaction. Although the yeast cyclase is stimulated by high concentrations of potassium phosphate buffer, high concentrations of potassium or sodium chloride inhibit activity. The concentration range of Triton X-100 for optimal activity is 0.7-l .2%.

Oxidosqualene cyclase (O.S.C.) (2$epoxysqualene lanosterd-cyclase EC:1 :1:14). the enzyme which mediates the

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Oxidosqualene cyclases catalyze the biotransformation of acyclic (3S)-2,3-oxidosqualene (OS) to a variety of polycyclic sterols and triterpenoids, generating over 100 distinct triterpenoid skeletons with the formula C 30 H 50 O. [1-3, 4 and references therein] Product specificity is species-dependen