Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions.
作者信息
Wu Tung-Kung, Liu Yuan-Ting, Chang Cheng-Hsian
机构信息
Department of Biological Science and Technology, Center for Interdisciplinary Molecular Science, National Chiao Tung University, 300 Hsin-Chu, Taiwan, Republic of China.
出版信息
Chembiochem. 2005 Jul;6(7):1177-81. doi: 10.1002/cbic.200500084.
PMID:15915534
Abstract
摘要
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Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions.来自酿酒酵母的氧化角鲨烯-羊毛甾醇环化酶第234位的组氨酸残基同时影响环化、重排和去质子化反应。
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Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions.来自酿酒酵母的氧化角鲨烯-羊毛甾醇环化酶中的色氨酸232影响重排和去质子化反应，但不影响环化反应。
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Alteration of the substrate's prefolded conformation and cyclization stereochemistry of oxidosqualene-lanosterol cyclase of Saccharomyces cerevisiae by substitution at phenylalanine 699.通过取代酵母麦角固醇环化酶的苯丙氨酸 699 来改变底物的预折叠构象和环化立体化学。
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The cysteine 703 to isoleucine or histidine mutation of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae generates an iridal-type triterpenoid.来自酿酒酵母的角鲨烯-羊毛甾醇环化酶的半胱氨酸 703 异亮氨酸或组氨酸突变产生了一种艾杜醇型三萜。
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Mutation of isoleucine 705 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae affects lanosterol's C/D-ring cyclization and 17α/β-exocyclic side chain stereochemistry.酵母氧化鲨烯-羊毛甾醇环化酶的异亮氨酸 705 突变影响羊毛甾醇的 C/D 环环化和 17α/β-外环侧链立体化学。
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