Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions

Tung-Kung Wu; Mei Ting Yu; Yuan Ting Liu; Cheng Hsian Chang; Hsing Ju Wang; Wei-Guang Diau

doi:10.1021/ol053134w

Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions

Tung-Kung Wu^*, Mei Ting Yu, Yuan Ting Liu, Cheng Hsian Chang, Hsing Ju Wang, Wei-Guang Diau

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3β-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.

Original language	English
Pages (from-to)	1319-1322
Number of pages	4
Journal	Organic Letters
Volume	8
Issue number	7
DOIs	https://doi.org/10.1021/ol053134w
State	Published - 30 Mar 2006

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@article{07986550b5254fb5a17d32a285165575,

title = "Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions",

abstract = "Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3β-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.",

author = "Tung-Kung Wu and Yu, {Mei Ting} and Liu, {Yuan Ting} and Chang, {Cheng Hsian} and Wang, {Hsing Ju} and Wei-Guang Diau",

year = "2006",

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doi = "10.1021/ol053134w",

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volume = "8",

pages = "1319--1322",

journal = "Organic Letters",

issn = "1523-7060",

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Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions. / Wu, Tung-Kung; Yu, Mei Ting; Liu, Yuan Ting; Chang, Cheng Hsian; Wang, Hsing Ju; Diau, Wei-Guang.

In: Organic Letters, Vol. 8, No. 7, 30.03.2006, p. 1319-1322.

Research output: Contribution to journal › Article › peer-review

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AU - Wu, Tung-Kung

AU - Yu, Mei Ting

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AU - Chang, Cheng Hsian

AU - Wang, Hsing Ju

AU - Diau, Wei-Guang

PY - 2006/3/30

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N2 - Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3β-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.

AB - Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3β-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.

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