Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae

Tung-Kung Wu; Wen Hsuan Li; Cheng Hsiang Chang; Hao Yu Wen; Yuan Ting Liu; Yi Chun Chang

doi:10.1002/ejoc.200900638

Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae

Tung-Kung Wu^*, Wen Hsuan Li, Cheng Hsiang Chang, Hao Yu Wen, Yuan Ting Liu, Yi Chun Chang

^*Corresponding author for this work

Department of Biological Science and Technology

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

15 Scopus citations

Abstract

The function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion, and site-saturated mutants. Two truncated intermediates, (13αH)- isomalabarica-14Z,17E,21-trien-3βol and. (13α\H)-isomalabarica-14Z, 17.E,21.-trien-3β-ol, were isolated from the ERG7^Y99X mutants. These results suggest that the functional role of ERG7^Y99 is to affect both chair-boat 6-65 tricyclic Markovnikov C-14 cation stabilization and the stereochemistry of the protons at the C-15 position for subsequent deprotonation.

Original language	English
Pages (from-to)	5731-5737
Number of pages	7
Journal	European Journal of Organic Chemistry
Issue number	33
DOIs	https://doi.org/10.1002/ejoc.200900638
State	Published - 1 Dec 2009

Keywords

Cyclization
Enzymes
Mutagenesis
Reaction mechanisms
Terpenoids

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@article{238a033bc58b446eb140f3f7e6b23de5,

title = "Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae",

abstract = "The function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion, and site-saturated mutants. Two truncated intermediates, (13αH)- isomalabarica-14Z,17E,21-trien-3βol and. (13α\H)-isomalabarica-14Z, 17.E,21.-trien-3β-ol, were isolated from the ERG7Y99X mutants. These results suggest that the functional role of ERG7Y99 is to affect both chair-boat 6-65 tricyclic Markovnikov C-14 cation stabilization and the stereochemistry of the protons at the C-15 position for subsequent deprotonation.",

keywords = "Cyclization, Enzymes, Mutagenesis, Reaction mechanisms, Terpenoids",

author = "Tung-Kung Wu and Li, {Wen Hsuan} and Chang, {Cheng Hsiang} and Wen, {Hao Yu} and Liu, {Yuan Ting} and Chang, {Yi Chun}",

year = "2009",

month = dec,

day = "1",

doi = "10.1002/ejoc.200900638",

language = "English",

pages = "5731--5737",

journal = "European Journal of Organic Chemistry",

issn = "1434-193X",

publisher = "Wiley-VCH Verlag",

number = "33",

}

Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae. / Wu, Tung-Kung; Li, Wen Hsuan; Chang, Cheng Hsiang; Wen, Hao Yu; Liu, Yuan Ting; Chang, Yi Chun.

In: European Journal of Organic Chemistry, No. 33, 01.12.2009, p. 5731-5737.

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

TY - JOUR

T1 - Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae

AU - Wu, Tung-Kung

AU - Li, Wen Hsuan

AU - Chang, Cheng Hsiang

AU - Wen, Hao Yu

AU - Liu, Yuan Ting

AU - Chang, Yi Chun

PY - 2009/12/1

Y1 - 2009/12/1

N2 - The function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion, and site-saturated mutants. Two truncated intermediates, (13αH)- isomalabarica-14Z,17E,21-trien-3βol and. (13α\H)-isomalabarica-14Z, 17.E,21.-trien-3β-ol, were isolated from the ERG7Y99X mutants. These results suggest that the functional role of ERG7Y99 is to affect both chair-boat 6-65 tricyclic Markovnikov C-14 cation stabilization and the stereochemistry of the protons at the C-15 position for subsequent deprotonation.

AB - The function of the Tyr99 residue from Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase (ERG7) was analyzed by constructing deletion, and site-saturated mutants. Two truncated intermediates, (13αH)- isomalabarica-14Z,17E,21-trien-3βol and. (13α\H)-isomalabarica-14Z, 17.E,21.-trien-3β-ol, were isolated from the ERG7Y99X mutants. These results suggest that the functional role of ERG7Y99 is to affect both chair-boat 6-65 tricyclic Markovnikov C-14 cation stabilization and the stereochemistry of the protons at the C-15 position for subsequent deprotonation.

KW - Cyclization

KW - Enzymes

KW - Mutagenesis

KW - Reaction mechanisms

KW - Terpenoids

UR - http://www.scopus.com/inward/record.url?scp=72849119293&partnerID=8YFLogxK

U2 - 10.1002/ejoc.200900638

DO - 10.1002/ejoc.200900638

M3 - Article

AN - SCOPUS:72849119293

SP - 5731

EP - 5737

JO - European Journal of Organic Chemistry

JF - European Journal of Organic Chemistry

SN - 1434-193X

IS - 33

ER -

Differential stereocontrolled formation of tricyclic triterpenes by mutation of tyrosine 99 of the oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae

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Keywords

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