(Q45127007)

English

Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae

scientific article published in December 2004

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

Saccharomyces cerevisiae

1 reference

based on heuristic

inferred from title

author name string

Tung-Kung Wu

1

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

Cheng-Hsiang Chang

2

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

publication date

1 December 2004

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

1712-1715

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

Beta-amyrin synthase--cloning of oxidosqualene cyclase that catalyzes the formation of the most popular triterpene among higher plants

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Steric bulk at position 454 in Saccharomyces cerevisiae lanosterol synthase influences B-ring formation but not deprotonation

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Conversion of a plant oxidosqualene-cycloartenol synthase to an oxidosqualene-lanosterol cyclase by random mutagenesis

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Conversion of squalene to the pentacarbocyclic hopene

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Studies on the Substrate Binding Segments and Catalytic Action of Lanosterol Synthase. Affinity Labeling with Carbocations Derived from Mechanism-Based Analogs of 2,3-Oxidosqualene and Site-Directed Mutagenesis Probes

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Functional analyses of Tyr420 and Leu607 of Alicyclobacillus acidocaldarius squalene-hopene cyclase. Neoachillapentaene, a novel triterpene with the 1,5,6-trimethylcyclohexene moiety produced through folding of the constrained boat structure

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Mechanistic insights into oxidosqualene cyclizations through homology modeling

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis

1 reference

https://api.crossref.org/works/10.1002%2FCBIC.200400079

21 January 2018

Identifiers

10.1002/CBIC.200400079

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 December 2017

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