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-Reference-Cited by-同舟云学术

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

Published:1997-02-01 Issue:6 Volume:119 Page:1289-1296
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Corey E. J.¹,Cheng Hengmiao¹,Baker C. Hunter¹,Matsuda Seiichi P. T.¹,Li Ding¹,Song Xuelei¹

Affiliation:

1. Contribution from the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja963228o

Reference19 articles.

1. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes

2. 2,3-Iminosqualene, a potent inhibitor of the enzymic cyclization of 2,3-oxidosqualene to sterols

3. An experimental demonstration of the stereochemistry of enzymic cyclization of 2,3-oxidosqualene to the protosterol system, forerunner of lanosterol and cholesterol

4. New mechanistic and stereochemical insights on the biosynthesis of sterols from 2,3-oxidosqualene

5. The methyl group at C(10) of 2,3-oxidosqualene is crucial to the correct folding of this substrate in the cyclization-rearrangement step of sterol biosynthesis

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