Protonation state and fine structure of the active site determine the reactivity of dehydratase: hydration and isomerization of β-myrcene catalyzed by linalool dehydratase/isomerase from Castellaniella defragrans-Reference-Cited by-同舟云学术

Protonation state and fine structure of the active site determine the reactivity of dehydratase: hydration and isomerization of β-myrcene catalyzed by linalool dehydratase/isomerase from Castellaniella defragrans

Published:2018 Issue:25 Volume:20 Page:17342-17352
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ling Baoping¹²³⁴⁵^ORCID,Wang Xiya⁵⁶⁷⁴^ORCID,Su Hao⁵⁶⁷⁴,Liu Rutao⁵⁶⁷⁴^ORCID,Liu Yongjun⁵⁶⁷⁴^ORCID

Affiliation:

1. School of Chemistry and Chemical Engineering

2. Qufu Normal University

3. Qufu

4. China

5. School of Chemistry and Chemical Engineering & Environmental Science and Engineering

6. Shandong University

7. Jinan

Abstract

Linalool dehydratase/isomerase (LinD) from Castellaniella defragrans is a bifunctional enzyme that catalyzes the hydration of β-myrcene to (S)-linalool and isomerization of (S)-linalool to geraniol.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C8CP02362J

Reference51 articles.

1. Linalool Dehydratase-Isomerase, a Bifunctional Enzyme in the Anaerobic Degradation of Monoterpenes

2. H. E. M. Dobson , in Insect-Plant Interactions , ed. E. Bernays , CRC Press , Boca Raton, FL , 1994 , vol. V, pp. 47–81

3. Floral scents—a checklist of volatile compounds isolated by head-space techniques