Kinetics and thermodynamics of enzymatic decarboxylation of α,β-unsaturated acid: a theoretical study-Reference-Cited by-同舟云学术

Kinetics and thermodynamics of enzymatic decarboxylation of α,β-unsaturated acid: a theoretical study

Published:2022 Issue:22 Volume:12 Page:14223-14234
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Promma Phorntep¹,Lao-ngam Charoensak²,Lai Rung-Yi¹^ORCID,Sagarik Kritsana¹^ORCID

Affiliation:

1. School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand

2. Chemistry Program, Faculty of Science and Technology, Nakhon Ratchasima Rajabhat University, Nakhon Ratchasima 30000, Thailand

Abstract

The kinetically controlled path for enzymatic decarboxylation of α,β-unsaturated acid is proposed based on DFT and TST methods. The mechanism involves fluctuation of the local dielectric environment in the active site of the FDC1 enzyme.

Funder

Suranaree University of Technology

Thailand Science Research and Innovation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/RA/D2RA02626K

Reference25 articles.

1. New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition

2. Decarboxylation mechanisms in biological system

3. Mechanism of the Novel Prenylated Flavin-Containing Enzyme Ferulic Acid Decarboxylase Probed by Isotope Effects and Linear Free-Energy Relationships

4. Evidence for a 1,3-Dipolar Cyclo-addition Mechanism in the Decarboxylation of Phenylacrylic Acids Catalyzed by Ferulic Acid Decarboxylase

5. The Decarboxylation of α,β-Unsaturated Acid Catalyzed by Prenylated FMN-Dependent Ferulic Acid Decarboxylase and the Enzyme Inhibition

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