QM/MM Study of the Reaction Mechanism of the Dehydratase Domain from Mammalian Fatty Acid Synthase-Reference-Cited by-同舟云学术

QM/MM Study of the Reaction Mechanism of the Dehydratase Domain from Mammalian Fatty Acid Synthase

Published:2018-10-08 Issue:11 Volume:8 Page:10267-10278
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Medina Fabiola E.¹^ORCID,Neves Rui P. P.¹^ORCID,Ramos Maria J.¹^ORCID,Fernandes Pedro A.¹

Affiliation:

1. UCIBIO, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007 Porto, Portugal

Funder

European Regional Development Fund

Comisi?n Nacional de Investigaci?n Cient?fica y Tecnol?gica

Funda??o para a Ci?ncia e a Tecnologia

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.8b02616

Reference76 articles.

1. The type I fatty acid and polyketide synthases: a tale of two megasynthases

2. The Crystal Structure of a Mammalian Fatty Acid Synthase

3. Modeling of Human Fatty Acid Synthase and in Silico Docking of Acyl Carrier Protein Domain and Its Partner Catalytic Domains

4. β-Hydroxyacyl-acyl Carrier Protein Dehydratase (FabZ) from Francisella tularensis and Yersinia pestis: Structure Determination, Enzymatic Characterization, and Cross-Inhibition Studies

5. Crystal structure of FabZ-ACP complex reveals a dynamic seesaw-like catalytic mechanism of dehydratase in fatty acid biosynthesis

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