Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.
Acyl Coenzyme A
/ metabolism
Acyl-CoA Dehydrogenase
/ chemistry
Anti-Bacterial Agents
/ pharmacology
Bacterial Proteins
/ chemistry
Binding Sites
Catalytic Domain
Drug Resistance, Bacterial
/ genetics
Fatty Acids
/ chemistry
Models, Molecular
Mutation
Mycobacterium
/ drug effects
Protein Conformation
Structure-Activity Relationship
Substrate Specificity
acyl-CoA dehydrogenase
fatty acid
mycobacteria
tuberculosis
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
14 07 2020
14 07 2020
Historique:
pubmed:
1
7
2020
medline:
24
9
2020
entrez:
1
7
2020
Statut:
ppublish
Résumé
FadE, an acyl-CoA dehydrogenase, introduces unsaturation to carbon chains in lipid metabolism pathways. Here, we report that FadE5 from
Identifiants
pubmed: 32601219
pii: 2002835117
doi: 10.1073/pnas.2002835117
pmc: PMC7368279
doi:
Substances chimiques
Acyl Coenzyme A
0
Anti-Bacterial Agents
0
Bacterial Proteins
0
Fatty Acids
0
Acyl-CoA Dehydrogenase
EC 1.3.8.7
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
16324-16332Déclaration de conflit d'intérêts
The authors declare no competing interest.
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