Crystal structure of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB) in complex with the inhibitor O-isobutenyl oxalylhydroxamate.
3-Isopropylmalate dehydrogenase
Crystal structure
Haemophilus influenzae
Inhibitor
Leucine biosynthesis
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
16 04 2020
16 04 2020
Historique:
received:
29
01
2020
accepted:
04
02
2020
pubmed:
16
2
2020
medline:
27
10
2020
entrez:
16
2
2020
Statut:
ppublish
Résumé
3-isopropylmalate dehydrogenases (LeuB) belong to the leucine biosynthetic pathway and catalyze the irreversible oxidative decarboxylation of 3IPM to 2-ketoisocaproate that is finally converted into leucine by a branched-chain aminotransferase. Since leucine is an essential amino acid for humans, and it is also vital for the growth of many pathogenic bacteria, the enzymes belonging to this pathway can be considered as potential target sites for designing of a new class of antibacterial agents. We have determined the crystal structure of the Haemophilus influenzae LeuB in complex with the cofactor NAD
Identifiants
pubmed: 32059844
pii: S0006-291X(20)30288-6
doi: 10.1016/j.bbrc.2020.02.022
pii:
doi:
Substances chimiques
Enzyme Inhibitors
0
Hydroxamic Acids
0
3-Isopropylmalate Dehydrogenase
EC 1.1.1.85
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
996-1002Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.