enoyl-[acyl-carrier-protein] reductase (NADH)
NADH-enoyl acyl carrier protein reductase
acyl-[acyl-carrier-protein]:NAD+ oxidoreductase
trans-2,3-Dehydroacyl-[acyl-carrier protein]
Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase.
Crystallization of the NADH-specific enoyl acyl carrier protein reductase from Brassica napus.
Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-382.
Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase.
A mechanism of drug action revealed by structural studies of enoyl reductase.
Evidence for the essential histidine at the NADPH binding site of enoyl-CoA reductase domain of pigeon liver fatty acid synthetase.
The X-ray structure of Escherichia coli enoyl reductase with bound NAD+ at 2.1 A resolution.
Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis.
Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis.
Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan.
Mechanism of triclosan inhibition of bacterial fatty acid synthesis.
Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition.
Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 84-380.
Crystallographic analysis of triclosan bound to enoyl reductase.
Structural basis and mechanism of enoyl reductase inhibition by triclosan.
Molecular genetic analysis of enoyl-acyl carrier protein reductase inhibition by diazaborine.
Molecular basis for triclosan activity involves a flipping loop in the active site.
Kinetic mechanism of NADH-enoyl-ACP reductase from Brassica napus.
1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI).
A study of the structure-activity relationship for diazaborine inhibition of Escherichia coli enoyl-ACP reductase.
Can an optimization/scoring procedure in ligand-protein docking be employed to probe drug-resistant mutations in proteins?
Characterization of a novel enoyl-acyl carrier protein reductase of diazaborine-resistant Rhodobacter sphaeroides mutant.
Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase.
Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI).
Targeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data.
Exploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases.
Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK.
Role of inhibitor aliphatic chain in the thermodynamics of inhibitor binding to Escherichia coli enoyl-ACP reductase and the Phe203Leu mutant: a proposed mechanism for drug resistance.
Structural basis for the variation in triclosan affinity to enoyl reductases.