Cofactors

There are no Cofactors for this Enzyme

Reaction Mechanism

enoyl-[acyl-carrier-protein] reductase (NADH) By Reference

Enoyl ACP reductase catalyses the last step in fatty acid biosynthesis. Therefore it is a potential target for antibacterial agent development. It catalyses the NAD(P)H-dependent reduction of enoyl acyl carrier protein.

The bacterial form of the enzyme is different from the human form as it exists as a free globular protein rather than a part of a multienzyme complex. EACPR's show homology, and similarity to hydroxysteroid dehydrogenase, and also beta-keto reductase, suggesting divergent evolution has played a role in the development of the pathway of lipid biosynthesis.




• Summary
• Step 1
• Step 2
• Products

The catalytic mechanism involves C3 of the substrate being subject to hydride attack by NADH, a bound cofactor. Formation of an enolate intermediate follows, which accepts a proton from Tyr 156. A role in transition state stabilisation through hydrogen bonding has also been suggested for Tyr 156. The enol product would then tautomerise to give the reduced acyl product. Tyr 156 therefore acts as the base that donates the proton to the enolate anion, and Lys 163 acts to stabilise the negatively charged transition state.

Catalytic Residues

AA	Uniprot	Uniprot Resid	PDB	PDB Resid
Tyr	P0AEK4	156	1qsg	159
Lys	P0AEK4	163	1qsg	166

Step Components

overall reactant used, proton transfer, overall product formed, native state of enzyme regenerated, keto-enol tautomerisation, cofactor used, hydride transfer, michael addition



Step 1.

C3 of the substrate is attacked by a hydride from NADH, forming an enolate and NAD. The oxygen of the enolate is protonated by Tyr156 resulting in an enol.



Step 2.

The enol tautomerises to form the product.



Products.

The products of the reaction.

View Reaction Mechanisms in M-CSA

Reaction Parameters

There are no kinetic parameters information for this Enzyme

Associated Proteins

Citations

• Synthesis and evaluation of phenylimidazole FabK inhibitors as new Anti-C. Difficile agents.
• Structure-based identification of novel inhibitors targeting the enoyl-ACP reductase enzyme of Acinetobacter baumannii.
• Facing Antitubercular Resistance: Identification of Potential Direct Inhibitors Targeting InhA Enzyme and Generation of 3D-pharmacophore Model by in silico Approach.
• Integrative transcriptome and proteome revealed high-yielding mechanisms of epsilon-poly-L-lysine by Streptomyces albulus.
• Mapping the castor bean endosperm proteome revealed a metabolic interaction between plastid, mitochondria, and peroxisomes to optimize seedling growth.
• Genomic analysis of the marine yeast Rhodotorula sphaerocarpa ETNP2018 reveals adaptation to the open ocean.
• Structure-based drug design of novel M. tuberculosis InhA inhibitors based on fragment molecular orbital calculations.
• Biotechnological production of omega-3 fatty acids: current status and future perspectives.
• Do Go Chasing Waterfalls: Enoyl Reductase (FabI) in Complex with Inhibitors Stabilizes the Tetrameric Structure and Opens Water Channels.
• Mitochondria-derived vesicles and their potential roles in kidney stone disease.
• An optimized reverse β-oxidation pathway to produce selected medium-chain fatty acids in Saccharomyces cerevisiae.