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spinqualitylabelsall models Enoyl-ACP Reductase InhA Homotetramer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 Introduction 1.1 FAS-II System 1.2 Mechanism of Action 2 Structure 2.1 Fatty Acyl Binding Crevice 2.2 Catalytic Triad 2.3 Hydrogen Bonding Interactions 3 Clinical Applications

Introduction

FAS-II System

Mechanism of Action

Structure

Crystal structures of InhA reveal a (each subunit featured with a different color) with separate ligand binding sites in each subunit. Each subunit features a single domain with a central core that supports a NADH binding site. The alpha6 and alpha7 helices of the monomer form one side of the fatty acyl substrate binding crevice of InhA. Within this binding crevice, many hydrophobic side chains from the amino acids involved in forming the substrate binding loop, , interact with the substrates. One side of this cavity is open and exposed to solvent, which allows the substrates to access the binding pocket of this enzyme. The size of the substrate binding loop is a primary determinant of the ability of InhA to distinguish between shorter and longer substrates and provide for the enoyl-ACP reductase reaction.

Fatty Acyl Binding Crevice

In the substrate binding pocket, NADH sits on the top shelf of the fold, and the fatty acyl substrate sits on top of NADH. Both molecules are held in place by interactions with amino acid residues in the substrate binding loop.

Catalytic Triad

Hydrogen Bonding Interactions

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Clinical Applications

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