enoyl-[acyl-carrier-protein] reductase (NADH) activity

Definition

Target type: molecularfunction

Catalysis of the reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + H+ + NADH. [RHEA:10240]

Enoyl-[acyl-carrier-protein] reductase (NADH) activity is a key enzyme involved in the biosynthesis of fatty acids. This enzyme catalyzes the reduction of a double bond in the enoyl-acyl carrier protein (ACP) substrate, using NADH as a reducing agent. The reaction proceeds in two steps:

1. **Hydration:** Water is added to the double bond of the enoyl-ACP, forming a hydroxyl group. This reaction is catalyzed by the enzyme enoyl-CoA hydratase.
2. **Reduction:** NADH donates electrons to the hydroxyl group, converting it to a saturated alkyl group. This step is catalyzed by enoyl-[acyl-carrier-protein] reductase (NADH).

The overall reaction is crucial for elongating fatty acid chains. The reductase's action ensures that each cycle of fatty acid synthesis adds two carbons to the growing chain.

Specifically, the enzyme utilizes a flavin adenine dinucleotide (FAD) cofactor to facilitate the transfer of electrons from NADH to the enoyl-ACP substrate. The FAD undergoes a redox cycle, accepting electrons from NADH and then donating them to the enoyl-ACP substrate. This process allows for the efficient reduction of the double bond and the production of a saturated fatty acid chain.

Enoyl-[acyl-carrier-protein] reductase (NADH) activity is essential for the synthesis of a variety of fatty acids, including those required for cell membranes, signaling molecules, and energy storage. Consequently, its activity is tightly regulated by various factors, including substrate availability, cellular energy status, and hormonal signals.
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Proteins (1)

Compounds (12)