--- title: "NAD⁺ hydride transfer (alcohol dehydrogenase) Template | MolDraw" url: https://www.moldraw.com/templates/enzyme-adh-hydride-transfer/ description: "NAD⁺ hydride transfer (alcohol dehydrogenase) template: In liver alcohol dehydrogenase ethanol binds to the catalytic Zn²⁺, loses its proton (relayed to…" lang: en publisher: Scidart Academy generated: 2026-11-13 --- [MolDraw](https://www.moldraw.com/) › [Templates](https://www.moldraw.com/templates/) › [Biochemistry](https://www.moldraw.com/templates/biochemistry/) › NAD⁺ hydride transfer (alcohol dehydrogenase) [Biochemistry](https://www.moldraw.com/templates/biochemistry/)Premium # NAD⁺ hydride transfer (alcohol dehydrogenase) template ![NAD⁺ hydride transfer (alcohol dehydrogenase) template: In liver alcohol dehydrogenase ethanol binds to the catalytic Zn²⁺, loses its proton (relayed to His51), and the alkoxide transfers a hydride ion to C4 of NAD⁺, giving acetaldehyde and NADH.](https://www.moldraw.com/templates/enzyme-adh-hydride-transfer.webp) [Edit in MolDraw](https://www.moldraw.com/)Download with Pro Premium template. Preview and edit it free in MolDraw; downloading and exporting it is part of [MolDraw Pro](https://www.moldraw.com/pricing). In liver alcohol dehydrogenase ethanol binds to the catalytic Zn²⁺, loses its proton (relayed to His51), and the alkoxide transfers a hydride ion to C4 of NAD⁺, giving acetaldehyde and NADH. ## Mechanism step by step A Zn²⁺-bound alkoxide gives a hydride to C4 of the nicotinamide ring: ethanol → acetaldehyde, NAD⁺ → NADH 1. **Alkoxide formation** – Zn²⁺ lowers the pKa of bound ethanol; the proton is relayed (Ser48, ribose 2′-OH) to His51 2. **Hydride transfer** – C=O forms as H⁻ moves to C4 of the nicotinamide; the ring N⁺ takes the electrons ## Key points - The hydride (H⁻: a proton and two electrons) goes to C4, para to the ring nitrogen; the positive charge of NAD⁺ is the electron sink. - Transfer is stereospecific: ADH is an A-side (pro-R) dehydrogenase, so NADH carries the transferred H on a defined face of C4. - Zn²⁺ (bound to Cys46, His67 and Cys174 in horse liver ADH) is a Lewis acid that holds and polarises the substrate oxygen. - In yeast fermentation the reaction runs backwards (acetaldehyde + NADH → ethanol), regenerating NAD⁺ for glycolysis. Drawn with 73 atoms, 9 arrows, 6 shapes – every one editable in MolDraw. ## Sources - [Nelson & Cox, Lehninger Principles of Biochemistry, 8th ed., 2021, ch. 14](https://openlibrary.org/isbn/9781319228002) Textbook - [Berg, Tymoczko, Gatto & Stryer, Biochemistry, 9th ed., 2019, ch. 16](https://openlibrary.org/isbn/9781319114657) Textbook ## How to use this template 1. Press **Edit in MolDraw**. The template opens on the canvas of the free MolDraw editor. 2. Change anything: move structures, edit atoms and labels, recolour highlights or delete what you do not need. 3. Add your own structures, arrows and text next to it, or combine several templates on one page. 4. Export the drawing as PNG, SVG or PDF for slides, worksheets, theses and papers. ## Frequently asked questions ### Is the NAD⁺ hydride transfer (alcohol dehydrogenase) template free? You can preview the NAD⁺ hydride transfer (alcohol dehydrogenase) template here and open and edit it in MolDraw for free. Downloading or exporting it is part of MolDraw Pro, together with the other premium templates. ### Can I edit the NAD⁺ hydride transfer (alcohol dehydrogenase) template? Yes. It opens as an ordinary MolDraw drawing, so every structure, arrow, label and colour can be changed, and you can add your own content around it. ### Is the chemistry checked? Every structure is checked with RDKit and every curly arrow passes MolDraw’s electron-flow audit. The sources used are listed on this page. ### Are the biochemical pathways drawn with structures? Yes. 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