---
title: "Enzyme inhibition types Template – Chemistry Diagram | MolDraw"
url: https://www.moldraw.com/templates/concept-enzyme-inhibition/
description: "Enzyme inhibition types template: Competitive, uncompetitive and pure non-competitive inhibition, each with its Lineweaver–Burk lines with and without…"
lang: en
publisher: Scidart Academy
generated: 2026-11-13
---
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# Enzyme inhibition types template

![Enzyme inhibition types template: Competitive, uncompetitive and pure non-competitive inhibition, each with its Lineweaver–Burk lines with and without inhibitor, and a table of apparent Km and Vmax (α and α′ factors, mixed inhibition included).](https://www.moldraw.com/templates/concept-enzyme-inhibition.webp)

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Competitive, uncompetitive and pure non-competitive inhibition, each with its Lineweaver–Burk lines with and without inhibitor, and a table of apparent Km and Vmax (α and α′ factors, mixed inhibition included).

## What the template shows

- Reversible inhibitors told apart by their Lineweaver–Burk plots: what happens to Km and Vmax
- Lineweaver–Burk plots with and without inhibitor
- Solid: no inhibitor (Km = Vmax = 1). Dashed: with inhibitor (α or α′ = 2)
- I binds only free E, at the active site
- Km ↑ (×α), Vmax unchanged
- lines meet on the 1/v₀ axis
- I binds only the ES complex
- Km ↓ and Vmax ↓ (both ÷α′)
- parallel lines
- Non-competitive (pure)
- I binds E and ES equally (α = α′)
- Km unchanged, Vmax ↓ (÷α)
- lines meet on the 1/[S] axis
- Type Inhibitor binds Apparent Km Apparent Vmax Lineweaver–Burk lines Competitive E only αKm (↑) Vmax meet on the y-axis Uncompetitive ES only Km/α′ (↓) Vmax/α′ (↓) parallel Mixed E and ES (α ≠ α′) αKm/α′ Vmax/α′ (↓) meet off both axes Non-competitive E and ES (α = α′) Km Vmax/α (↓) meet on the x-axis
- α = 1 + [I]/Kᵢ (binding to E), α′ = 1 + [I]/Kᵢ′ (binding to ES)
- Competitive inhibition is overcome by enough substrate (Vmax unchanged): malonate on succinate dehydrogenase, methotrexate on dihydrofolate reductase.
- An uncompetitive inhibitor binds only ES, so it lowers Km and Vmax by the same factor; the slope Km/Vmax stays the same and the lines are parallel.
- Pure non-competitive inhibition is the special case of mixed inhibition with α = α′; irreversible inhibitors (e.g. DIFP on serine proteases) instead remove active enzyme.

Drawn with 256 shapes – every one editable in MolDraw.

## Sources

- [Nelson & Cox, Lehninger Principles of Biochemistry, 8th ed., 2021, ch. 6](https://openlibrary.org/isbn/9781319228002) Textbook
- [Berg, Tymoczko, Gatto & Stryer, Biochemistry, 9th ed., 2019](https://openlibrary.org/isbn/9781319114657) Textbook
- [Voet & Voet, Biochemistry, 4th ed., Wiley 2011](https://openlibrary.org/isbn/9780470570951) 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 Enzyme inhibition types template free?

You can preview the Enzyme inhibition types 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 Enzyme inhibition types 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. Pathway templates show the intermediates as structures, with enzymes and cofactors (NAD⁺, FAD, ATP) on the arrows.

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