---
title: "Biotin carboxylation (acetyl-CoA carboxylase) Template | MolDraw"
url: https://www.moldraw.com/templates/enzyme-biotin-carboxylation/
description: "Biotin carboxylation (acetyl-CoA carboxylase) template: Bicarbonate attacks the γ-phosphate of ATP to form carboxyphosphate, which gives CO₂ and phosphate…"
lang: en
publisher: Scidart Academy
generated: 2026-11-13
---
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# Biotin carboxylation (acetyl-CoA carboxylase) template

![Biotin carboxylation (acetyl-CoA carboxylase) template: Bicarbonate attacks the γ-phosphate of ATP to form carboxyphosphate, which gives CO₂ and phosphate; N1′ of biotin (on a Lys) takes up the CO₂, and in the carboxyltransferase site carboxybiotin releases CO₂ to the enolate of acetyl-CoA, giving malonyl-CoA.](https://www.moldraw.com/templates/enzyme-biotin-carboxylation.webp)

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Bicarbonate attacks the γ-phosphate of ATP to form carboxyphosphate, which gives CO₂ and phosphate; N1′ of biotin (on a Lys) takes up the CO₂, and in the carboxyltransferase site carboxybiotin releases CO₂ to the enolate of acetyl-CoA, giving malonyl-CoA.

## Mechanism step by step

ATP activates bicarbonate as carboxyphosphate; biotin carries the CO₂ to acetyl-CoA, giving malonyl-CoA

1. **Carboxyphosphate** – Bicarbonate attacks the γ-phosphorus of ATP (R = adenosine); ADP leaves
2. **CO₂ release** – Carboxyphosphate breaks down to CO₂ and phosphate (drawn as one step)
3. **Carboxybiotin** – Phosphate removes the N1′–H of biotin as N1′ attacks CO₂
4. **CO₂ leaves biotin** – In the carboxyltransferase site carboxybiotin gives CO₂ and the biotin N1′ anion
5. **Malonyl-CoA** – Biotin N⁻ takes an α-H of acetyl-CoA; the enolate carbon adds to CO₂ (drawn concerted)

## Key points

- Biotin is bound by an amide to a Lys ε-amino group of the biotin carboxyl carrier protein; the long arm swings CO₂ between the two active sites.
- ATP is spent to activate HCO₃⁻: carboxyphosphate is a mixed anhydride, and N1′-carboxybiotin stores the "activated CO₂" (Lane & Lynen 1963).
- Acetyl-CoA carboxylase makes malonyl-CoA, the committed step of fatty-acid synthesis; citrate activates it and AMPK phosphorylation inhibits it.
- Pyruvate carboxylase and propionyl-CoA carboxylase use the same biotin chemistry; raw egg white avidin binds biotin and blocks them.

Drawn with 199 atoms, 19 arrows, 8 shapes – every one editable in MolDraw.

## Sources

- [Nelson & Cox, Lehninger Principles of Biochemistry, 8th ed., 2021, ch. 21](https://openlibrary.org/isbn/9781319228002) Textbook
- [Berg, Tymoczko, Gatto & Stryer, Biochemistry, 9th ed., 2019, ch. 22](https://openlibrary.org/isbn/9781319114657) Textbook
- [Lane & Lynen, Proc. Natl. Acad. Sci. USA 1963, 49, 379](https://doi.org/10.1073/pnas.49.3.379) Original paper

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