---
title: "Class I aldolase (Schiff base) Template | MolDraw"
url: https://www.moldraw.com/templates/enzyme-aldolase-schiff-base/
description: "Class I aldolase (Schiff base) template: Fructose 1,6-bisphosphate (open chain) forms a protonated Schiff base with Lys229; Asp33 removes the C4–OH proton…"
lang: en
publisher: Scidart Academy
generated: 2026-11-13
---
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# Class I aldolase (Schiff base) template

![Class I aldolase (Schiff base) template: Fructose 1,6-bisphosphate (open chain) forms a protonated Schiff base with Lys229; Asp33 removes the C4–OH proton, the C3–C4 bond breaks with the iminium as electron sink to release glyceraldehyde 3-phosphate, and the enamine is protonated and hydrolysed to dihydroxyacetone phosphate.](https://www.moldraw.com/templates/enzyme-aldolase-schiff-base.webp)

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Fructose 1,6-bisphosphate (open chain) forms a protonated Schiff base with Lys229; Asp33 removes the C4–OH proton, the C3–C4 bond breaks with the iminium as electron sink to release glyceraldehyde 3-phosphate, and the enamine is protonated and hydrolysed to dihydroxyacetone phosphate.

## Mechanism step by step

Lys229 forms an iminium ion with fructose 1,6-bisphosphate; a retro-aldol cleavage of C3–C4 releases GAP

1. **Lys229 adds to C2** – The ε-amino group attacks the ketone: a carbinolamine (zwitterion)
2. **Iminium ion** – Proton transfers and loss of water: the protonated Schiff base (arrows not shown)
3. **Retro-aldol cleavage** – Asp33 takes the C4–OH proton; C3–C4 breaks and the iminium takes the electrons
4. **Enamine protonation** – C3 takes a proton: the iminium ion of DHAP
5. **Hydrolysis (summarised)** – Water adds to C=N⁺ and Lys229 leaves: DHAP and free enzyme

## Key points

- The protonated Schiff base (iminium) is a better electron sink than C=O, so it stabilises the C3 carbanion/enamine (Horecker: NaBH₄ traps it on Lys).
- Class II aldolases (bacteria, fungi) use Zn²⁺ instead of a Schiff base to polarise the carbonyl.
- ΔG°′ = +23.8 kJ/mol, yet in cells ΔG ≈ 0 because the products are removed and kept at low concentration.
- In gluconeogenesis the same enzyme runs the aldol forward: DHAP + GAP → fructose 1,6-bisphosphate.

Drawn with 235 atoms, 15 arrows, 8 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
- [Grazi, Rowley, Cheng, Tchola & Horecker, Biochem. Biophys. Res. Commun. 1962, 9, 38](https://doi.org/10.1016/0006-291x(62)90083-9) Original paper

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## Frequently asked questions

### Is the Class I aldolase (Schiff base) template free?

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### Is the chemistry checked?

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