---
title: "Kinase phosphoryl transfer (hexokinase) Template | MolDraw"
url: https://www.moldraw.com/templates/enzyme-kinase-phosphoryl-transfer/
description: "Kinase phosphoryl transfer (hexokinase) template: Hexokinase: an Asp side chain removes the proton of the glucose C6–OH as it attacks the γ-phosphorus…"
lang: en
publisher: Scidart Academy
generated: 2026-11-13
---
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# Kinase phosphoryl transfer (hexokinase) template

![Kinase phosphoryl transfer (hexokinase) template: Hexokinase: an Asp side chain removes the proton of the glucose C6–OH as it attacks the γ-phosphorus opposite the β,γ-bridging oxygen (in-line, inversion at P), and ADP leaves; Mg²⁺ bound to the β- and γ-phosphates shields their charge. In ATP hydrolysis water is the nucleophile.](https://www.moldraw.com/templates/enzyme-kinase-phosphoryl-transfer.webp)

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Hexokinase: an Asp side chain removes the proton of the glucose C6–OH as it attacks the γ-phosphorus opposite the β,γ-bridging oxygen (in-line, inversion at P), and ADP leaves; Mg²⁺ bound to the β- and γ-phosphates shields their charge. In ATP hydrolysis water is the nucleophile.

## Mechanism step by step

In-line attack on the γ-phosphorus of MgATP²⁻: glucose 6-OH becomes glucose 6-phosphate; water does the same in ATP hydrolysis

1. **Phosphoryl transfer** – Asp (base) takes the 6-OH proton; O6 attacks Pγ in line with the leaving β,γ-bridge oxygen
2. **ATP hydrolysis** – The same in-line attack with water as the nucleophile (ATPases, myosin)

## Key points

- The true substrate is MgATP²⁻: Mg²⁺ on the β- and γ-phosphates shields the negative charge so the nucleophile can approach Pγ.
- In-line attack goes through a trigonal-bipyramidal transition state and inverts the configuration at P (shown with chiral [¹⁶O,¹⁷O,¹⁸O]-phosphoryl groups).
- Hexokinase closes around glucose (induced fit, Koshland), which shuts water out of the site so ATP is not simply hydrolysed.
- ATP hydrolysis: ΔG°′ ≈ −30.5 kJ/mol; in cells ΔG is about −50 to −65 kJ/mol because [ATP]/[ADP][Pᵢ] is held far from equilibrium.

Drawn with 153 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. 9](https://openlibrary.org/isbn/9781319114657) Textbook

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## Frequently asked questions

### Is the Kinase phosphoryl transfer (hexokinase) template free?

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### 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.

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