[Durgical](https://durgical.com/en/) › [DurgiPedia](https://durgical.com/en/durgipedia/) › [Biochemistry](https://durgical.com/en/biochemistry/) › Glutamate dehydrogenase (GDH)

[Biochemistry](https://durgical.com/en/biochemistry/) · Enzyme

# Glutamate dehydrogenase (GDH)

Glutamate dehydrogenase frees ammonia from glutamate in liver mitochondria and links amino acid breakdown to the Krebs cycle.

Updated 2026-11-01

Loading the 3D model…

## Key facts

- Glutamate + NAD(P)⁺ + H₂O ⇌ α-ketoglutarate + NH₄⁺ + NAD(P)H; reversible.
- It can use NAD⁺ or NADP⁺, which is unusual among dehydrogenases.
- With the transaminases it forms transdeamination: the amino group of almost any amino acid ends as NH₄⁺.
- A mitochondrial hexamer abundant in liver, kidney and brain.

**EC number**
[1.4.1.3](https://www.enzyme-database.org/query.php?ec=1.4.1.3)

**Genes**
GLUD1

**Structure (PDB)**
[1L1F](https://www.rcsb.org/structure/1L1F)

## Structure

- 1L1F is human GDH with no ligands: six subunits with an «antenna» that relays allosteric signals.

## Regulation

- ADP and leucine activate it (low energy or plenty of amino acids).
- GTP and ATP inhibit it (high energy).

## Inhibitors and toxins

- GTP (physiological inhibitor)
- Epigallocatechin gallate from green tea (experimental)

## Clinical notes

- Activating GLUD1 mutations, which remove GTP inhibition, cause the hyperinsulinism–hyperammonaemia syndrome.
- In that syndrome, protein-rich meals (leucine) trigger hypoglycaemia, and ammonia stays mildly and constantly high.

## Related conditions

- [Hyperammonaemia](https://durgical.com/en/conditions/hyperammonaemia/)

## Related

- [Glutamate (glutamic acid)](https://durgical.com/en/biochemistry/molecules/glutamate/)
- [Ammonia (ammonium)](https://durgical.com/en/biochemistry/molecules/ammonia/)
- [NAD⁺ (nicotinamide adenine dinucleotide)](https://durgical.com/en/biochemistry/molecules/nad/)
- [Krebs cycle (citric acid cycle)](https://durgical.com/en/biochemistry/pathways/krebs-cycle/)
- [Transamination and deamination](https://durgical.com/en/biochemistry/topics/transamination-and-deamination/)

## Test yourself

Think of the answer, then tap the question to see it.

## Which reaction does glutamate dehydrogenase catalyse?

Oxidative deamination of glutamate: it releases NH₄⁺ and forms α-ketoglutarate, using NAD⁺ or NADP⁺.

## Which molecules activate it, and which inhibit it?

ADP and leucine activate it; GTP and ATP inhibit it.

## Why does an overactive GDH cause hypoglycaemia?

In the beta cell it makes more α-ketoglutarate and ATP, which triggers insulin release, especially after protein.

[Add to my cards (3)](https://durgical.app/estudiar/?add=/en/biochemistry/enzymes/glutamate-dehydrogenase/)

Educational information, not medical advice. For any symptom, see a health professional.

Sources: [GLUD1: Glutamate dehydrogenase 1, mitochondrial (human)](https://www.uniprot.org/uniprotkb/P00367/entry) (UniProt, 2026); [Congenital hyperinsulinism: MedlinePlus Genetics](https://medlineplus.gov/genetics/condition/congenital-hyperinsulinism/) (MedlinePlus, US National Library of Medicine, 2026); [1L1F: Structure of human glutamate dehydrogenase-apo form](https://www.rcsb.org/structure/1L1F) (RCSB Protein Data Bank, 2026).

[← All of biochemistry](https://durgical.com/en/biochemistry/)

## **Spotted a mistake?** We are always improving for the community. Tell us what is wrong and our team will review it. Report a mistake

Representative model, for educational purposes only.

---
Source: https://durgical.com/en/biochemistry/enzymes/glutamate-dehydrogenase/
License: CC BY 4.0 (https://creativecommons.org/licenses/by/4.0/). Cite as: DurgiPedia (durgical.com), https://durgical.com/en/biochemistry/enzymes/glutamate-dehydrogenase/