Product Name

L-Glutamic Dehydrogenase from bovine liver

Synonym

L-GLDH, L-Glutamate:NAD[P]₊ Oxidoreductase (deaminating), Glutamate Dehydrogenase from bovine liver

Assay

≥40 units/mg protein,Type I

CAS Number

9029-12-3

MDL number

MFCD00131461

Suitability

BioReagent

l Physical and Chemical Information

Appearance

ammonium sulfate suspension

Physical form

Suspension in 2.0 M (NH⁴)²SO⁴ solution

l Biological Information

Biochem/Physiol Actions

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. The bovine enzyme is characterized by three sets of properties:

• It has a reversible concentration-dependent association, producing higher molecular weight forms.

• Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.

• Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.

Preparation Note

This product is supplied as a suspension in 2.0 M ammonium sulfate, pH 7.0. This solution is then diluted to 0.3 - 0.6 units/ml using triethanolamine buffer, pH 7.3, for use in enzymatic assays.

Unit Definition

One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.3 at 25 °C, in the presence of ammonium ions.

l Packaging & Storage

Storage temp.

2-8°C

l Precautions and Disclaimer

This product is for R&D use only, not for drug, household, or other uses.

l References

1. http://www.drugbank.ca

2. https://ncit.nci.nih.gov

3. https://www.ncbi.nlm.nih.gov