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G2626

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

Type II, 50% glycerol solution, ≥35 units/mg protein

Synonyme(s) :

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

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About This Item

Numéro CAS:
9029-12-3
Numéro de classification (Commission des enzymes):
1.4.1.3 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131461
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine liver

Type

Type II

Forme

glycerol solution (50%)

Activité spécifique

≥35 units/mg protein

Poids mol.

310-350 kDa

Numéro d'accès UniProt

P00366

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Informations sur le gène

cow ... GLUD1(281785)

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Application

L-glutamic dehydrogenase was used to catalyze the conversion of isocitrate into α-ketoglutarate and carbon dioxide.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

50% glycerol solution

Remarque sur l'analyse

Protein determined by biuret.

Substrat

Réf. du produit
Description
Tarif

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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S Vesce et al.
FEBS letters, 411(1), 107-109 (1997-07-07)
The mechanisms of HIV-1 neurotoxicity remain still undefined although the induction of signalling events and a modest inhibition of glutamate uptake induced by the envelope glycoprotein, gp120, have called attention to astrocytes. Here we demonstrate that the levels at which
Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.
Bezsudnova, et al.
PLoS ONE, 16, e0255098-e0255098 (2021)
Sabine Ruegenberg et al.
Nature communications, 12(1), 2176-2176 (2021-04-14)
The hexosamine pathway (HP) is a key anabolic pathway whose product uridine 5'-diphospho-N-acetyl-D-glucosamine (UDP-GlcNAc) is an essential precursor for glycosylation processes in mammals. It modulates the ER stress response and HP activation extends lifespan in Caenorhabditis elegans. The highly conserved
Mariagrazia Grimaldi et al.
Human molecular genetics, 26(18), 3453-3465 (2017-09-16)
Congenital hyperinsulinism/hyperammonemia (HI/HA) syndrome gives rise to unregulated protein-induced insulin secretion from pancreatic beta-cells, fasting hypoglycemia and elevated plasma ammonia levels. Mutations associated with HI/HA were identified in the Glud1 gene, encoding for glutamate dehydrogenase (GDH). We aimed at identifying
Virginia Kroef et al.
eLife, 11 (2022-03-02)
The hexosamine biosynthetic pathway (HBP) produces the essential metabolite UDP-GlcNAc and plays a key role in metabolism, health, and aging. The HBP is controlled by its rate-limiting enzyme glutamine fructose-6-phosphate amidotransferase (GFPT/GFAT) that is directly inhibited by UDP-GlcNAc in a
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