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Merck

G2626

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

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

Sinónimos:

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

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

origen biológico

bovine liver

tpo

Type II

formulario

glycerol solution (50%)

actividad específica

≥35 units/mg protein

mol peso

310-350 kDa

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

Información sobre el gen

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Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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.

Forma física

50% glycerol solution

Nota de análisis

Protein determined by biuret.

sustrato

Referencia del producto
Descripción
Precios

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

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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

Artículos

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