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Key Documents

G2501

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

Type I, ammonium sulfate suspension, ≥40 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:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Type

Type I

Forme

ammonium sulfate suspension

Activité spécifique

≥40 units/mg protein

Poids mol.

310-350 kDa

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

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Actions biochimiques/physiologiques

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.

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

Suspension in 2.0 M (NH4)2SO4 solution

Remarque sur l'analyse

Protein determined by biuret

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Les clients ont également consulté

Michisuke Yuzaki
The European journal of neuroscience, 32(2), 191-197 (2010-07-22)
Several C1q family members, especially the Cbln and C1q-like subfamilies, are highly and predominantly expressed in the central nervous system. Cbln1, a member of the Cbln subfamily, plays two unique roles at parallel fiber (PF)-Purkinje cell synapses in the cerebellum:
Cleanthe Spanaki et al.
Neurotoxicity research, 21(1), 117-127 (2011-11-01)
Glutamate dehydrogenase (GDH) catalyzes the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia. High levels of GDH activity is found in mammalian liver, kidney, brain, and pancreas. In the liver, GDH reaction appears to be close-to-equilibrium, providing the appropriate ratio
Shanti Balasubramaniam et al.
Journal of pediatric endocrinology & metabolism : JPEM, 24(7-8), 573-577 (2011-09-22)
Hyperinsulinism-hyperammonemia syndrome (HI/HA) (OMIM 606762), the second most common form of congenital hyperinsulinism (CHI) is associated with activating missense mutations in the GLUD1 gene, which encodes the mitochondrial matrix enzyme, glutamate dehydrogenase (GDH). Patients present with recurrent symptomatic postprandial hypoglycemia
Nayla Munawar et al.
Extremophiles : life under extreme conditions, 16(3), 463-476 (2012-04-25)
Enzymes produced by halophilic archaea are generally heat resistant and organic solvent tolerant, and accordingly important for biocatalytic applications in 'green chemistry', frequently requiring a low-water environment. NAD(+)-dependent glutamate dehydrogenase from an extremely halophilic archaeon Halobacterium salinarum strain NRC-36014 was
Glutamic dehydrogenase.
H J STRECKER
Archives of biochemistry and biophysics, 46(1), 128-140 (1953-09-01)

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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