G2501
L-Glutamic Dehydrogenase from bovine liver
Type I, ammonium sulfate suspension, ≥40 units/mg protein
Synonym(s):
L-GLDH, L-Glutamate:NAD[P]+ Oxidoreductase (deaminating), Glutamate Dehydrogenase from bovine liver
type
Type I
Quality Level
form
ammonium sulfate suspension
specific activity
≥40 units/mg protein
mol wt
310-350 kDa
UniProt accession no.
storage temp.
2-8°C
Gene Information
cow ... GLUD1(281785)
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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:
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
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.
Physical form
Suspension in 2.0 M (NH4)2SO4 solution
Analysis Note
Protein determined by biuret
Other Notes
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
低风险生物材料
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Glutamic dehydrogenase.
H J STRECKER
Archives of biochemistry and biophysics, 46(1), 128-140 (1953-09-01)
Mehran Karimi et al.
Seminars in thrombosis and hemostasis, 35(4), 426-438 (2009-07-15)
Factor XIII (FXIII) is a tetrameric zymogen (FXIII-A (2)B (2)) that is converted into an active transglutaminase (FXIIIa) by thrombin and Ca (2+) in the terminal phase of the clotting cascade. By cross-linking fibrin chains and alpha (2) plasmin inhibitor
Hyperinsulinism and hyperammonaemia syndrome and severe myoclonic epilepsy of infancy.
F Pérez Errazquin et al.
Neurologia (Barcelona, Spain), 26(4), 248-252 (2010-12-18)
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
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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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