| Identification | Back Directory | [Name]
GLDH | [CAS]
9029-12-3 | [Synonyms]
GLDH
GLDH USP/EP/BP
Glutamate dehydrogenase 1
glutamic acid dehydrogenase
Glutamic acid dehydrogenase 1
L-Glutamic acid dehydrogenase
NAD(P)-glutamate dehydrogenase
GLUTAMATE DEHYDROGENASE, BOVINE
GlutamateDehydrogenaseExBovineLiver
GLUTAMATE DEHYDROGENASE (BOVINE LIVER)
Glutamate dehydrogenase(NAD dependent)
Gldh(GlutamateDehyrogenase),BovineLiver
glutamate dehydrogenase F. bovine liver
glutamic dehydrogenase from bovine liver
RECOMBINANT HUMAN GLUTAMATE DEHYDROGENASE
l-glutamic dehydrogenase from bovine liver
L-GLUTAMIC DEHYDROGENASE TYPE I*FROM BOV INE LIVER
GLUTAMATE DEHYDROGENASE F. BOVINE LIVER, ~1600 U/ML
L-GLUTAMIC DEHYDROGENASE TYPE II*FROM BO VINE LIVER
Glutamate dehydrogenase from bovine liver, lyophil.
L-GLUTAMIC DEHYDROGENASE TYPE III*FROM B OVINE LIVER
L-Glutamic Dehydrogenase,Suspension,from Beef Liver
GLUTAMATE DEHYDROGENASE F. BOVINE LIVER, LYO.,STAB.,>10U/MG
dehydrogenase,glutamate(nicotinamideadeninedinucleotide(phosphate))
L-GLDH, Glutamate Dehydrogenase, L-Glutamate: NAD[P]+ oxidoreductase (deaminating)
GLUTAMATE DEHYDROGENASE, RECOMBINANT, FROM PYROCOCCUS FURIOSUS GLDH CDNA EXPRESSED IN E. COLI | [EINECS(EC#)]
232-848-4 | [MDL Number]
MFCD01323386 |
| Hazard Information | Back Directory | [Chemical Properties]
Found in enzyme mothers, higher plants, and animals. The commercial product is typically a crystal suspension extracted from bovine liver in a 2 mol·L-1 ammonium sulfate solution. Its pH is 7. Each ml contains 20 mg of enzyme, with an activity of 450,000 units per mg. The activity remains stable for 12 months, but the aqueous solution may become slightly turbid after a few months. | [Uses]
L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-ketoglutarate and carbon dioxide. | [Biochem/physiol Actions]
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. |
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