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ChemicalBook--->CAS DataBase List--->9029-12-3

9029-12-3

9029-12-3 Structure

9029-12-3 Structure
IdentificationBack 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
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[form ]

solution (viscous)
[color ]

amber
[biological source]

bovine liver
[Specific Activity]

≥40units/mg protein
[EPA Substance Registry System]

Dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)) (9029-12-3)
Safety DataBack Directory
[Symbol(GHS) ]


GHS08
[Signal word ]

Danger
[Hazard statements ]

H334
[Precautionary statements ]

P261-P284-P501
[WGK Germany ]

3
[F ]

3-10
Hazard InformationBack Directory
[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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