- glutamate dehydrogenase
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- $5.50 / 100KU
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2023-08-03
- CAS:9029-12-3
- Min. Order: 100KU
- Purity: ≥ 50U/mg
- Supply Ability: 10000ku
- Glutamic Dehydrogenase
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- $0.00 / 5KU
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2021-09-29
- CAS:9029-12-3
- Min. Order: 5KU
- Purity: ≥99.0%
- Supply Ability: 400u/mg
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| Product Name: | GLDH | | Synonyms: | dehydrogenase,glutamate(nicotinamideadeninedinucleotide(phosphate));glutamate dehydrogenase F. bovine liver;L-GLUTAMIC DEHYDROGENASE TYPE II*FROM BO VINE LIVER;GLUTAMATE DEHYDROGENASE F. BOVINE LIVER, LYO.,STAB.,>10U/MG;L-GLUTAMIC DEHYDROGENASE TYPE III*FROM B OVINE LIVER;L-GLUTAMIC DEHYDROGENASE TYPE I*FROM BOV INE LIVER;GLUTAMATE DEHYDROGENASE F. BOVINE LIVER, ~1600 U/ML;GlutamateDehydrogenaseExBovineLiver | | CAS: | 9029-12-3 | | MF: | | | MW: | 0 | | EINECS: | 232-848-4 | | Product Categories: | | | Mol File: | Mol File | ![GLDH Structure]() |
| 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. |
| | GLDH Preparation Products And Raw materials |
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