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G4387

Sigma-Aldrich

L-Glutamic Dehydrogenase (NADP) from Proteus sp.

buffered aqueous solution, ≥4,000 units/mL

Synonym(s):

L-Glutamate:NADP+ oxidoreductase (deaminating)

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About This Item

CAS Number:
9029-11-2
Enzyme Commission number:
1.4.1.4 (BRENDA, IUBMB)
MDL number:
MFCD00131461
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Proteus spp.)

Quality Level

200

form

buffered aqueous solution

specific activity

≥4,000 units/mL

mol wt

~300 kDa

storage temp.

2-8°C

Application

This enzyme is useful for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201) in clinical analysis. In vitro, various activity assays of this enzyme examine the conversion of α-ketoglutarate to L-glutamate, in the presence of excess ammonium ions (NH4+) and NADPH.

Biochem/physiol Actions

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.

Physical properties

Isoelectric point : 4.6
Michaelis constants : 1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate)
1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+)
Structure : 6 subunits (M.W.50,000) per mol of enzyme
Inhibitors : Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine,
2,2′-dithiopyridine
Optimum pH : 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature : 45oC(α-KG−L-Glu) 45-55oC (L-Glu→α-KG)
pH stability : pH 6.0 - 8.5 (25oC, 20hr)
Thermal stability : below 50oC (pH 7.4, 10min)

Unit Definition

One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30 °C in the presence of ammonium ions and NADPH.

Physical form

Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide

Other Notes

Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

ISHL Notified Names

Substances Subject to be Notified Names

JAN Code

G4387-5KU:
G4387-VAR:
G4387-500UN:
G4387-BULK:
G4387-1KU:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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J Bailey et al.
The Journal of biological chemistry, 257(10), 5579-5583 (1982-05-25)
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At ph 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both
D P Hornby et al.
The Biochemical journal, 223(1), 161-168 (1984-10-01)
In steady-state kinetic studies of ox liver glutamate dehydrogenase in 0.11 M-potassium phosphate buffer, pH7, at 25 degrees C, the concentration of ADP was varied from 0.5 to 1000 microM. Inhibition was observed except when the concentrations of both glutamate
Daria V Borsakova et al.
Scientific reports, 12(1), 5437-5437 (2022-04-02)
Excessive ammonium blood concentration causes many serious neurological complications. The medications currently used are not very effective. To remove ammonium from the blood, erythrocyte-bioreactors containing enzymes that processing ammonium have been proposed. The most promising bioreactor contained co-encapsulated glutamate dehydrogenase
Wei-Li Liao et al.
Fungal genetics and biology : FG & B, 45(4), 514-526 (2007-10-24)
The function of GLN3, a GATA factor encoding gene, in nitrogen metabolism of Candida albicans was examined. GLN3 null mutants had reduced growth rates on multiple nitrogen sources. More severe growth defects were observed in mutants lacking both GLN3 and
Jette Thykaer et al.
Journal of biotechnology, 139(4), 280-282 (2009-01-27)
New morphological aspects of Penicillium chrysogenum were found during physiological characterisation of two NADPH-dependent glutamate dehydrogenase mutant strains. A morphological characterisation of the previously constructed strains, together with the two beta-lactam producing industrial recipient strains, was conducted. The reference strains
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