G4387
L-Glutamic Dehydrogenase (NADP) from Proteus sp.
buffered aqueous solution, ≥4,000 units/mL
Synonym(s):
L-Glutamate:NADP+ oxidoreductase (deaminating)
Sign Into View Organizational & Contract Pricing
All Photos(6)
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
bacterial (Proteus spp.)
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)
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
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
Marta Rodríguez-Sáiz et al.
Molecular biotechnology, 41(2), 165-172 (2008-11-19)
The gdhA gene encoding the NADP-dependent glutamate dehydrogenase (GDH) activity from Xanthophyllomyces dendrorhous has been cloned and characterized, and its promoter used for controlled gene expression in this red-pigmented heterobasidiomycetous yeast. We determined the nucleotide sequence of a 4701 bp
T Sanui et al.
Oral microbiology and immunology, 24(5), 361-368 (2009-08-26)
The purpose of this study was to examine the Streptococcus mutans biofilm cellular proteins recognized by immunoglobulin A (IgA) in saliva from various caries-defined populations. Biofilm and planktonic S. mutans UA159 cells were prepared. The proteins were extracted, separated by
Tom A Williams et al.
Molecular biology and evolution, 26(2), 445-450 (2008-11-28)
Aminoacyl tRNA synthetases (aaRS) are crucial enzymes that join amino acids to their cognate tRNAs, thereby implementing the genetic code. These enzymes fall into two unrelated structural classes whose evolution has not been explained. The leading hypothesis, proposed by Rodin
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service