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G2501

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

Type I, ammonium sulfate suspension, ≥40 units/mg protein

Synonym(s):

L-GLDH, L-Glutamate:NAD[P]+ Oxidoreductase (deaminating), Glutamate Dehydrogenase from bovine liver

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About This Item

CAS Number:
9029-12-3
Enzyme Commission number:
1.4.1.3 (BRENDA, IUBMB)
EC Number:
232-848-4
MDL number:
MFCD00131461
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type I

form

ammonium sulfate suspension

specific activity

≥40 units/mg protein

mol wt

310-350 kDa

UniProt accession no.

P00366

storage temp.

2-8°C

Gene Information

cow ... GLUD1(281785)

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Biochem/physiol Actions

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

Unit Definition

One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.3 at 25 °C, in the presence of ammonium ions.

Physical form

Suspension in 2.0 M (NH4)2SO4 solution

Analysis Note

Protein determined by biuret

substrate

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Hyperinsulinism and hyperammonaemia syndrome and severe myoclonic epilepsy of infancy.
F Pérez Errazquin et al.
Neurologia (Barcelona, Spain), 26(4), 248-252 (2010-12-18)
Mehran Karimi et al.
Seminars in thrombosis and hemostasis, 35(4), 426-438 (2009-07-15)
Factor XIII (FXIII) is a tetrameric zymogen (FXIII-A (2)B (2)) that is converted into an active transglutaminase (FXIIIa) by thrombin and Ca (2+) in the terminal phase of the clotting cascade. By cross-linking fibrin chains and alpha (2) plasmin inhibitor
Glutamic dehydrogenase.
H J STRECKER
Archives of biochemistry and biophysics, 46(1), 128-140 (1953-09-01)
Konstantinos Kanavouras et al.
Journal of neurochemistry, 109 Suppl 1, 167-173 (2009-05-07)
Glutamate dehydrogenase (GDH) in human exists in GLUD1 and GLUD2 gene-encoded isoforms (hGDH1 and hGDH2, respectively), differing in their regulation and tissue expression pattern. Whereas hGDH1 is subject to GTP control, hGDH2 uses for its regulation, a novel molecular mechanism
Ioannis Zaganas et al.
Neurochemistry international, 55(1-3), 52-63 (2009-05-12)
In all mammals, glutamate dehydrogenase (GDH), an enzyme central to the metabolism of glutamate, is encoded by a single gene (GLUD1 in humans) which is expressed widely (housekeeping). Humans and other primates also possess a second gene, GLUD2, which encodes
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Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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