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G5921

Sigma-Aldrich

L-Glutamate Oxidase from Streptomyces sp.

recombinant, expressed in E. coli, lyophilized powder, ≥5.0 units/mg solid

Sinónimos:

L-Glutamate:oxygen oxidoreductase (deaminating)

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

recombinant

expressed in E. coli

form

lyophilized powder

specific activity

≥5.0 units/mg solid

storage temp.

2-8°C

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General description

Glutamate is a non-essential amino acid. It acts as a primary excitatory neurotransmitter. In major trauma, major surgery, sepsis and bone marrow transplantation, glutamate functions as an essential amino acid.

Application

L-Glutamate Oxidase from Streptomyces sp has been used to determine the enzyme activity of the immobilized glutamate oxidase (GOx). It has also been used as a component of imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging.

Biochem/physiol Actions

L-glutamate oxidase catalyzes the conversion of L-glutamate to 2-oxoglutarate.
Major enzyme in the synthesis or degradation of glutamic acid; transfers an amine to α-ketoglutaric acid to form L-glutamic acid or deamidates L-glutamic acid

Unit Definition

One unit will form 1.0 μmole of α-ketoglutaric acid from L-glutamic acid per min at pH 7.4 at 30 °C.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Polycomb repressive complex 1 generates discrete compacted domains that change during differentiation
Kundu S, et al.
Molecular Cell, 65(3), 432-446 (2017)
Dopamine and Glutamate in Psychiatric Disorders (2010)
Sensing based on the motion of enzyme-modified nanorods
Bunea AI, et al.
Biosensors And Bioelectronics, 67(9), 42-48 (2015)
II. Glutamine and glutamate
Tapiero H, et al.
Biomedicine and Pharmacotherapy, 56(9), 446-457 (2002)
Colm P McMahon et al.
The Analyst, 131(1), 68-72 (2005-12-21)
The apparent Michaelis constant, K(M), for glutamate oxidase (GluOx) immobilised on Pt electrodes increased systematically with enzyme loading. The effect was due, at least in part, to electrostatic repulsion between neighbouring oxidase molecules and the anionic substrate, glutamate (Glu). This

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