G5921
L-Glutamate Oxidase from Streptomyces sp.
recombinant, expressed in E. coli, lyophilized powder, ≥5.0 units/mg solid
Synonym(s):
L-Glutamate:oxygen oxidoreductase (deaminating)
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About This Item
Specific activity:
≥5.0 units/mg solid
Recombinant:
expressed in E. coli
Product Name
L-Glutamate Oxidase from Streptomyces sp., recombinant, expressed in E. coli, lyophilized powder, ≥5.0 units/mg solid
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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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
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.
Other Notes
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Purification and properties of a new enzyme, L-glutamate oxidase, from Streptomyces sp X-119-6 grown on wheat bran.
H. Yoshino
Agricultural and Biological Chemistry, 74, 1323-1328 (1983)
Polycomb repressive complex 1 generates discrete compacted domains that change during differentiation
Kundu S, et al.
Molecular Cell, 65(3), 432-446 (2017)
II. Glutamine and glutamate
Tapiero H, et al.
Biomedicine and Pharmacotherapy, 56(9), 446-457 (2002)
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)
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