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)
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
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 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
Regulatory Information
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Dopamine and Glutamate in Psychiatric Disorders (2010)
II. Glutamine and glutamate
Tapiero H, et al.
Biomedicine and Pharmacotherapy, 56(9), 446-457 (2002)
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)
W H Oldenziel et al.
Journal of neuroscience methods, 140(1-2), 117-126 (2004-12-14)
Hydrogel-coated microsensors based on carbon fiber electrodes (CFEs) are promising tools for in vivo analysis of endogeneous compounds such as glutamate. However, their construction generally depends on manual fabrication, which often results in poor reproducibility. The aim of this study
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