Literature summary for 1.4.3.11 extracted from

McMahon, C.P.; Rocchitta, G.; Serra, P.A.; Kirwan, S.M.; Lowry, J.P.; ONeill, R.D.
The efficiency of immobilised glutamate oxidase decreases with surface enzyme loading: an electrostatic effect, and reversal by a polycation significantly enhances biosensor sensitivity (2006), Analyst, 131, 68-72.

Search for more literature for 1.4.3.11

Application

Application	Comment	Organism
medicine	Pt/polyethyleneimine/GluOx/poly(o-phenylenediamine) biosensors of both cylinder and disk configurations display superb sensitivity in the linear glutamate calibration region, would provide excellent glutamate sensitivity and spatial resolution in neurochemical monitoring involving small brain areas or layered structures in vivo	Streptomyces sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	L-glutamate	KM for surface immobilised GluOx increases systematically with enzyme loading, due in part to electrostatic repulsion between the anionic substrate and neighbouring enzyme molecules at neutral pH	Streptomyces sp.

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamate + O2 + H2O	-	Streptomyces sp.	2-oxoglutarate + NH3 + H2O2	-	?

Synonyms

Synonyms	Comment	Organism
GluOx	-	Streptomyces sp.
glutamate oxidase	-	Streptomyces sp.

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Release 2023.1 (January 2023)