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Literature summary 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.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.4.3.11 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.11 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

EC Number Organism UniProt Comment Textmining
1.4.3.11 Streptomyces sp.
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.4.3.11 GluOx
-
 Streptomyces sp.
1.4.3.11 glutamate oxidase
-
 Streptomyces sp.