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1.4.3.11: L-glutamate oxidase

This is an abbreviated version!
For detailed information about L-glutamate oxidase, go to the full flat file.

Word Map on EC 1.4.3.11

Reaction

L-glutamate
+
O2
 +
H2O
=
2-oxoglutarate
 +
NH3
 +
H2O2

Synonyms

dehydrogenase, glutamate (acceptor), GLOD, GluOx, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), GOX, L-GLOD, l-GlOx, L-glutamate oxidase, L-glutamic acid oxidase, LGOX

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.11 L-glutamate oxidase

Engineering

Engineering on EC 1.4.3.11 - L-glutamate oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F94L
single point mutant with improved enzymatic activity
H533R
single point mutant with improved enzymatic activity
I282M
single point mutant with improved enzymatic activity
S280T
single point mutant with improved enzymatic activity
S280T/H533L
mutant shows 90% higher enzymatic activity than the wild-type control
H312A
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids
R305A
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine)
R305D
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-arginine)
R305K
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine)
R305L
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine)
W564A
the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids
R305E
wild-type enzyme shows strict substrate specificity for L-glutamate. The mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine. R305E is a thermostable and pH stable enzyme
additional information
-
construction of a highly sensitive and selective glutamate microbiosensor based on polypyrrole, multiwalled carbon nanotubes, and glutamate oxidase deposited on the transducer platinum electrode, i.e. Pt/PPy/MWCNT/GluOx electrodes, overview. The biosensor has a high sensitivity, low response to interferences such as ascorbic acid, uric acid and acetaminophen, a fast response time, low detection limit, a linear range of 0.14 mM, and a satisfactory stability, mass transfer-limiting outer membrane of polyurethane, optimization, overview