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1.7.3.1: nitroalkane oxidase

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

Word Map on EC 1.7.3.1

Reaction

ethylnitronate
+
O2
+
FMNH2
=
acetaldehyde
+
nitrite
+
FMN
+
H2O

Synonyms

2-npdl, More, NAO, NaoA, nitroalkane oxidase, nitroalkane-oxidizing enzyme, nitroethane oxidase, nitroethane:oxygen oxidoreductase, NOE, oxidase, nitroethane, PA4202

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.3 With oxygen as acceptor
                1.7.3.1 nitroalkane oxidase

Engineering

Engineering on EC 1.7.3.1 - nitroalkane oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C397S
D402A
-
site-directed mutation of the active site base, 20fold reduced catalytic efficiency with neutral nitroethane as substrate compared to the wild-type enzyme, while the wild-type enzyme prefers the neutral substrate the mutant prefers the anion substrate form, altered pH-dependence with both substrate forms compared to the wild-type enzyme
D402E
D402N
R409K
S171A
S171T
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
S171V
-
the mutation results in decreases in the rate constants for removal of the substrate proton by about 5fold and decreases in the rate constant for product release of about 2fold, the mutation alters the rate constant for flavin oxidation
S276A
Y398F
D399N
the mutation decreases the kcat/KM value for nitroethane over 2 orders of magnitude
R406K
the mutation decreases the kcat/KM value for nitroethane about 64fold
S373A
the mutation decreases the kcat/KM value for nitroethane about 3fold
H183C
-
the mutant shows reduced activity compared to the wild type enzyme
H183S
-
the mutant shows reduced activity compared to the wild type enzyme
H179D
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
H179K
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
H179V
residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity
additional information