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
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1.7.3.1
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atlantic
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oscillation
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climate
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winter
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atmospheric
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orange
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robot
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weather
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acridine
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ocean
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interannual
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summer
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arctic
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nai
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phenology
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cardiolipin
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humanoid
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forecast
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nonyl
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rainfall
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meteorological
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hydrological
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seabird
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snow
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latitudinal
- 1.7.3.1
-
atlantic
-
oscillation
-
climate
-
winter
-
atmospheric
- orange
-
robot
-
weather
- acridine
-
ocean
-
interannual
-
summer
-
arctic
- nai
-
phenology
- cardiolipin
-
humanoid
-
forecast
-
warmer
-
nonyl
-
rainfall
-
meteorological
-
hydrological
-
seabird
-
snow
-
latitudinal
Reaction
Synonyms
2-npdl, More, NAO, NaoA, nitroalkane oxidase, nitroalkane-oxidizing enzyme, nitroethane oxidase, nitroethane:oxygen oxidoreductase, NOE, oxidase, nitroethane, PA4202
ECTree
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Engineering
Engineering on EC 1.7.3.1 - nitroalkane oxidase
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C397S
D402A
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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
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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
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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
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the mutant shows reduced activity compared to the wild type enzyme
H183S
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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
the mutant shows reduced activity compared to the wild type enzyme
C397S
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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 mutant enzyme is less stable than the wild type enzyme
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site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, mutation has no effect on the rate of reaction of the reduced enzyme with oxygen, reaction mechanism analysis
D402E
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mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme, determined at 2.4 A resolution, shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402. The interaction of this residue with Ser276 is perturbed
D402E
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the mutation results in a decrease in the rate constant for proton abstraction of 18fold. The structure of the D402E enzyme shows that there is a smaller increase in the distance between Arg409 and the carboxylate at position 402 (compared to mutant enzyme R409K), and the interaction of this residue with Ser276 is perturbed
D402E
the mutant shows severely reduced activity compared to the wild type enzyme
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site-directed mutation of the active site base, 140fold 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
D402N
no detectable activity with neutral substrates. Crystallization data in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD
D402N
the mutant shows reduced activity compared to the wild type enzyme
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the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
R409K
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the mutation results in a decrease in the rate constant for proton abstraction of 100fold. Analysis of the three-dimensional structure of the R409K enzyme, determined by X-ray crystallography to a resolution of 2.65 A, shows that the critical structural change is an increase in the distance between the carboxylate of Asp402 and the positively charged nitrogen in the side chain of the residue at position 409
R409K
the mutant shows severely reduced activity compared to the wild type enzyme
the mutant shows reduced activity compared to the wild type enzyme
S171A
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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
S276A
the mutant shows severely reduced activity compared to the wild type enzyme
the mutant shows reduced activity compared to the wild type enzyme
Y398F
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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 mutant enzyme is less stable than the wild type enzyme
naoA disruption accelerates growth of the naoA-disruption mutant, which can restore its phenotype and morphology as a wild-type strain by complementation of a single copy number of naoA inserted into the chromosome. The introduction of an extra copy of naoA into the wild-type strain results in delayed growth
additional information
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naoA disruption accelerates growth of the naoA-disruption mutant, which can restore its phenotype and morphology as a wild-type strain by complementation of a single copy number of naoA inserted into the chromosome. The introduction of an extra copy of naoA into the wild-type strain results in delayed growth