1.13.12.16: nitronate monooxygenase
This is an abbreviated version!
For detailed information about nitronate monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.16
-
1.13.12.16
-
nitroalkanes
-
flavin
-
nitroethane
-
neurospora
-
crassa
-
fmn
-
hansenula
-
mrakii
-
flavosemiquinone
-
1-nitropropane
-
denitrification
-
3-nitropropionic
-
ansochromogenes
-
fmn-dependent
-
saturnus
- 1.13.12.16
- nitroalkanes
- flavin
- nitroethane
- neurospora
- crassa
- fmn
- hansenula
- mrakii
-
flavosemiquinone
- 1-nitropropane
-
denitrification
-
3-nitropropionic
- ansochromogenes
-
fmn-dependent
- saturnus
Reaction
Synonyms
2-nitropropane dioxygenase, EC 1.13.11.32, NAO, ncd2, nitroalkane oxidase, nitroalkane-oxidizing enzyme, nitronate monooxygenase, nitropropane dioxygenase, NMO, NMO-Nc, NMO-Ws, nmoA, Npd1, Npd2, Npd3, Npd4, Npd5, Npd6, oxidase, nitroalkane, oxygenase, 2-nitropropane di-, P3N monooxygenase, Pa-NMO, PA4202, protein PA4202, Rv1894c, Sa-NAO
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.12.16 - nitronate monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
H196N
H152A
S288A
H179D
mutant enzyme shows no activity. Crystal structure of mutant H179D is determined: The structural superimposition of wild-type Sa-NAO and mutant H179D-nitroethane shows no significant structural variation
additional information
-
the H196N variant form of the enzyme does to catalyze the formation of ethylnitronate from nitroethane. The H196N variant is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
H196N
-
site-directed mutagenesis, does to catalyze the formation of ethylnitronate from nitroethane. It is a better catalyst than the wild-type enzyme for oxidative turnover with ethylnitronate
His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon
H152A
site-directed mutagenesis. His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon
mutant enzyme forms inclusion bodies when overexpressed in Escherichia coli
S288A
site-directed mutagenesis. Mutant enzyme forms inclusion bodies when overexpressed in Escherichia coli
construction of an enzyme deletion mutant by the in vivo recombination system of the yeast Saccharomyces cerevisiae strain InvSc1, overview. Quantitative RT-PCR enzyme expression analysis. The expression of ddlA is not changed in the DELTAnmoA mutant compared to the wild-type
additional information
-
construction of an enzyme deletion mutant by the in vivo recombination system of the yeast Saccharomyces cerevisiae strain InvSc1, overview. Quantitative RT-PCR enzyme expression analysis. The expression of ddlA is not changed in the DELTAnmoA mutant compared to the wild-type