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1.14.13.210: 4-methyl-5-nitrocatechol 5-monooxygenase

This is an abbreviated version!
For detailed information about 4-methyl-5-nitrocatechol 5-monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.210

Reaction

4-methyl-5-nitrocatechol
+
NAD(P)H
 +
H+
 +
O2
=
2-hydroxy-5-methylquinone
 +
nitrite
 +
NAD(P)+
 +
H2O

Synonyms

4-methyl-5-nitrocatechol monooxygenase, 4-methyl-5-nitrocatechol oxygenase, 4M5NC monooxygenase, dntB, MNC, MNC monooxygenase, MNC oxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.210 4-methyl-5-nitrocatechol 5-monooxygenase

Engineering

Engineering on EC 1.14.13.210 - 4-methyl-5-nitrocatechol 5-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L380I
site-directed mutagenesis, the mutant shows unaltered activity with 4-nitrophenol compared to the wild-type enzyme
M22L
site-directed mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
M22L/L380I
error-prone PCR, protein engineering for nitrite removal, the mutant enzyme accepts two addtional substrates 4-nitrophenol and 3-methyl-4-nitrophenol. With 4-nitrophenol, the initial rate of the mutant M22L/L380I enzyme is 10fold higher than that of the wild-type enzyme, the catalytic efficiency for 4-nitrophenol degradation is 11fold higher, and with 3-methyl-4-nitrophenol, the initial rate is 4fold higher compared to the wild-type enzyme
M22L/L380M
simultaneous saturation mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
M22S/L380V
simultaneous saturation mutagenesis, the mutant shows 20% enhanced degradation of 4-nitrophenol compared to mutant M22L/L380I
L380I
-
site-directed mutagenesis, the mutant shows unaltered activity with 4-nitrophenol compared to the wild-type enzyme
-
M22L
-
site-directed mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
-
M22L/L380I
-
error-prone PCR, protein engineering for nitrite removal, the mutant enzyme accepts two addtional substrates 4-nitrophenol and 3-methyl-4-nitrophenol. With 4-nitrophenol, the initial rate of the mutant M22L/L380I enzyme is 10fold higher than that of the wild-type enzyme, the catalytic efficiency for 4-nitrophenol degradation is 11fold higher, and with 3-methyl-4-nitrophenol, the initial rate is 4fold higher compared to the wild-type enzyme
-
M22L/L380M
-
simultaneous saturation mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
-
M22S/L380V
-
simultaneous saturation mutagenesis, the mutant shows 20% enhanced degradation of 4-nitrophenol compared to mutant M22L/L380I
-