1.14.13.B28: monooxygenase CYP119A2
This is an abbreviated version!
For detailed information about monooxygenase CYP119A2, go to the full flat file.
Word Map on EC 1.14.13.B28
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1.14.13.B28
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lauric
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porphyrin
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photolysis
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kbind
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benzyl
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first-order
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flash
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sulfur
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peroxynitrite
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ironiv-oxo
- 1.14.13.B28
-
lauric
- porphyrin
-
photolysis
-
kbind
-
benzyl
-
first-order
- flash
- sulfur
- peroxynitrite
-
ironiv-oxo
Reaction
Synonyms
CYP119, cytochrome P450 119, P450st
ECTree
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Engineering
Engineering on EC 1.14.13.B28 - monooxygenase CYP119A2
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delL151-E156
the Km value of the mutant is about 2times lower than that of the wild-type.
F310A/A320Q
site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s
delL151-E156
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the Km value of the mutant is about 2times lower than that of the wild-type.
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F310A/A320Q
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site-directed mutagenesis, the mutant exhibits a 30 mV positive shift in redox potential for the FeIII/FeII couple compared with wild-type P450st due to weakening of the electron-donating effect (push effect) of the proximal thiolate in the mutant. This result indicates that the electron density around the heme is decreased, and thus the Lewis acidity of the heme is expected to be increased. Mutant F310A/A320Q maintains higher thermal stability than typical P450s
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