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
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lauric
- porphyrin
-
photolysis
-
kbind
-
benzyl
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first-order
- flash
- sulfur
- peroxynitrite
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ironiv-oxo
Reaction
Synonyms
CYP119, cytochrome P450 119, P450st
ECTree
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Substrates Products
Substrates Products on EC 1.14.13.B28 - monooxygenase CYP119A2
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REACTION DIAGRAM
styrene + cumen hydroperoxide
styrene epoxide + ?
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?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
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?
styrene + NADH + H+ + O2
styrene epoxide + NAD+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene epoxide + NADP+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene + NADPH + H+ + O2
styrene epoxide + NADP+ + H2O
the initial rate of catalysis with NADH is slightly higher than with NADPH
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?
styrene + tert-butyl hydroperoxide
styrene epoxide + ?
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?
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the initial activities of CYP119 in the presence of tert-butyl hydroperoxide and cumene hydroperoxide are two- and fivefold higher than that observed with H2O2. tert-Butyl hydroperoxide increases both turnover rate and the stability of the enzyme under the oxidizing reaction conditions
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additional information
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the initial activities of CYP119 in the presence of tert-butyl hydroperoxide and cumene hydroperoxide are two- and fivefold higher than that observed with H2O2. tert-Butyl hydroperoxide increases both turnover rate and the stability of the enzyme under the oxidizing reaction conditions
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additional information
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the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant
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?
additional information
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electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
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?
additional information
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the enzyme also catalyzes hydrogen peroxide-driven ethylbenzene hydroxylation. The ethylbenzene hydroxylation activity is higher than the styrene epoxidation activity, maybe due to a difference in the binding affinity of the two substrates. The rate-limiting steps of ethylbenzene hydroxylation and styrene epoxidation are the same, and may be any step before formation of the active oxidant
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-
?
additional information
?
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electron-transfer reaction between the electrode and heme iron. Direct electrochemistry of P450st in a didodecyldimethylammonium bromide film on a plastic formed carbon electrode is demonstrated. A quasi-reversible redox response is observed at temperatures of up to 80°C
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?