1.11.2.4: fatty-acid peroxygenase
This is an abbreviated version!
For detailed information about fatty-acid peroxygenase, go to the full flat file.
Word Map on EC 1.11.2.4
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1.11.2.4
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peroxygenases
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oletje
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alkene
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self-sufficient
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cumene
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phanerochaete
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chrysosporium
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monooxygenation
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paucimobilis
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peroxygenation
- 1.11.2.4
-
peroxygenases
-
oletje
- alkene
-
self-sufficient
- cumene
-
phanerochaete
-
chrysosporium
-
monooxygenation
- paucimobilis
-
peroxygenation
Reaction
Synonyms
alpha-fatty acid hydroxylase, CYP152A1, CYP152A2, CYP152B1, CYP505, cytochrome P450 monooxygenase, cytochrome P450BSbeta, fatty-acid hydroxylase, fatty-acid subterminal hydroxylase, hydrogen peroxide-dependent cytochrome P450BSbeta, hydrogen peroxide-dependent fatty acid alpha-hydroxylase, hydrogen peroxide-dependent peroxygenase cytochrome P450, P450 BM-3 peroxygenase 21B3, P450 peroxygenase, P450BSbeta, P450CLA, P450foxy, P450SPalpha, peroxygenase cytochrome P450, peroxygenase P450, peroxygenase P450SPalpha
ECTree
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Engineering
Engineering on EC 1.11.2.4 - fatty-acid peroxygenase
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A246K
the mutant shows a large decrease in activity and a roughly 19fold lower affinity for myristic acid than the wild type enzyme
A246S
the mutation decreases the catalytic activity, but does not affect affinity for myristic acid
A246V
the mutant shows slightly reduced activity and moderately reduced affinity for myristic acid
F250K
the mutant shows decreased specific activity compared to the wild type enzyme
F79L
the specific activity is reduced by half compared to the wild type enzyme
F79L/V170F
the double mutant exhibits 10% of the activity of the wild type enzyme
I244K
the mutant shows decreased specific activity compared to the wild type enzyme
I247K
the mutant shows decreased specific activity compared to the wild type enzyme
L237K
the mutants shows specific activity similar to the wild type enzyme
L241K
the mutants shows specific activity similar to the wild type enzyme
L251K
the mutant shows decreased specific activity compared to the wild type enzyme
P243A
the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450
P243H
inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243K
inactive, the mutant gives an absorption spectrum characteristic of a nitrogenous ligand-bound form of a ferric P450
P243S
the mutant shows decreased specific activity compared to the wild type enzyme and gives an absorption spectrum that is not characteristic of a nitrogenous ligand-bound form of a ferric P450
R242A
the mutant shows about a 5fold lower affinity than the wild type for myristic acid, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution
R242K
S248K
the mutant shows decreased specific activity compared to the wild type enzyme
V170F
V245K
the mutant shows decreased specific activity compared to the wild type enzyme
Y249K
the mutant shows decreased specific activity compared to the wild type enzyme
F878A
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P450 BM-3 heme domain containing the single amino acid substitution F87A is significantly more active than wild type heme domain in reactions driven by H2O2
the mutant enzyme bound with deuterated myristic acid shows greatly increased rate of 3,5,3',5'-tetramethylbenzidine oxidation
R242K
the mutant shows a large decrease in activity for myristic acid and H2O2, if cumene hydroperoxide is used instead of H2o2, however, the Km value is not affected much by this substitution
the hydroxylation activity of V170F for myristic acid is about one third of that of the wild type, but its catalytic activities for aromatic hydroxylation in the presence of octanoic acid or nonanoic acid are comparable to the catalytic activity of the wild type with pentanoic acid
V170F
the mutant exhibits 30% of the activity of the wild type enzyme