1.14.15.8: steroid 15beta-monooxygenase
This is an abbreviated version!
For detailed information about steroid 15beta-monooxygenase, go to the full flat file.
Word Map on EC 1.14.15.8
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1.14.15.8
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megaterium
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p-450-dependent
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ferredoxins
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synthesis
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adrenodoxin
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autologous
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triterpene
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11-oxidase
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testosterone
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flavodoxin
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flavoprotein
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hydroxylases
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aniline
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11-deoxycortisol
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nadph-dependent
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fmn-containing
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paramagnetic
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iron-sulfur
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biocatalyst
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11-keto
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11-deoxycorticosterone
- 1.14.15.8
- megaterium
-
p-450-dependent
- ferredoxins
- synthesis
- adrenodoxin
-
autologous
-
triterpene
-
11-oxidase
- testosterone
- flavodoxin
- flavoprotein
- hydroxylases
- aniline
- 11-deoxycortisol
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nadph-dependent
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fmn-containing
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paramagnetic
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iron-sulfur
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biocatalyst
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11-keto
- 11-deoxycorticosterone
Reaction
Synonyms
15beta-hydroxylase, 15beta-hydroxylase CYP106A2, BmCYP106A2, Cyp106A1, CYP106A2, cytochrome P-450meg, cytochrome P450meg, steroid-15-beta-monooxygenase
ECTree
Advanced search results
Engineering
Engineering on EC 1.14.15.8 - steroid 15beta-monooxygenase
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A106T
kcat/Km for conversion of 11-deoxycortisol is 3.17fold higher than wild-type value, 1.43fold increase in progesterone conversion
A106T/Q189K/T399S/R409L
kcat/Km for conversion of 11-deoxycortisol is 4.3fold higher than wild-type value, 1.13fold increase in progesterone conversion
A106T/R409L
kcat/Km for conversion of 11-deoxycortisol is 3fold higher than wild-type value, 1.43fold increase in progesterone conversion
A243S
mutant engineered for steroid 9alpha- and 6beta-hydroxylation, 10fold increase in the selectivity towards 6alpha-hydroxylation of progesterone. Mutant produces 3.4% 15beta-hydroxy-progesterone plus 4.6% 11alpha-hydroxy-progesterone plus 2.4% 9alpha-hydroxy-progesterone plus 82.7% 6beta-hydroxy-progesterone
A395L
Vmax/Km for progesterone is 2fold lower than wild-type value
D153V/I214F
kcat/Km for conversion of 11-deoxycortisol is 2.64fold higher than wild-type value, progesterone conversion is 93% of wild-type value
D217V
kcat/Km for conversion of 11-deoxycortisol is 2.68fold higher than wild-type value, 1.18fold increase in progesterone conversion
E90V/D185G
Vmax/Km for progesterone is 1.3fold higher than wild-type value
F165L/A395E/G397V
mutant engineered for steroid 9alpha- and 6beta-hydroxylation, 10fold increase in the selectivity towards progesterone 9lpha-hydroxylation. Mutant produces 11.3% 15beta-hydroxy-progesterone plus 17.2% 11alpha-hydroxy-progesterone plus 59.7% 9alpha-hydroxy-progesterone plus 6.8% 6beta-hydroxy-progesterone
G397P
the mutant exhibits 2% of the wild-type activity, Vmax/Km for progesterone is 51.7fold lower than wild-type value
I86T
Vmax/Km for progesterone is 2fold higher than wild-type value
K27R/I71T/I215T
Vmax/Km for progesterone is 2.5fold higher than wild-type value
Q398S
Vmax/Km for progesterone is 5fold lower than wild-type value
S394I
Vmax/Km for progesterone is 7.5fold lower than wild-type value
S72A/V73I
mutant does not show a better stability in the crystallization process than the wild-type protein
T396R
mutant does not produce any hydroxylated product up to an adrenodoxin concentration of 0.1 mM
additional information
modelling of CYP106A2 and site-directed mutagenesis of the protein to check the accuracy of the computer-derived model of CYP106A2
additional information
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recombinant reconstitution of the whole cell conversion of 11-keto-beta-boswellic acid in Bacillus megaterium strain MS941 by coexpression of heterologous redox chain of the P450, bovine adrenodoxin reductase, and bovine adrenodoxin, as well as a a NADPH-regenerating system
additional information
Priestia megaterium ATCC 13368
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recombinant reconstitution of the whole cell conversion of 11-keto-beta-boswellic acid in Bacillus megaterium strain MS941 by coexpression of heterologous redox chain of the P450, bovine adrenodoxin reductase, and bovine adrenodoxin, as well as a a NADPH-regenerating system
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additional information
Priestia megaterium ATCC 13368
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construction of a CYP106A2 knockout strain
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