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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

Reaction

progesterone
+
reduced ferredoxin
 +
O2
 +
H+
=
15beta-hydroxyprogesterone
 +
oxidized ferredoxin
 +
H2O

Synonyms

15beta-hydroxylase, 15beta-hydroxylase CYP106A2, BmCYP106A2, Cyp106A1, CYP106A2, cytochrome P-450meg, cytochrome P450meg, steroid-15-beta-monooxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.15.8 steroid 15beta-monooxygenase

Engineering

Engineering on EC 1.14.15.8 - steroid 15beta-monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
F165I
1.25fold increase in progesterone conversion
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
T248V
-
specificity for 15beta-hydroxylation is improved
T396R
mutant does not produce any hydroxylated product up to an adrenodoxin concentration of 0.1 mM
additional information