1.14.99.14: progesterone 11alpha-monooxygenase
This is an abbreviated version!
For detailed information about progesterone 11alpha-monooxygenase, go to the full flat file.
Reaction
Synonyms
CYP106A2, CYP5311B1, progesterone 11alpha-hydroxylase, steroid 11alpha-hydroxylase
ECTree
1.14.99.14 progesterone 11alpha-monooxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.99.14 - progesterone 11alpha-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A106T/A395I
site-directed mutagenesis, the mutant shows 14.3fold higher regioselectivity for 11alpha-hydroxylation and 39.3fold increased catalytic efficiency compared to the wild-type enzyme
A106T/A395I/R409L
site-directed mutagenesis, the mutant shows 12.6fold higher regioselectivity for 11alpha-hydroxylation and 108fold increased catalytic efficiency compared to the wild-type enzyme
A106T/A395W/G379K/R409L
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
A243V/A395I
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
A243V/A395W/G397K
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
A395I
site-directed mutagenesis, the mutant shows 8.9fold higher 11alpha-hydroxylation activity compared to the wild-type enzyme
A395W/G397K
site-directed mutagenesis, the mutant shows 11.5fold higher 11alpha-hydroxylation activity compared to the wild-type enzyme
D217V/A395I
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
M155I/F165L/A395I
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
T247V/A395I
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
T247W/A395W/G379K
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
T248V/A395I
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
T89N/A106T/A395I/R409L
site-directed mutagenesis, the mutant shows higher regioselectivity for 11alpha-hydroxylation and increased catalytic efficiency compared to the wild-type enzyme
T89N/A395I
site-directed mutagenesis, the mutant shows 11.8fold higher regioselectivity for 11alpha-hydroxylation and 24.4fold increased catalytic efficiency compared to the wild-type enzyme. The production of 15beta-hydroxyprogesterone decreases from 50.4% of the wild-type to 4.8% of mutant T89N/A395I enzyme, whereas that of 11alpha-hydroxyprogesterone increases from 27.7% to 80.9%
additional information
additional information
direction of the regioselectivity of the enzyme towards hydroxylation at position 11 in the C ring of the steroid through a combination of saturation mutagenesis and rational site-directed mutagenesis, with aid of data from a homology model of CYP106A2 containing docked progesterone, together with site-directed mutagenesis of active site residues. Distributions of amounts of monohydroxylated progesterone products (15beta-,11alpha-, 9alpha-, and 6beta-hydroxyprogesterone) in vivo of wild-type and mutant enzymes, overview
additional information
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gene CYP509C12, production of a recombinant Pichia pastoris engieered to coexpress gene CYP509C12, ecoding the enzyme with the NAD(P)H-dependent reductase also from Rhizopus oryzae, to improve electron transfer to CYP509C12 and thus increases the production of 11-hydroxyprogesterone by 7fold. The engineered strain displays total bioconversion of progesterone into 11alpha-hydroxyprogesterone and small amounts of 6beta-hydroxyprogesterone and is useful for biotechnologic applications
additional information
Rhizopus arrhizus RA 99-880
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gene CYP509C12, production of a recombinant Pichia pastoris engieered to coexpress gene CYP509C12, ecoding the enzyme with the NAD(P)H-dependent reductase also from Rhizopus oryzae, to improve electron transfer to CYP509C12 and thus increases the production of 11-hydroxyprogesterone by 7fold. The engineered strain displays total bioconversion of progesterone into 11alpha-hydroxyprogesterone and small amounts of 6beta-hydroxyprogesterone and is useful for biotechnologic applications
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