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Information on EC 1.14.14.197 - progesterone 11alpha-monooxygenase
for references in articles please use BRENDA:EC1.14.14.197
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.197 progesterone 11alpha-monooxygenase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) enzyme. The enzyme, isolated from fungi, can hydroxylate testosterone, androst-4-ene-3,17-dione, and 11-deoxycorticosterone, forming the respective 11α-hydroxy compounds (cf. EC 1.14.15.4, steroid 11β-monooxygenase). The CYP509C12 enzyme from Rhizopus arrhizus can also 6-hydroxylate testosterone and 11-deoxycorticosterone, forming the respective β-hydroxy compounds .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
show+
+
=
+
+
+
[reduced NADPHhemoprotein reductase]
+
=
+
[oxidized NADPHhemoprotein reductase]
+
Synonyms
CYP106A2, CYP509C12, CYP5311B1, CYP68L1, CYP68L8, EC 1.14.99.14, progesterone 11alpha-hydroxylase, steroid 11alpha-hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP509C12
-
-
-
-
CYP5311B1
CYP68L1
-
-
-
-
CYP68L8
-
-
-
-
EC 1.14.99.14
-
-
formerly
-
progesterone 11alpha-hydroxylase
-
-
-
-
steroid 11alpha-hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
progesterone + [reduced NADPHhemoprotein reductase] + O2 = 11alpha-hydroxyprogesterone + [oxidized NADPHhemoprotein reductase] + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
progesterone,[reduced NADPHhemoprotein reductase]:oxygen oxidoreductase (11alpha-hydroxylating)
A cytochrome P-450 (heme-thiolate) enzyme. The enzyme, isolated from fungi, can hydroxylate testosterone, androst-4-ene-3,17-dione, and 11-deoxycorticosterone, forming the respective 11alpha-hydroxy compounds (cf. EC 1.14.15.4, steroid 11beta-monooxygenase). The CYP509C12 enzyme from Rhizopus arrhizus can also 6-hydroxylate testosterone and 11-deoxycorticosterone, forming the respective beta-hydroxy compounds [2].
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CAS REGISTRY NUMBER
COMMENTARY
37256-77-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
16,17alpha-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16,17alpha-epoxyprogesterone + A + H2O
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
11-deoxycorticosterone + AH2 + O2
? + A + H2O
-
Substrates: -
Products: -
Products: -
?
11-deoxycorticosterone + AH2 + O2
? + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
11alpha-hydroxyprogesterone + NADPH + O2
6beta,11alpha-dihydroxyprogesterone
-
Substrates: -
Products: -
Products: -
?
11alpha-hydroxyprogesterone + NADPH + O2
6beta,11alpha-dihydroxyprogesterone
-
Substrates: -
Products: -
Products: -
?
16,17alpha-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16,17alpha-epoxyprogesterone + A + H2O
Substrates: -
Products: -
Products: -
?
16,17alpha-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16,17alpha-epoxyprogesterone + A + H2O
Absidia caerulea AS3.65
Substrates: -
Products: -
Products: -
?
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
Rhizopus arrhizus CICC 40467
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Aspergillus ochraceus CICC41473
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Beauveria bassiana ACCC30728
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Cunninghamella elegans CICC40250
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Metarhizium anisopliae ACCC30194
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Rhizopus stolonifer CGMCC33900
-
Substrates: -
Products: -
Products: -
?
19-nortestosterone + NADPH + O2
11alpha-hydroxy-19-nortestosterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
19-nortestosterone + NADPH + O2
11alpha-hydroxy-19-nortestosterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: multicomponent monooxygenase system
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: necessary step in the synthesis of cortico-steroid hormones
Products: -
Products: -
?
testosterone + AH2 + O2
11alpha-hydroxytestosterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
testosterone + AH2 + O2
11alpha-hydroxytestosterone + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows low activity on progesterone and no activities on testosterone and 11-deoxycortisol
Products: -
Products: -
?
additional information
?
-
Absidia caerulea AS3.65
Substrates: the enzyme shows low activity on progesterone and no activities on testosterone and 11-deoxycortisol
Products: -
Products: -
?
additional information
?
-
-
Substrates: 11alpha-hydroxylase induced by progesterone or 19-nortestosterone is free from associated 6beta-hydroxylase or 17beta-hydroxysteroid dehydrogenase activity, but induction with 11alpha-hydroxyprogesterone yields an enzyme with both 6beta- and 11alpha-hydroxylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 11alpha-hydroxylase induced by progesterone or 19-nortestosterone is free from associated 6beta-hydroxylase or 17beta-hydroxysteroid dehydrogenase activity, but induction with 11alpha-hydroxyprogesterone yields an enzyme with both 6beta- and 11alpha-hydroxylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is capable of converting useful pharmaceutical targets such as 3-oxo-DELTA4-steroids (e.g., testosterone, 11-deoxycorticosterone, androstenedione, and progesterone) mainly into their 15beta-hydroxy homologues. In addition, the enzyme hydroxylates progesterone to a minor extent at the 11alpha-, 9alpha-, and 6beta-positions
Products: -
Products: -
?
additional information
?
-
Substrates: CYP106A2-catalyzed hydroxylations of progesterone at the 15beta-, 11alpha-, 9alpha-, and 6beta-positions
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydroxylations take place predominantly at 11alpha and 6beta positions of the steroid ring system
Products: -
Products: -
?
additional information
?
-
Rhizopus arrhizus RA 99-880
-
Substrates: hydroxylations take place predominantly at 11alpha and 6beta positions of the steroid ring system
Products: -
Products: -
?
additional information
?
-
-
Substrates: multi-enzyme complex contains cytochrome P450 and NADPH cytochrome c reductase
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
additional information
?
-
Substrates: the enzyme is capable of converting useful pharmaceutical targets such as 3-oxo-DELTA4-steroids (e.g., testosterone, 11-deoxycorticosterone, androstenedione, and progesterone) mainly into their 15beta-hydroxy homologues. In addition, the enzyme hydroxylates progesterone to a minor extent at the 11alpha-, 9alpha-, and 6beta-positions
Products: -
Products: -
?
11-deoxycorticosterone + AH2 + O2
? + A + H2O
-
Substrates: -
Products: -
Products: -
?
11-deoxycorticosterone + AH2 + O2
? + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
16alpha,17-epoxyprogesterone + AH2 + O2
11alpha-hydroxy-16alpha,17-epoxyprogesterone + A + H2O
Rhizopus arrhizus CICC 40467
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Aspergillus ochraceus CICC41473
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Beauveria bassiana ACCC30728
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Cunninghamella elegans CICC40250
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Metarhizium anisopliae ACCC30194
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
17alpha-hydroxyprogesterone + AH2 + O2
11alpha,17alpha-dihydroxyprogesterone + A + H2O
Rhizopus stolonifer CGMCC33900
-
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + AH2 + O2
11alpha-hydroxyprogesterone + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: activity dependent upon NADPH and O2
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: multicomponent monooxygenase system
Products: -
Products: -
?
progesterone + NADPH + O2
11alpha-hydroxyprogesterone + NADP+ + H2O
-
Substrates: necessary step in the synthesis of cortico-steroid hormones
Products: -
Products: -
?
testosterone + AH2 + O2
11alpha-hydroxytestosterone + A + H2O
-
Substrates: -
Products: -
Products: -
?
testosterone + AH2 + O2
11alpha-hydroxytestosterone + A + H2O
Rhizopus arrhizus RA 99-880
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395I
0.026
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395W/G397K
0.028
progesterone
pH not specified in the publication, 30°C, mutant D217V/A395I
0.032
progesterone
pH not specified in the publication, 30°C, mutants A395I and M155I/F165L/A395I
0.038
progesterone
pH not specified in the publication, 30°C, mutant T247V/A395I
0.039
progesterone
pH not specified in the publication, 30°C, mutant T247W/A395W/G379K
0.046
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I/R409L
0.048
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395W/G379K/R409L
0.052
progesterone
pH not specified in the publication, 30°C, mutant T248V/A395I
0.055
progesterone
pH not specified in the publication, 30°C, mutant A395W/G397K
0.084
progesterone
pH not specified in the publication, 30°C, mutant T89N/A395I
0.091
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I
0.109
progesterone
pH not specified in the publication, 30°C, mutant T89N/A106T/A395I/R409L
0.203
progesterone
pH not specified in the publication, 30°C, wild-type
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
progesterone
pH not specified in the publication, 30°C, wild-type
0.9
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395W/G397K
1.1
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395I
1.2
progesterone
pH not specified in the publication, 30°C, mutant A395W/G397K
1.3
progesterone
pH not specified in the publication, 30°C, mutant A395I
1.9
progesterone
pH not specified in the publication, 30°C, mutant T247V/A395I
2.5
progesterone
pH not specified in the publication, 30°C, mutant T89N/A106T/A395I/R409L
2.7
progesterone
pH not specified in the publication, 30°C, mutant T247W/A395W/G379K
2.9
progesterone
pH not specified in the publication, 30°C, mutant T89N/A395I
3.5
progesterone
pH not specified in the publication, 30°C, mutant T248V/A395I
4.3
progesterone
pH not specified in the publication, 30°C, mutant D217V/A395I
4.5
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395W/G379K/R409L
5
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I
6.4
progesterone
pH not specified in the publication, 30°C, mutant M155I/F165L/A395I
6.9
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I/R409L
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
progesterone
pH not specified in the publication, 30°C, wild-type
21.7
progesterone
pH not specified in the publication, 30°C, mutant A395W/G397K
23.2
progesterone
pH not specified in the publication, 30°C, mutant T89N/A106T/A395I/R409L
34.2
progesterone
pH not specified in the publication, 30°C, mutant T89N/A395I
34.5
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395W/G397K
42
progesterone
pH not specified in the publication, 30°C, mutants A395II
49.9
progesterone
pH not specified in the publication, 30°C, mutant T247V/A395I
53.1
progesterone
pH not specified in the publication, 30°C, mutant A243V/A395I
55.1
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I
66.8
progesterone
pH not specified in the publication, 30°C, mutant T248V/A395I
70.6
progesterone
pH not specified in the publication, 30°C, mutant T247W/A395W/G379K
93.4
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395W/G379K/R409L
151.4
progesterone
pH not specified in the publication, 30°C, mutant A106T/A395I/R409L
151.5
progesterone
pH not specified in the publication, 30°C, mutant D217V/A395I
201.8
progesterone
pH not specified in the publication, 30°C, mutant M155I/F165L/A395I
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in complete medium, an increase in temperature inhibits 11alpha-hydroxylase activity and completely suppresses 6beta-hydroxylase activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the strain has steroid-hydroxylating activity and can introduce a hydroxyl group into the progesterone molecule mainly at positions C11(alpha) and C21 with predominant formation of 21-hydroxyprogesterone (deoxycortone). In addition, formation of 6beta,11alpha-dihydroxyprogesterone is observed
additional information
-
the strain has steroid-hydroxylating activity and can introduce a hydroxyl group into the progesterone molecule mainly at positions C11(alpha) and C21 with predominant formation of 21-hydroxyprogesterone (deoxycortone). In addition, formation of 6beta,11alpha-dihydroxyprogesterone is observed
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 components, rhizoporedoxin and rhizoporedoxin reductase, DEAE-cellulose chromatography
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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
-
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
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CYP509C12, cloning from a cDNA library, DNA and amino acid sequence determination and analysis, phylogenetic analysis, and recombinant expression in Pichia pastoris, coexpression with NAD(P)H-dependent reductase also from Rhizopus oryzae, which improves 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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP509C12 expression is induced by progesterone
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
membrane-associated enzymes catalyse several reactions of industrial interest, including steroid hydroxylation
synthesis
-
immobilisation of membrane-bound multi-enzyme complexes for industrial use
synthesis
because of its capacity to hydroxylate steroids, CYP106A2 is an interesting candidate for industrial production of steroids or their intermediates. CYP106A2 is known as a 15beta-hydroxylase, but also shows minor 11alpha-hydroxylase activity for progesterone. 11alpha-Hydroxyprogesterone is an important pharmaceutical compound with anti-androgenic and blood-pressure-regulating activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jayanthi, C.R.; Madyastha, P.; Madyastha, K.M.
Microsomal 11alpha-hydroxylation of progesterone in Aspergillus ochraceus: Part I: Characterization of the hydroxylase system
Biochem. Biophys. Res. Commun.
106
1262-1268
1982
Aspergillus ochraceus, Aspergillus ochraceus NRRL 405, Aspergillus ochraceus TS, Rhizopus arrhizus, Rhizopus stolonifer
brenda
Shibahara, M.; Moody, J.A.; Smith, L.L.
Microbial hydroxylations. V. 11alpha-hydroxylation of progesterone by cell-free preparations of Aspergillus ochraceus
Biochim. Biophys. Acta
202
172-179
1979
Aspergillus ochraceus, Aspergillus ochraceus NRRL 405, Priestia megaterium
brenda
Hanisch, W.H.; Dunnill, P.
Regeneration of the progesterone 11alpha-hydroxylase of Rhizopus nigricans by the use of periodate
Biotechnol. Lett.
2
123-126
1980
Rhizopus stolonifer
-
brenda
Ghosh, D.; Samanta, T.B.
11alpha-Hydroxylation of progesterone by cell free preparation of Aspergillus ochraceus TS
J. Steroid Biochem.
14
1063-1067
1981
Aspergillus ochraceus, Aspergillus ochraceus TS
brenda
Cresnar, B.; Breskvar, K.; Hudnik-Plevnik, T.
Resolution and reconstitution of the NADPH-cytochrome c (P-450) reductase induced by progesterone in Rhizopus nigricans
Biochem. Biophys. Res. Commun.
133
1057-1063
1985
Rhizopus stolonifer
brenda
Broad, D.F.; Pontin, S.; Dunnill, P.
Studies for the large scale isolation of membrane-associated progesterone 11alpha-hydroxylase:enzyme stability in Rhizopus nigricans ATCC 6277b cells
Enzyme Microb. Technol.
9
546-548
1986
Rhizopus stolonifer
-
brenda
Bonnerjea, J.; Pontin, S.; Hoare, M.; Dunnill, P.
Poly(ethylene glycol) precipitation and two aquaeous-phase separation of progesterone 11-alpha hydroxylase from Rhizopus nigricans
Appl. Microbiol. Biotechnol.
27
362-365
1988
Rhizopus stolonifer
-
brenda
Lenasi, H.; Hudnik-Plevnik, T.
Identification and partial characterization of cytosolic progesterone-binding sites in the filamentous fungus Rhizopus nigricans
Arch. Biochem. Biophys.
330
80-86
1996
Rhizopus stolonifer
brenda
Dutta, T.K.; Samanta, T.B.
Bioconversion of progesterone by the activated immobilized conidia of Aspergillus ochraceus TS
Curr. Microbiol.
39
309-312
1999
Aspergillus ochraceus, Aspergillus ochraceus G8, Aspergillus ochraceus TS, Rhizopus stolonifer
brenda
Kunic, B.; Makovec, T.; Breskvar, K.
Comparison of two monooxygenase systems with cytochrome P450 in filamentous fungus Rhizopus nigricans
Pflugers Arch.
439
R107-108
2000
Rhizopus stolonifer
brenda
Petric, S.; Hakki, T.; Bernhardt, R.; Zigon, D.; Cresnar, B.
Discovery of a steroid 11alpha-hydroxylase from Rhizopus oryzae and its biotechnological application
J. Biotechnol.
150
428-437
2010
Rhizopus arrhizus, Rhizopus arrhizus RA 99-880
brenda
Nguyen, K.T.; Virus, C.; Guennewich, N.; Hannemann, F.; Bernhardt, R.
Changing the regioselectivity of a P450 from C15 to C11 hydroxylation of progesterone
ChemBioChem
13
1161-1166
2012
Priestia megaterium (Q06069)
brenda
Chen, X.; Luo, X.; Cao, F.; Zhu, T.; Fan, Y.; Jia, X.; Shen, Y.
Molecular cloning, expression of CPR gene from Rhizopus oryzae into Rhizopus nigericans and its application in the 11alpha-hydroxylation of 16alpha, 17-epoxy-progesterone
Enzyme Microb. Technol.
66
28-34
2014
Rhizopus arrhizus, Rhizopus arrhizus CICC 40467
brenda
Wang, R.; Sui, P.; Hou, X.; Cao, T.; Jia, L.; Lu, F.; Singh, S.; Wang, Z.; Liu, X.
Cloning and identification of a novel steroid 11alpha-hydroxylase gene from Absidia coerulea
J. Steroid Biochem. Mol. Biol.
171
254-261
2017
Absidia caerulea (A0A173GQ95), Absidia caerulea AS3.65 (A0A173GQ95)
brenda
Gao, Q.; Qiao, Y.; Shen, Y.; Wang, M.; Wang, X.; Liu, Y.
Screening for strains with 11alpha-hydroxylase activity for 17alpha-hydroxy progesterone biotransformation
Steroids
124
67-71
2017
Aspergillus ochraceus, Aspergillus ochraceus CICC41473, Beauveria bassiana, Beauveria bassiana ACCC30728, Cunninghamella elegans, Cunninghamella elegans CICC40250, Metarhizium anisopliae, Metarhizium anisopliae ACCC30194, Rhizopus stolonifer, Rhizopus stolonifer CGMCC33900
brenda
Savinova, O.S.; Solyev, P.N.; Vasina, D.V.; Tyazhelova, T.V.; Fedorova, T.V.; Savinova, T.S.
Biotransformation of Progesterone by the ascomycete Aspergillus niger N402
Biochemistry (Moscow)
83
26-31
2018
Aspergillus niger, Aspergillus niger N402
brenda
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