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EC Tree
IUBMB Comments A single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17alpha-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in Reaction (1). The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13alpha-lactone, such as testololactone, is shown in Reaction (2). The oxidative cleavage of the 17beta-side-chain of 17alpha-hydroxyprogesterone to produce androstenedione and acetate is shown in Reaction (3). Reaction (1) is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
steroid hydroxylase, baeyer-villiger monooxygenase, cyp106a2, steroid monooxygenase, steroid hormone hydroxylase, steroid hydroxylating cytochrome,
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17alpha-Hydroxyprogesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, side-chain cleaving)
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Androgen hydroxylase
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Androstenedione, NADPH2:oxygen oxidoreductase (17-hydroxylating, lactonizing)
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Baeyer-Villiger monooxygenase
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Hydroxylase, steroid
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NADPH-dependent steroid Baeyer-Villiger monooxygenase
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Oxygenase, steroid mono-
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Progesterone, NADPH2:oxygen oxidoreductase (20-hydroxylating, ester-producing)
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Steroid hormone hydroxylase
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Steroid hydroxylase
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steroid hydroxylating cytochrome
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Steroid-ketone monooxygenase
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Steroid monooxygenase
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17alpha-hydroxyprogesterone + NADPH + H+ + O2 = androstenedione + acetate + NADP+ + H2O
(3)
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a ketosteroid + NADPH + H+ + O2 = a steroid ester/lactone + NADP+ + H2O
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androstenedione + NADPH + H+ + O2 = testololactone + NADP+ + H2O
(2)
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progesterone + NADPH + H+ + O2 = testosterone acetate + NADP+ + H2O
(1)
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ketosteroid,NADPH:oxygen oxidoreductase (20-hydroxylating, ester-producing/20-hydroxylating, side-chain cleaving/17-hydroxylating, lactonizing)
A single FAD-containing enzyme catalyses three types of monooxygenase (Baeyer-Villiger oxidation) reaction. The oxidative esterification of a number of derivatives of progesterone to produce the corresponding 17alpha-hydroxysteroid 17-acetate ester, such as testosterone acetate, is shown in Reaction (1). The oxidative lactonization of a number of derivatives of androstenedione to produce the 13,17-secoandrosteno-17,13alpha-lactone, such as testololactone, is shown in Reaction (2). The oxidative cleavage of the 17beta-side-chain of 17alpha-hydroxyprogesterone to produce androstenedione and acetate is shown in Reaction (3). Reaction (1) is also catalysed by EC 1.14.99.4 (progesterone monooxygenase), and Reactions (2) and (3) correspond to that catalysed by EC 1.14.99.12 (androst-4-ene-3,17-dione monooxygenase). The possibility that a single enzyme is responsible for the reactions ascribed to EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded.
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1,4-Pregnadiene-17alpha,21-diol-3,11,20-trione + NADPH + O2
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11-deoxycortisol + NADPH + O2
? + NADP+ + H2O
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?
11beta-Hydroxyprogesterone + NADPH + O2
?
17alpha-hydroxypregnenolone + NADPH + O2
?
17alpha-Hydroxyprogesterone + NADPH + O2
androstenedione + acetate + NADP+ + H2O
18-Hydroxydeoxycorticosterone + NADPH + O2
?
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?
21-Deoxycortisol + NADPH + O2
?
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?
Aldosterone + NADPH + O2
?
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?
androstenedione + NADPH + O2
3-oxo-13,17-secoandrost-4-eno-17,13-alpha-lactone + NADP+ + H2O
Corticosterone + NADPH + O2
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?
Cortisol + NADPH + O2
?
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?
Cortisone + NADPH + O2
?
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?
deoxycorticosterone + NADPH + O2
?
phenylacetone + NADPH + H+ + O2
benzylacetate + NADP+ + H2O
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?
Pregnenolone + NADPH + O2
?
progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
additional information
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the enzyme does not accept 3beta-hydroxy-5-ene steroids as substrates
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?
11beta-Hydroxyprogesterone + NADPH + O2
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?
11beta-Hydroxyprogesterone + NADPH + O2
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?
17alpha-hydroxypregnenolone + NADPH + O2
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?
17alpha-hydroxypregnenolone + NADPH + O2
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?
17alpha-Hydroxyprogesterone + NADPH + O2
androstenedione + acetate + NADP+ + H2O
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?
17alpha-Hydroxyprogesterone + NADPH + O2
androstenedione + acetate + NADP+ + H2O
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the 17-ketosteroid acts first with the enzyme, and then NADPH
4-androstene-3,17-dione
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17alpha-Hydroxyprogesterone + NADPH + O2
androstenedione + acetate + NADP+ + H2O
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the 17-ketosteroid acts first with the enzyme, and then NADPH
4-androstene-3,17-dione
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17alpha-Hydroxyprogesterone + NADPH + O2
androstenedione + acetate + NADP+ + H2O
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?
androstenedione + NADPH + O2
3-oxo-13,17-secoandrost-4-eno-17,13-alpha-lactone + NADP+ + H2O
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?
androstenedione + NADPH + O2
3-oxo-13,17-secoandrost-4-eno-17,13-alpha-lactone + NADP+ + H2O
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i.e. testololactone
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androstenedione + NADPH + O2
3-oxo-13,17-secoandrost-4-eno-17,13-alpha-lactone + NADP+ + H2O
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i.e. testololactone
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androstenedione + NADPH + O2
3-oxo-13,17-secoandrost-4-eno-17,13-alpha-lactone + NADP+ + H2O
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deoxycorticosterone + NADPH + O2
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deoxycorticosterone + NADPH + O2
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Pregnenolone + NADPH + O2
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Pregnenolone + NADPH + O2
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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?
progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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?
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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progesterone + NADPH + H+ + O2
Testosterone acetate + NADP+ + H2O
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?
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FAD
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FAD
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enzyme contains 1.6 mol of FAD per mol of enzyme
NADPH
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5-Pregnene-3beta,20alpha-diol
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lactonization of androstenedione
pregnenolone
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and other C21-20-ketosteroids which are the substrates for oxygenative esterification of the enzyme, strongly inhibit lactonization of androstenedione
progesterone
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strong, competitive inhibitor of lactonization of 17-ketosteroids
testosterone
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lactonization of androstenedione
Testosterone acetate
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lactonization of androstenedione
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Genetic Diseases, Inborn
Regulation of steroid hydroxylase gene expression: importance to physiology and disease.
Herpes Zoster
Cytological maturity of zona fasciculata cells in the fetal sheep adrenal following ACTH infusion: an electron microscope study.
Herpes Zoster
Differential effects of adrenocorticotropic hormone on steroid hydroxylase activities in the inner and outer zones of the guinea pig adrenal cortex.
Hypotension
Inhibition of aldosterone biosynthesis by staurosporine.
Prostatic Neoplasms
Regulation of steroid hydroxylase CYP7B1 by androgens and estrogens in prostate cancer LNCaP cells.
Tuberculosis
Crystal structure of the TetR/CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance.
Tuberculosis
Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA.
Tuberculosis
Resolution of fused bicyclic ketones by a recombinant biocatalyst expressing the Baeyer-Villiger monooxygenase gene Rv3049c from Mycobacterium tuberculosis H37Rv.
Tuberculosis
The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase.
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0.07
O2
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with progesterone and NADPH as cosubstrates
0.0004 - 0.055
progesterone
0.00044
NADPH
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pH 8.3, 37°C
0.002
NADPH
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with androstenedione and O2 as cosubstrates
0.0043
NADPH
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with progesterone and O2 as cosubstrates
0.2
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.2
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.6
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.8
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
2.6
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.0004
progesterone
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0.055
progesterone
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pH 8.3, 37°C
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0.2
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.6
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.5
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.8
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
3
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
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1.2
phenylacetone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.2
phenylacetone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.5
phenylacetone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
2.1
phenylacetone
mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
2.2
phenylacetone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
2.6
phenylacetone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
0.1
progesterone
kcat_Km less than 0.1 1/sec*min, mutant enzyme L500Y, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.4
progesterone
mutant enzyme K295A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.7
progesterone
mutant enzyme V291A, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
1.8
progesterone
wild type enzyme, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
3.9
progesterone
mutant enzyme P157Q, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
5.2
progesterone
mutant enzyme T345L, in 50 mM Tris/HCl, pH 7.5, temperature not specified in the publication
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additional information
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6.5
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androstenedione monooxygenase reaction
7.8
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progesterone monooxygenase reaction
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5.5 - 8
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pH 5.5: about 20% of maximal activity, pH 8.0: about 40% of maximal activity, androstenedione monooxygenase activity
6 - 9
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pH 6.0: about 35% of maximal activity, pH 9.0: about 65% of maximal activity, progesterone monooxygenase activity
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45
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progesterone monooxygenase activity
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ATTC 11011
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brenda
ATTC 11011
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brenda
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brenda
strain ATCC 13368
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brenda
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UniProt
brenda
starin IFO 2228
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brenda
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O50641_RHORH
549
0
60136
TrEMBL
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116000
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gel filtration, gel electrophoresis
56000
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2 * 56000, SDS-PAGE
60000
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x * 60000, SDS-PAGE
60133
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x * 60133, calculated from the deduced amino acid sequence
60919
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x * 60919, holoenzyme, calculated from the deduced amino acid sequence
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?
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x * 60000, SDS-PAGE
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x * 60133, calculated from the deduced amino acid sequence
?
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x * 60919, holoenzyme, calculated from the deduced amino acid sequence
dimer
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2 * 56000, SDS-PAGE
dimer
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2 * 56000, SDS-PAGE
-
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sitting drop vapor diffusion method, using 1.8-2.2 M MgSO4, 0.1 M MES/HCl, pH 6.2-6.5
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K295A
the mutant is 3times more active than the wild type enzyme
L500Y
the mutant is about 2.5times more active than the wild type enzyme
P157Q
the mutant shows wild type activity
T345L
the mutation turns the enzyme inactive against progesterone without altering the catalytic efficiency for phenylacetone
V291A
the mutant is less active than the wild type enzyme
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-80°C, Tris buffer, stable for more than 6 months, enzyme in crude extract
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Ni2+-affinity column chromatography and Superdex 75 gel filtration
recombinant enzyme from Escherichia coli
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expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli BL21(DE3) CodonPlus cells
expression in Escherichia coli
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reconstitution of recombinant protein using adrenodoxin and adrenodoxin reductase
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Itagaki, E.
Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Oxygenative lactonization of androstenedione to testololactone
J. Biochem.
99
825-832
1986
Ilyonectria destructans, Ilyonectria destructans ATTC 11011
brenda
Itagaki, E.
Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization
J. Biochem.
99
815-824
1986
Ilyonectria destructans, Ilyonectria destructans ATTC 11011
brenda
Morii, S.; Sawamoto, S.; Yamauchi, Y.; Miyamoto, M.; Iwami, M.; Itagaki, E.
Steroid monooxygenase of Rhodococcus rhodochrous: sequencing of the genomic DNA, and hyperexpression, purification, and characterization of the recombinant enzyme
J. Biochem.
126
624-631
1999
Rhodococcus rhodochrous
brenda
Virus, C.; Bernhardt, R.
Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening
Lipids
43
1133-1141
2008
Priestia megaterium
brenda
Franceschini, S.; van Beek, H.L.; Pennetta, A.; Martinoli, C.; Fraaije, M.W.; Mattevi, A.
Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase
J. Biol. Chem.
287
22626-22634
2012
Rhodococcus rhodochrous (O50641), Rhodococcus rhodochrous
brenda
Swizdor, A.
Baeyer-Villiger oxidation of some C19 steroids by Penicillium lanosocoeruleum
Molecules
18
13812-13822
2013
Penicillium lanosocoeruleum
brenda
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