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(+)-benzphetamine + [reduced NADPH-cytochrome P-450 reductase] + O2
N-demethyl-benzphetamine + [oxidized NADPH-cytochrome P-450 reductase] + H2O
-
-
-
?
11,17-dihydroxyprogesterone + NADH + O2
cortisol + NAD+ + H2O
-
-
-
?
11beta-hydroxyprogesterone + NADH + O2
corticosterone + NAD+ + H2O
-
-
-
?
16,17-dehydroprogesterone + NADPH + O2
16,17-dehydro-21-hydroxyprogesterone + NADP+ + H2O
-
-
-
?
17,17-dimethyl-18-norandrosta-1,4,13-trien-3-one + [reduced NADPH-hemoprotein reductase] + O2
16beta-hydroxy-17,17-dimethyl-18-norandrosta-1,4,13-trien-3-one + 16alpha-hydroxy-17,17-dimethyl-18-norandrosta-1,4,13-trien-3-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. metandienone
product identification by GC-EI-MS analysis
-
?
17,17-dimethyl-18-norandrosta-1,4,13-trien-3-one + [reduced NADPH-hemoprotein reductase] + O2
20beta-hydroxy-17,17-dimethyl-18-norandrosta-1,4,13-trien-3-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. metandienone
product identification by GC-EI-MS analysis
-
?
17-fluoro-progesterone + [reduced NADPH-P450 reductase] + O2
17-fluoro-11-deoxycorticosterone + [oxidized NADPH-P450 reductase] + H2O
-
-
-
-
?
17-hydroxy-progesterone + NADH + O2
17-hydroxy-11-deoxy-corticosterone + NAD+ + H2O
17-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
17-hydroxyprogesterone + NADPH + O2
corticosteroids + NADP+ + H2O
-
-
-
?
17-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
17alpha-hydroxy-progesterone + NADH + O2
17alpha-hydroxy-11-deoxy-corticosterone + NAD+ + H2O
-
preferred substrate
-
-
?
17alpha-hydroxyprogesterone + AH2 + O2
11-deoxycortisol + A + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
17alpha-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
17alpha-hydroxyprogesterone + NADPH + H+ + O2
17,21-dihydroxyprogesterone + NADP+ + H2O
17alpha-hydroxyprogesterone + NADPH + O2
11-deoxycortisol + NADP+ + H2O
17alpha-hydroxyprogesterone + NADPH + O2
17,21-dihydroxyprogesterone + NADP+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
17alpha-hydroxyprogesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycortisol + [oxidized NADPH-P450 reductase] + H2O
a steroid + electron donor + O2
a 21-hydroxysteroid + oxidized electron donor + H2O
-
essential step in synthesis of steroid hormones by adrenal gland
-
?
allopregnanolone + NADH + O2
21-hydroxy-allopregnanolone + NAD+ + H2O
-
isozyme CYP2D4, CYP2D6
-
-
?
DELTA5-pregnen-3beta,17alpha-diol-20-one + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
DELTA5-pregnen-3beta-ol-20-one + NADH + O2
deoxycorticosterone + NAD+ + H2O
progesterone + AH2 + O2
deoxycorticosterone + A + H2O
-
-
-
-
?
progesterone + NADH + O2
11-deoxycorticosterone + NAD+ + H2O
-
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
progesterone + NADPH + H+ + O2
11-deoxycorticosterone + NADP+ + H2O
progesterone + NADPH + H+ + O2
deoxycorticosterone + NADP+ + H2O
progesterone + NADPH + O2
deoxycorticosterone + NADP+ + H2O
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
progesterone + [reduced NADPH-hemoprotein reductase] + O2
16alpha-hydroxy-progesterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
mutant V359A produces an additional metabolite, 16alpha-hydroxyprogesterone of progesterone, very low activity with the wild-type enzyme
product identification by TLC
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
16alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O
mutants V359A and V359G both produce an additional metabolite, 16alpha-hydroxyprogesterone
product identification by TLC
-
?
progesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-P450 reductase] + H2O
additional information
?
-
17-hydroxy-progesterone + NADH + O2
17-hydroxy-11-deoxy-corticosterone + NAD+ + H2O
-
-
-
-
?
17-hydroxy-progesterone + NADH + O2
17-hydroxy-11-deoxy-corticosterone + NAD+ + H2O
-
isozyme CYP2D
-
-
?
17-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
-
-
-
-
?
17-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
-
-
-
?
17-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
the redox cofactor provides the electrons required for a P450-dependent hydroxylation. Maximal CYP 21 activity is observed in presence of low substrate concentrations of 0.2 mM. Higher substrate concentrations reduce the activity and inhibit the enzyme
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADH + O2
17,21-dihydroxyprogesterone + NAD+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
-
P450c21 catalyzes hydroxylation at C-21, 17alpha-hydroxyprogesterone is a better substrate for P450c21 than progesterone from the catalytic coupling with consumption of NADPH
-
-
?
17alpha-hydroxyprogesterone + NADPH + H+ + O2
11-deoxycortisol + NADP+ + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + NADPH + H+ + O2
17,21-dihydroxyprogesterone + NADP+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADPH + H+ + O2
17,21-dihydroxyprogesterone + NADP+ + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + NADPH + O2
11-deoxycortisol + NADP+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + NADPH + O2
11-deoxycortisol + NADP+ + H2O
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycortisol + [oxidized NADPH-hemoprotein reductase] + H2O
preferred substrate. The 17alpha-hydroxyprogesterone metabolites formed by mutants of V470 and I471 include a second, unidentified product. Both mutants V359A and V359G also metabolize 17alpha-hydroxyprogesterone to 11-deoxycortisol and this second product, and for mutation V359G, the unidentified compound is the major product. The second compound is not androstenedione and is neither the 16alpha- nor 6beta-hydroxylation products (pregn-4-ene-16alpha,17alpha-diol-3,20-dione and pregn-4-ene-6beta,17alpha-diol-3,20-dione, respectively)
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycortisol + [oxidized NADPH-P450 reductase] + H2O
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycortisol + [oxidized NADPH-P450 reductase] + H2O
two 17alpha-hydroxyprogesterone molecules are bound to the enzyme, the distal one being located at the entrance of the substrate access channel and the proximal one bound in the active site
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycortisol + [oxidized NADPH-P450 reductase] + H2O
-
-
-
-
?
17alpha-hydroxyprogesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycortisol + [oxidized NADPH-P450 reductase] + H2O
-
-
-
?
DELTA5-pregnen-3beta-ol-20-one + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
very small yields, presumably via dehydrogenation followed by C-21 hydroxylation
?
DELTA5-pregnen-3beta-ol-20-one + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
no substrate of cytochrome P-450-linked mixed function oxidase system
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
isozyme CYP2D
-
-
?
progesterone + NADH + O2
deoxycorticosterone + NAD+ + H2O
-
-
-
?
progesterone + NADPH + H+ + O2
11-deoxycorticosterone + NADP+ + H2O
-
P450c21 catalyzes hydroxylation at C-21
-
-
?
progesterone + NADPH + H+ + O2
11-deoxycorticosterone + NADP+ + H2O
-
-
-
-
?
progesterone + NADPH + H+ + O2
11-deoxycorticosterone + NADP+ + H2O
-
-
-
?
progesterone + NADPH + H+ + O2
11-deoxycorticosterone + NADP+ + H2O
-
-
-
-
?
progesterone + NADPH + H+ + O2
deoxycorticosterone + NADP+ + H2O
-
-
-
-
?
progesterone + NADPH + H+ + O2
deoxycorticosterone + NADP+ + H2O
-
-
-
?
progesterone + NADPH + O2
deoxycorticosterone + NADP+ + H2O
-
-
-
?
progesterone + NADPH + O2
deoxycorticosterone + NADP+ + H2O
-
-
-
?
progesterone + NADPH + O2
deoxycorticosterone + NADP+ + H2O
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
progesterone + [reduced NADPH-hemoprotein reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-P450 reductase] + H2O
-
-
-
?
progesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-P450 reductase] + H2O
-
-
-
-
?
progesterone + [reduced NADPH-P450 reductase] + O2
11-deoxycorticosterone + [oxidized NADPH-P450 reductase] + H2O
-
-
-
?
additional information
?
-
-
no substrate: 17alpha-hydroxy-progesterone
-
-
?
additional information
?
-
-
enzyme deficiency, i.e. 21-OHD, causes congenital adrenal hyperplasia in pubertal subjects
-
-
?
additional information
?
-
CYP21 performs the regio- and stereo-selective 21-hydroxylation of 17-alpha-hydroxyprogesterone when recombinantly expressed in Schizosaccharomyces pombe
-
-
?
additional information
?
-
-
CYP21 performs the regio- and stereo-selective 21-hydroxylation of 17-alpha-hydroxyprogesterone when recombinantly expressed in Schizosaccharomyces pombe
-
-
?
additional information
?
-
reaction method optimization, overview
-
-
?
additional information
?
-
-
reaction method optimization, overview
-
-
?
additional information
?
-
-
metandienone hydroxylation activities and metabolism in vivo, product analysis, overview
-
-
?
additional information
?
-
17alpha-hydroxyprogesterone is hydroxylated 28times faster than progesterone by the wild-type enzyme. No activity of the wild-type enzyme with pregnenolone, 17alpha-hydroxypregnenolone, and 5alpha-pregnane-3alpha-ol-20-one (allopregnanolone)
-
-
?
additional information
?
-
-
17alpha-hydroxyprogesterone is hydroxylated 28times faster than progesterone by the wild-type enzyme. No activity of the wild-type enzyme with pregnenolone, 17alpha-hydroxypregnenolone, and 5alpha-pregnane-3alpha-ol-20-one (allopregnanolone)
-
-
?
additional information
?
-
-
21-trifluorosteroids mht by a substrates for CYP21A2, substrate specificity analysis of CP21A2 with diverse halogenated steroid substrates, e.g. introducing one or more halogen atom to the 17- and 21-positions of progesterone and pregnenolone, 21,21,21-tribromoprogesterone and 21,21,21-trichloroprogesterone, overview
-
-
?
additional information
?
-
-
human CYP21A2 also has progesterone 16alpha-hydroxylase activity. Product analysis by LC-MS/MS
-
-
?
additional information
?
-
C-H bond breaking is a rate-limiting step over a 10000fold range of catalytic efficiency
-
-
?
additional information
?
-
-
C-H bond breaking is a rate-limiting step over a 10000fold range of catalytic efficiency
-
-
?
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2.3 - 9.2
17-hydroxy-progesterone
0.0038 - 0.031
17-hydroxyprogesterone
0.00044 - 0.022
17alpha-hydroxyprogesterone
0.00021 - 9.2
progesterone
additional information
additional information
-
2.3
17-hydroxy-progesterone
-
37°C, mutant P482S
8.5
17-hydroxy-progesterone
-
37°C, wild-type
9.2
17-hydroxy-progesterone
-
37°C, mutant A15T
0.0038
17-hydroxyprogesterone
-
head kidney microsomes
0.0055
17-hydroxyprogesterone
-
-
0.031
17-hydroxyprogesterone
-
liver microsomes
0.00044
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
0.00044
17alpha-hydroxyprogesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
0.00046
17alpha-hydroxyprogesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.00046
17alpha-hydroxyprogesterone
-
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.00061
17alpha-hydroxyprogesterone
pH 7.4, 37°C, mutant V359G
0.00082
17alpha-hydroxyprogesterone
pH 7.4, 37°C, mutant V359A
0.00135
17alpha-hydroxyprogesterone
-
mutant enzyme D322G, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.00138
17alpha-hydroxyprogesterone
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0014
17alpha-hydroxyprogesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
0.0015
17alpha-hydroxyprogesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0015
17alpha-hydroxyprogesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0015
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
0.0016
17alpha-hydroxyprogesterone
-
wild type enzyme
0.0016
17alpha-hydroxyprogesterone
pH 7.4, 37°C, wild-type enzyme
0.0016
17alpha-hydroxyprogesterone
pH 7.4, 37°C, mutant V470A/I471A
0.0017
17alpha-hydroxyprogesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.0017
17alpha-hydroxyprogesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
0.00181
17alpha-hydroxyprogesterone
-
mutant enzyme A265V, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.0019
17alpha-hydroxyprogesterone
pH 7.4, 37°C, wild-type CYP21
0.002
17alpha-hydroxyprogesterone
-
mutant enzyme P453S
0.0024
17alpha-hydroxyprogesterone
pH 7.4, 37°C, CYP21 mutant T241R/L442A
0.0024
17alpha-hydroxyprogesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
0.0025
17alpha-hydroxyprogesterone
pH 7.4, 37°C, mutant V470A
0.0026
17alpha-hydroxyprogesterone
-
mutant enzyme K121Q
0.0036
17alpha-hydroxyprogesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.0046
17alpha-hydroxyprogesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
0.0049
17alpha-hydroxyprogesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
0.0073
17alpha-hydroxyprogesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.0108
17alpha-hydroxyprogesterone
37°C, pH 7.4, presence of 0.002% Cymal 5
0.013
17alpha-hydroxyprogesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.013
17alpha-hydroxyprogesterone
-
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.022
17alpha-hydroxyprogesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.00021
progesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00021
progesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.00021
progesterone
recombinant enzyme, at pH 7.4 and 37°C
0.00039
progesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
0.00048
progesterone
pH 7.4, 37°C, mutant V359A
0.0005
progesterone
recombinant enzyme, at pH 7.4 and 37°C
0.00072
progesterone
-
mutant enzyme D322G, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.00072
progesterone
-
wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.00079
progesterone
-
mutant enzyme A265V, in 50 mM potassium phosphate buffer (pH 7.4), at 37°C
0.001
progesterone
pH 7.4, 37°C, mutant V470A
0.0011
progesterone
pH 7.4, 37°C, wild-type enzyme
0.0011
progesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.0011
progesterone
-
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.0012
progesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.0012
progesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
0.0015
progesterone
-
wild type enzyme
0.0015
progesterone
-
mutant enzyme P453S
0.0015
progesterone
pH 7.4, 37°C, mutant V470A/I471A
0.0018
progesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
0.0024
progesterone
-
mutant enzyme K121Q
0.0027
progesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.0032
progesterone
pH 7.4, 37°C, mutant V359G
0.0038
progesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
0.0047
progesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
0.0055
progesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.0055
progesterone
-
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.0096
progesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.0129
progesterone
37°C, pH 7.4, presence of 0.002% Cymal 5
0.022
progesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.11
progesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
3
progesterone
-
37°C, mutant P482S
6.4
progesterone
-
37°C, wild-type
9.2
progesterone
-
37°C, mutant A15T
additional information
additional information
reaction kinetic, overview
-
additional information
additional information
-
reaction kinetic, overview
-
additional information
additional information
-
calculation of intramolecular and intermolecular kinetic isotope effects for wild-type and mutant enzymes with substrates 21-[2H]-progesterone, 21,21,21-[2H3]-progesterone, and 21,21,21-[2H3]-17-hydroxyprogesterone, overview
-
additional information
additional information
Pre-steady-state and steady-state binding kinetics with 17alpha-hydroxyprogesterone, stopped-flow spectroscopic measurements, overview
-
additional information
additional information
-
Pre-steady-state and steady-state binding kinetics with 17alpha-hydroxyprogesterone, stopped-flow spectroscopic measurements, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.322
17a-hydroxyprogesterone
-
-
0.00003 - 4
17alpha-hydroxyprogesterone
0.0001 - 2.8
progesterone
0.00003
17alpha-hydroxyprogesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.000033
17alpha-hydroxyprogesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
0.00005
17alpha-hydroxyprogesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.00022
17alpha-hydroxyprogesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.0005
17alpha-hydroxyprogesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.003
17alpha-hydroxyprogesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
0.028
17alpha-hydroxyprogesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.03
17alpha-hydroxyprogesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
0.032
17alpha-hydroxyprogesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.032
17alpha-hydroxyprogesterone
-
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.033
17alpha-hydroxyprogesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
0.045
17alpha-hydroxyprogesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.063
17alpha-hydroxyprogesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
0.22
17alpha-hydroxyprogesterone
pH 7.4, 37°C, CYP21 wild-type and mutant T241R/L442A
0.67
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
1.4
17alpha-hydroxyprogesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
4
17alpha-hydroxyprogesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
4
17alpha-hydroxyprogesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
4
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
0.0001
progesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.0001
progesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
0.00013
progesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.00027
progesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.00083
progesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.0015
progesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
0.0077
progesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.008
progesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
0.02
progesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
0.06
progesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.062
progesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
0.078
progesterone
recombinant enzyme, at pH 7.4 and 37°C
0.2
progesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
0.38
progesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
1.033
progesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
2.8
progesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
2.8
progesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2.8
progesterone
recombinant enzyme, at pH 7.4 and 37°C
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0.016 - 2667
17alpha-hydroxyprogesterone
0.012 - 13333
progesterone
0.016
17alpha-hydroxyprogesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
0.02
17alpha-hydroxyprogesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.02
17alpha-hydroxyprogesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.03
17alpha-hydroxyprogesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.12
17alpha-hydroxyprogesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.62
17alpha-hydroxyprogesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
2.3
17alpha-hydroxyprogesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
2.3
17alpha-hydroxyprogesterone
-
mutant G65E, pH not specified in the publication, temperature not specified in the publication
13.3
17alpha-hydroxyprogesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
61.7
17alpha-hydroxyprogesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
66.7
17alpha-hydroxyprogesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
100
17alpha-hydroxyprogesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
100
17alpha-hydroxyprogesterone
-
mutant T296N, pH not specified in the publication, temperature not specified in the publication
817
17alpha-hydroxyprogesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
1567
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
2667
17alpha-hydroxyprogesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
2667
17alpha-hydroxyprogesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2667
17alpha-hydroxyprogesterone
recombinant enzyme, at pH 7.4 and 37°C
0.012
progesterone
mutant R357W, pH not specified in the publication, temperature not specified in the publication
0.012
progesterone
mutant W303R, pH not specified in the publication, temperature not specified in the publication
0.013
progesterone
mutant P31Q, pH not specified in the publication, temperature not specified in the publication
0.03
progesterone
mutant L108R, pH not specified in the publication, temperature not specified in the publication
0.07
progesterone
mutant G292C, pH not specified in the publication, temperature not specified in the publication
0.82
progesterone
mutant I172N, pH not specified in the publication, temperature not specified in the publication
6.7
progesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
7
progesterone
mutant T296N, pH not specified in the publication, temperature not specified in the publication
11.2
progesterone
mutant G65E, pH not specified in the publication, temperature not specified in the publication
11.2
progesterone
-
mutant G65E, pH not specified in the publication, temperature not specified in the publication
43.3
progesterone
mutant G292S, pH not specified in the publication, temperature not specified in the publication
50
progesterone
mutant R409C, pH not specified in the publication, temperature not specified in the publication
267
progesterone
mutant V282L, pH not specified in the publication, temperature not specified in the publication
317
progesterone
mutant P31L, pH not specified in the publication, temperature not specified in the publication
1517
progesterone
recombinant enzyme, at pH 7.4 and 37°C
13330
progesterone
recombinant enzyme, at pH 7.4 and 37°C
13333
progesterone
wild-type, pH not specified in the publication, temperature not specified in the publication
13333
progesterone
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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T241R
site-directed mutagenesis, the mutant shows improved solubility properties compared to the wild-type enzyme
T241R/L442A
site-directed mutagenesis, the mutant shows greatly improved solubility properties compared to the wild-type enzyme
A15T
-
natural mutation found in patients with classical congenital adrenal hyperplasia, no significant difference in activity compared to wild-type
A265C
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
A391T
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region
A434V
naturally occuring mutation, the mutation causes steric clashes with the heme rendering the enzyme almost inactive
C169R
naturally occuring mutation, the mutation alters the region's hydrophobicity, conserved residue C169 makes hydrophobic interactions with the loop between E-F helices and F-helix
D407N
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
E320K
naturally occuring mutation, the mutation of E320, which is a highly conserved residue on a negatively charged Glu-Glu-Leu-Asp (EELD) motif, alters the charge on the motif
E351K
-
rare missense mutation located in the ERR triad and found in a patient with virilizing congenital hyperplasia. Residual activity is about 1% of wild-type for both 17-hydroxyprogesterone and progesterone
E431K
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
F404S
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia
G178A
naturally occuring mutation, the mutation causes reduced structural flexibility of the sharp fold between the E- and F-helices
G291C
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia
G291R
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia
G291S
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia
G292C
0.32% of wild-type efficiency with substrate progesterone
G292D
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia
G292S
0.0005% of wild-type efficiency with substrate progesterone
G424S
naturally occuring mutation, the mutation imparts rigidity to the loop between K'- and L-helix
G56R
naturally occuring mutation, P57 and G56 form the hinge between the membrane interacting N-terminus and rest of the protein. The substitution of G56 with a polar and rigid Arg residue disrupts the hinge affecting the interactions of CYP21A2 with the membrane
G90V
naturally occuring mutation, mutation of G90 to valine affects the ability of R91 to hydrogen bond with heme, causing salt-wasting congenital adrenal hyperplasia
H119R
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
H365W
-
the naturally occuring CYP21A2 mutant exhibits minimal 21-hydroxylase activity to convert 17-hydroxyprogesterone to 11-deoxycortisol or progesterone to 11-deoxycorticosterone compared to the wild-type
H62L
naturally occuring mutation, the mutation may disrupt hydrogen bonding to reduce, but not eliminate, enzyme activity
I171N
-
mutation identified in Italian patient with congenital adrenal hyperplasia, less than 1% of wild-type enzyme activity
I194N
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
I230T
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
I236N/V237E/M239K
-
naturally occuring mutant, no enzymic activity, dominant negative effect over wild-type with 35% decrease in activity
I471A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
I471G
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
I77T
naturally occuring mutation, the mutation disrupts the hydrophobic environment
K121Q
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
K122Q
-
missense mutation causing nonclassical 21-hydroxylase deficiency, shows reduced activity of 14% for the conversion of 17alpha-hydroxyprogesterone and 19% for the conversion of progesterone compared to wild type
L107R
naturally occuring mutation, the mutation abolishes heme binding and causes salt-wasting congenital adrenal hyperplasia
L107X
site-directed mutagenesis, inactive mutant
L108R
0.0003% of wild-type efficiency with substrate progesterone
L109X
site-directed mutagenesis, inactive mutant
L142P
naturally occuring mutation, the mutation of the D-helix causes helical disruption and destabilization of secondary structures
L166P
naturally occuring mutation, the mutation of the E-helix causes helical disruption and destabilization of secondary structures
L167P
naturally occuring mutation, the mutation of the E-helix causes helical disruption and destabilization of secondary structures
L236N/V237E/M239K
the mutation is associated with congenital adrenal hyperplasia
L261P
naturally occuring mutation, the mutation of the H-helix causes helical disruption and destabilization of secondary structures
L300F
naturally occuring mutation, the mutation causes localized destabilization of secondary structure
L307M
naturally occuring mutation, the mutation disrupts the optimal packing of side chains but does not alter the hydrophobic environment
L307V
naturally occuring mutation, the mutation disrupts the optimal packing of side chains but does not alter the hydrophobic environment
L308F
naturally occuring mutation, the mutation causes localized destabilization of secondary structure
L353R
naturally occuring mutation, the mutation abolishes heme binding and causes salt-wasting congenital adrenal hyperplasia
L363W
naturally occuring mutation, the mutation causes steric clashes with the heme rendering the enzyme almost inactive
N387K
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
P30E
naturally occuring mutation causing disruption of the interaction between the carbon of P30 in the N-terminal loop and the side chain of Y376 within the beta5-beta6 hairpin loop resuting in the salt-wasting disease
P31L
2.4% of wild-type efficiency with substrate progesterone
P31Q
0.0001% of wild-type efficiency with substrate progesterone
P432L
naturally occuring mutation, the mutation makes the structure more flexible and prevents cysteine from being presented to heme
P459H
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region
P463L
naturally occuring mutation, the mutation interferes with the conformation of the beta8-beta9 loop with the subsequent closure of substrate entrance channel
P482S
-
natural mutation found in patients with nonclassical congenital adrenal hyperplasia, precocious pubarche, menstrual irregularities or hypertrichosis, about 70% of activity compared to wild-type
Q318X
the mutation is associated with congenital adrenal hyperplasia
Q481P
naturally occuring mutation, the mutation destabilizes the structure rendering the protein inactive
R124H
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
R132C
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
R149C
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
R233G
naturally occuring mutation, the mutation may prevent R233 from binding to the 3-keto oxygen of the proximal 17OHP in the proper orientation, it does not influence protein activity significantly, resulting in minimal phenotype
R233K
naturally occuring mutation, the mutation may prevent R233 from binding to the 3-keto oxygen of the proximal 17OHP in the proper orientation, it does not influence protein activity significantly, resulting in minimal phenotype
R339H
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
R341W
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
R356P
naturally occuring mutation, the mutation disrupts the interaction of R356 with Q389 rendering the enzyme inactive and causing salt-wasting congenital adrenal hyperplasia
R357W
0.01% of wild-type efficiency with substrate progesterone
R369Q
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
R408C/L
naturally occuring mutation, the mutation destabilizes structural elements because of the extensive loss of hydrogen bonds
R408H
naturally occuring mutation, the mutation prevents normal hydrogen bonding with E351 and R354
R409C
0.4% of wild-type efficiency with substrate progesterone
R426C
naturally occuring mutation, the mutation disrupts the interaction of residues R91 and R426 rendering the protein nonfunctional and causing salt-wasting congenital adrenal hyperplasia
R426H
-
mutation identified in Italian patient with congenital adrenal hyperplasia, less than 1% of wild-type enzyme activity
R435C
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
R479L
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
R483P
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
S301Y
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
T168N
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
T295X
naturally occuring mutation, the mutation abolishes substrate binding and causes salt-wasting congenital adrenal hyperplasia
T450P
naturally occuring mutation, the mutation reduces flexibility of beta8-sheet, which helps stabilize the very long C-terminal loop
V139E
naturally occuring mutation, mutation to glutamate disrupts the interaction with residues V440 and L436 on the L-helix causing instability of the enzyme, charge repulsions between the side chain of mutated V139E and E437 of the E-helix render the protein unstable and inactive causing salt-wasting congenital adrenal hyperplasia
V249A
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
V281G
naturally occuring mutation, the mutation causes a loss of the hydrophobic pocket
V282L
2% of wild-type efficiency with substrate progesterone
V304M
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
V359G
site-directed mutagenesis, the mutant shows 10% reduced activity compared to the wild-type enzyme
V470A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
V470A/I471A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
V470G
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
W302R
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia
W303R
0.0001% of wild-type efficiency with substrate progesterone
Y47C
naturally occuring mutation, the mutation disables hydrogen bonding with H38, the interaction is compensated by a weak His-Cys interaction
Y47L
naturally occuring mutation, the mutation disrupts hydrogen bonds and causes salt-wasting congenital adrenal hyperplasia
Y59N
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region resulting in loss of function
A265V
-
the mutant enzyme activity is similar to wild type
A265V
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues
D322G
-
the mutation impacts significantly on enzyme function and exerts activity compatible with non-classical congenital adrenal hyperplasia, has about 27% activity for the conversion of progesterone to 11-deoxycorticosterone and 18% activity for the conversion of 17alpha-hydroxyprogesterone to 11-deoxycortisol compared to wild type activity
D322G
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
G65E
0.08% of wild-type activity with substrate progesterone
G65E
0.082% of wild-type efficiency with substrate progesterone
H365Y
naturally occuring mutation, the mutations causes the salt-wasting disease
H365Y
-
the naturally occuring CYP21A2 mutant exhibits minimal 21-hydroxylase activity to convert 17-hydroxyprogesterone to 11-deoxycortisol or progesterone to 11-deoxycorticosterone compared to the wild-type
H365Y/R356W
-
a naturally occuring 21-hydroxylase mutation in the CYP21A2 gene, that is involved in congenital adrenal hyperplasia, an autosomal recessive disorder, phenotype, overview. The H365Y enzyme is produced in more variable amounts than wild type
H365Y/R356W
-
heterozygote H365Y/R356W individuum for two CYP21A2 gene mutations each inherited from a different parent
I172N
-
naturally occuring mutant, 0-2% of wild-type activity, dominant negative effect over wild-type with 11% decrease in activity
I172N
the mutation is associated with congenital adrenal hyperplasia
I172N
naturally occuring mutation, the mutation causes a loss of the hydrophobic pocket, I172 forms a hydrophobic pocket with M186 and M187 residues of F-helix
I172N
0.006% of wild-type efficiency with substrate progesterone
L446P
-
mutation identified in Italian patient with congenital adrenal hyperplasia, less than 1% of wild-type enzyme activity
L446P
naturally occuring mutation, the mutation of the L-helix causes helical disruption and destabilization of secondary structures
P30L
missense mutation associated with congenital adrenal hyperplasia
P30L
the mutation is associated with congenital adrenal hyperplasia
P453S
-
the mutant shows a reduced activity of 36% of wild type for the conversion of 17alpha-hydroxyprogesterone and 44% for the conversion of progesterone
P453S
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region
R341P
-
mutation identified in Italian patient with congenital adrenal hyperplasia, less than 1% of wild-type enzyme activity
R341P
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase
R356W
-
naturally occuring mutant, no enzymic activity, no dominant negative effect on wild-type
R356W
the mutation is associated with congenital adrenal hyperplasia
R483Q
-
the mutant enzyme activities in the conversion of progesterone to deoxycorticosterone and 17alpha-hydroxyprogesterone to 11-deoxycortisol are measured as 2.0 and 1.89% of the wild type, respectively
R483Q
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure
T296N
0.05% of wild-type activity with substrate progesterone
T296N
0.05% of wild-type efficiency with substrate progesterone
V281L
-
naturally occuring mutant, 50% of wild-type activity, dominant negative effect over wild-type with 30% decrease in activity
V281L
the mutation is associated with congenital adrenal hyperplasia
V359A
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
V359A
-
site-directed mutagenesis, the mutant shows altered product formation compared to the wild-type enzyme
V359A
mutant displays significant 16alpha-hydroxylase activity. Substrate 16,17-dehydroprogesterone is converted to the 21-hydroxylated product and slightly more epoxide than wild-type
W302S
-
the mutation impacts significantly on enzyme function and exerts activity compatible with simple virilizing congenital adrenal hyperplasia, has residual enzyme activity of about 3% compared to wild type activity for both, the conversion of progesterone to 11-deoxycorticosterone and the conversion of 17alpha-hydroxyprogesterone to 11-deoxycortisol
W302S
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia
additional information
replacement of N-terminal membrane anchor and basic regions by the basic regions of CYP2C3 for efficient expression and purification. N-terminal membrane anchor and sequence of the basic region do not significantly affect either substrate-specificity or 21-hydroxylase activites
additional information
-
replacement of N-terminal membrane anchor and basic regions by the basic regions of CYP2C3 for efficient expression and purification. N-terminal membrane anchor and sequence of the basic region do not significantly affect either substrate-specificity or 21-hydroxylase activites
additional information
-
enzyme deficiency, i.e. 21-OHD, causes congenital adrenal hyperplasia, growth phenotypes of pubertal humans with salt wasting, simple virilizing, or non-classical 21-OHD, respectively, overview
additional information
an insertion (duplication) of 9-bp in exon 2 results in addition of three valine residues at codon 71 of the P450c21 protein lowering the structural stability of P450c21 thereby leading to the probable loss of its function
additional information
-
an insertion (duplication) of 9-bp in exon 2 results in addition of three valine residues at codon 71 of the P450c21 protein lowering the structural stability of P450c21 thereby leading to the probable loss of its function
additional information
deletions/conversions involving the promoter region of the CYP21A2 gene (IVS2-12C/A>G, F306-L307insT) are associated with congenital adrenal hyperplasia
additional information
-
deletions/conversions involving the promoter region of the CYP21A2 gene (IVS2-12C/A>G, F306-L307insT) are associated with congenital adrenal hyperplasia
additional information
two CYP21A2 intron 2 haplotype clusters, named c5 and c8, are related to the circulating steroid hormone levels in subjects with non-functioning adrenal incidentaloma
additional information
-
two CYP21A2 intron 2 haplotype clusters, named c5 and c8, are related to the circulating steroid hormone levels in subjects with non-functioning adrenal incidentaloma
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Ryan, K.J.; Engel, L.L.
Hydroxylation of steroids at carbon 21
J. Biol. Chem.
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103-114
1957
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Hiwatashi, A.; Ichikawa, Y.
Purification and reconstitution of the steroid 21-hydroxylase system (cytochrome P-450-linked mixed function oxidase system) of bovine adrenocortical microsomes
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-
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Studies on the steroid hydroxylation system in adrenal cortex microsomes
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complete nucleotide sequence of two steroid 21-hydroxylase genes tandemly arranged in human chromosomes: a pseudogene and a genuine gene
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Steroid 21-hydroxylase expression in cultured rat astrocytes
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Cytochrome P450 2D catalyze steroid 21-hydroxylation in the brain
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2003
Anguilla japonica
brenda
Felix-Lopez, X.; Riba, L.; Ordonez-Sanchez, M.L.; Ramirez-Jimenez, S.; Ventura-Gallegos, J.L.; Zentella-Dehesa, A.; Tusie-Luna, M.T.
Steroid 21-hydroxylase (P450c21) naturally occurring mutants I172N, V281L and I236N/V237E/M239K exert a dominant negative effect on enzymatic activity when co-expressed with the wild-type protein
J. Pediatr. Endocrinol. Metab.
16
1017-1024
2003
Homo sapiens
brenda
Martineau, I.; Belanger, A.; Tchernof, A.; Tremblay, Y.
Molecular cloning and expression of guinea pig cytochrome P450c21 cDNA (steroid 21-hydroxylase) isolated from the adrenals
J. Steroid Biochem. Mol. Biol.
86
123-132
2003
Cavia porcellus
brenda
Arase, M.; Waterman, M.R.; Kagawa, N.
Purification and characterization of bovine steroid 21-hydroxylase (P450c21) efficiently expressed in Escherichia coli
Biochem. Biophys. Res. Commun.
344
400-405
2006
Bos taurus (P00191), Bos taurus
brenda
Miguel, R.N.; Chen, S.; Nikfarjam, L.; Kominami, S.; Carpenter, B.; Dal Pra, C.; Betterle, C.; Zanchetta, R.; Nakamatsu, T.; Powell, M.; Hewer, R.; Blundell, T.L.; Smith, B.R.; Furmaniak, J.
Analysis of the interaction between human steroid 21-hydroxylase and various monoclonal antibodies using comparative structural modelling
Eur. J. Endocrinol.
153
949-961
2005
Homo sapiens
brenda
Dolzan, V.; Solyom, J.; Fekete, G.; Kovacs, J.; Rakosnikova, V.; Votava, F.; Lebl, J.; Pribilincova, Z.; Baumgartner-Parzer, S.M.; Riedl, S.; Waldhauser, F.; Frisch, H.; Stopar-Obreza, M.; Krzisnik, C.; Battelino, T.
Mutational spectrum of steroid 21-hydroxylase and the genotype-phenotype association in Middle European patients with congenital adrenal hyperplasia
Eur. J. Endocrinol.
153
99-106
2005
Homo sapiens
brenda
Supornsilchai, V.; Svechnikov, K.; Seidlova-Wuttke, D.; Wuttke, W.; Soeder, O.
Phytoestrogen resveratrol suppresses steroidogenesis by rat adrenocortical cells by inhibiting cytochrome P450 c21-hydroxylase
Horm. Res.
64
280-286
2005
Rattus norvegicus
brenda
Krone, N.; Riepe, F.G.; Groetzinger, J.; Partsch, C.; Braemswig, J.; Sippell, W.G.
The residue E351 is essential for the activity of human 21-hydroxylase: evidence from a naturally occurring novel point mutation compared with artificial mutants generated by single amino acid substitutions
J. Mol. Med.
83
561-568
2005
Homo sapiens
brenda
Barbaro, M.; Baldazzi, L.; Balsamo, A.; Lajic, S.; Robins, T.; Barp, L.; Pirazzoli, P.; Cacciari, E.; Cicognani, A.; Wedell, A.
Functional studies of two novel and two rare mutations in the 21-hydroxylase gene
J. Mol. Med.
84
521-528
2006
Homo sapiens
brenda
Trinh, L.; Nimkarn, S.; New, M.I.; Lin-Su, K.
Growth and pubertal characteristics in patients with congenital adrenal hyperplasia due to 21-hydroxylase deficiency
J. Pediatr. Endocrinol. Metab.
20
883-891
2007
Homo sapiens
brenda
Soardi, F.C.; Lemos-Marini, S.H.; Coeli, F.B.; Maturana, V.G.; Silva, M.D.; Bernardi, R.D.; Justo, G.Z.; de-Mello, M.P.
Heterozygosis for CYP21A2 mutation considered as 21-hydroxylase deficiency in neonatal screening
Arq. Bras. Endocrinol. Metabol.
52
1388-1392
2008
Homo sapiens
brenda
Concolino, P.; Mello, E.; Minucci, A.; Giardina, E.; Zuppi, C.; Toscano, V.; Capoluongo, E.
A new CYP21A1P/CYP21A2 chimeric gene identified in an Italian woman suffering from classical congenital adrenal hyperplasia form
BMC Med. Genet.
10
72
2009
Homo sapiens (P08686), Homo sapiens
brenda
Ono, M.; Kashimada, K.; Miyai, K.; Onishi, T.; Takagi, M.; Honma, S.; Mizutani, S.
In vitro enzyme assay of CYP21A2 mutation (R483Q) by a novel method using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)
Clin. Pediatr. Endocrinol.
17
49-56
2008
Homo sapiens
brenda
Marques, C.J.; Pignatelli, D.; Carvalho, B.; Barcelo, J.; Almeida, A.C.; Fernandes, S.; Witchel, S.F.; Sousa, M.; Oliveira, M.J.; Freitas, P.; Fontoura, M.; Carvalho, D.; Barros, A.; Carvalho, F.
Mutational characterization of steroid 21-hydroxylase gene in Portuguese patients with congenital adrenal hyperplasia
Exp. Clin. Endocrinol. Diabetes
118
505-512
2010
Homo sapiens (P08686), Homo sapiens
brenda
Bleicken, C.; Loidi, L.; Dhir, V.; Parajes, S.; Quinteiro, C.; Dominguez, F.; Groetzinger, J.; Sippell, W.G.; Riepe, F.G.; Arlt, W.; Krone, N.
Functional characterization of three CYP21A2 sequence variants (p.A265V, p.W302S, p.D322G) employing a yeast co-expression system
Hum. Mutat.
30
E443-E450
2009
Homo sapiens
brenda
Bratland, E.; Bredholt, G.; Mellgren, G.; Knappskog, P.M.; Mozes, E.; Husebye, E.S.
The purification and application of biologically active recombinant steroid cytochrome P450 21-hydroxylase: the major autoantigen in autoimmune Addisons disease
J. Autoimmun.
33
58-67
2009
Homo sapiens (P08686), Homo sapiens
brenda
Tosha, T.; Kagawa, N.; Arase, M.; Waterman, M.; Kitagawa, T.
Interaction between substrate and oxygen ligand responsible for effective O-O bond cleavage in bovine cytochrome P450 steroid 21-hydroxylase proved by Raman spectroscopy
J. Biol. Chem.
283
3708-3717
2008
Bos taurus
brenda
Dubey, S.; Idicula-Thomas, S.; Anwaruddin, M.; Saravanan, C.; Varma, R.R.; Maitra, A.
A novel 9-bp insertion detected in steroid 21-hydroxylase gene (CYP21A2): prediction of its structural and functional implications by computational methods
J. Biomed. Sci.
16
3-3
2009
Homo sapiens (P08686), Homo sapiens
brenda
Riepe, F.G.; Hiort, O.; Groetzinger, J.; Sippell, W.G.; Krone, N.; Holterhus, P.M.
Functional and structural consequences of a novel point mutation in the CYP21A2 gene causing congenital adrenal hyperplasia: potential relevance of helix C for P450 oxidoreductase-21-hydroxylase interaction
J. Clin. Endocrinol. Metab.
93
2891-2895
2008
Homo sapiens
brenda
Bratland, E.; Skinningsrud, B.; Undlien, D.E.; Mozes, E.; Husebye, E.S.
T cell responses to steroid cytochrome P450 21-hydroxylase in patients with autoimmune primary adrenal insufficiency
J. Clin. Endocrinol. Metab.
94
5117-5124
2009
Homo sapiens
brenda
Rottembourg, D.; Deal, C.; Lambert, M.; Mallone, R.; Carel, J.C.; Lacroix, A.; Caillat-Zucman, S.; le Deist, F.
21-Hydroxylase epitopes are targeted by CD8 T cells in autoimmune Addisons disease
J. Autoimmun.
35
309-315
2010
Homo sapiens (P08686), Homo sapiens
brenda
Zehentgruber, D.; Dragan, C.A.; Bureik, M.; Luetz, S.
Challenges of steroid biotransformation with human cytochrome P450 monooxygenase CYP21 using resting cells of recombinant Schizosaccharomyces pombe
J. Biotechnol.
146
179-185
2010
Homo sapiens (P08686), Homo sapiens
brenda
Gaffney, D.; Howie, A.; Bakkush, A.; Hoffmann, T.; Mason, J.; Wallace, A.; Donaldson, M.
Functional characterisation of the H365Y mutation of the 21-hydroxylase gene in congenital adrenal hyperplasia
J. Steroid Biochem. Mol. Biol.
123
109-114
2011
Homo sapiens
brenda
Sushko, T.A.; Gilep, A.A.; Usanov, S.A.
Mechanism of intermolecular interactions of microsomal cytochrome P450s CYP17 and CYP21 involved in steroid hormone biosynthesis
Biochemistry (Moscow)
77
585-592
2012
Homo sapiens
brenda
Mizrachi, D.; Wang, Z.; Sharma, K.K.; Gupta, M.K.; Xu, K.; Dwyer, C.R.; Auchus, R.J.
Why human cytochrome P450c21 is a progesterone 21-hydroxylase
Biochemistry
50
3968-3974
2011
Homo sapiens (P08686), Homo sapiens
brenda
Yoshimoto, F.K.; Zhou, Y.; Peng, H.M.; Stidd, D.; Yoshimoto, J.A.; Sharma, K.K.; Matthew, S.; Auchus, R.J.
Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates
Biochemistry
51
7064-7077
2012
Homo sapiens
brenda
Zhao, B.; Lei, L.; Kagawa, N.; Sundaramoorthy, M.; Banerjee, S.; Nagy, L.D.; Guengerich, F.P.; Waterman, M.R.
Three-dimensional structure of steroid 21-hydroxylase (cytochrome P450 21A2) with two substrates reveals locations of disease-associated variants
J. Biol. Chem.
287
10613-10622
2012
Bos taurus (P00191), Bos taurus, Homo sapiens (P08686)
brenda
Yoshimoto, F.K.; Desilets, M.C.; Auchus, R.J.
Synthesis of halogenated pregnanes, mechanistic probes of steroid hydroxylases CYP17A1 and CYP21A2
J. Steroid Biochem. Mol. Biol.
128
38-50
2012
Homo sapiens
brenda
Haider, S.; Islam, B.; DAtri, V.; Sgobba, M.; Poojari, C.; Sun, L.; Yuen, T.; Zaidi, M.; New, M.I.
Structure-phenotype correlations of human CYP21A2 mutations in congenital adrenal hyperplasia
Proc. Natl. Acad. Sci. USA
110
2605-2610
2013
Homo sapiens (P08686), Homo sapiens
brenda
Parr, M.K.; Zoellner, A.; Fusshoeller, G.; Opfermann, G.; Schloerer, N.; Zorio, M.; Bureik, M.; Schaenzer, W.
Unexpected contribution of cytochrome P450 enzymes CYP11B2 and CYP21, as well as CYP3A4 in xenobiotic androgen elimination - insights from metandienone metabolism
Toxicol. Lett.
213
381-391
2012
Homo sapiens
brenda
Pallan, P.S.; Wang, C.; Lei, L.; Yoshimoto, F.K.; Auchus, R.J.; Waterman, M.R.; Guengerich, F.P.; Egli, M.
Human cytochrome P450 21A2, the major steroid 21-hydroxylase: structure of the enzyme-progesterone substrate complex and rate-limiting C-H bond cleavage
J. Biol. Chem.
290
13128-13143
2015
Bos taurus (P00191), Bos taurus, Homo sapiens (P08686), Homo sapiens
brenda
Doleschall, M.; Szabo, J.A.; Pazmandi, J.; Szilagyi, A.; Koncz, K.; Farkas, H.; Toth, M.; Igaz, P.; Glaz, E.; Prohaszka, Z.; Korbonits, M.; Racz, K.; Fuest, G.; Patocs, A.
Common genetic variants of the human steroid 21-hydroxylase gene (CYP21A2) are related to differences in circulating hormone levels
PLoS ONE
9
e107244
2014
Homo sapiens (P08686), Homo sapiens
brenda
Yoshimoto, F.K.; Peng, H.M.; Zhang, H.; Anderson, S.M.; Auchus, R.J.
Epoxidation activities of human cytochromes P450c17 and P450c21
Biochemistry
53
7531-7540
2014
Homo sapiens (P08686), Homo sapiens
brenda
Wang, C.; Pallan, P.S.; Zhang, W.; Lei, L.; Yoshimoto, F.K.; Waterman, M.R.; Egli, M.; Guengerich, F.P.
Functional analysis of human cytochrome P450 21A2 variants involved in congenital adrenal hyperplasia
J. Biol. Chem.
292
10767-10778
2017
Homo sapiens (P08686), Homo sapiens
brenda
Pallan, P.S.; Lei, L.; Wang, C.; Waterman, M.R.; Guengerich, F.P.; Egli, M.
Research Resource Correlating human cytochrome P450 21A2 crystal structure and phenotypes of mutations in congenital adrenal hyperplasia
Mol. Endocrinol.
29
1375-1384
2015
Homo sapiens (P08686), Homo sapiens
brenda