1.1.1.149: 20alpha-hydroxysteroid dehydrogenase
This is an abbreviated version!
For detailed information about 20alpha-hydroxysteroid dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.149
-
1.1.1.149
-
progesterone
-
androgen
-
prostate
-
reductases
-
testosterone
-
prostaglandin
-
akr1cs
-
steroidogenic
-
luteal
-
castration-resistant
-
srd5a1
-
androstenedione
-
5alpha-reductase
-
cyp17a1
-
dihydrotestosterone
-
progestin
-
akr1b10
-
17beta-hydroxysteroid
-
3alpha-hsds
-
abiraterone
-
neurosteroids
-
luteolysis
-
hsd3b1
-
5alpha-dihydrotestosterone
-
17beta-hsds
-
enzalutamide
-
flufenamic
-
17beta
-
ketosteroid
-
allopregnanolone
-
3beta-hsd
-
17alpha
-
17alpha-hydroxyprogesterone
-
hydrogenans
-
pgf2alpha
-
hsd17b3
-
pre-receptor
-
intracrine
-
3-ketosteroids
-
dihydrodiol
-
scarb1
-
analysis
-
biotechnology
-
food industry
-
medicine
-
environmental protection
- 1.1.1.149
- progesterone
- androgen
- prostate
- reductases
- testosterone
- prostaglandin
- akr1cs
-
steroidogenic
- luteal
-
castration-resistant
- srd5a1
- androstenedione
-
5alpha-reductase
- cyp17a1
- dihydrotestosterone
- progestin
- akr1b10
-
17beta-hydroxysteroid
- 3alpha-hsds
- abiraterone
-
neurosteroids
-
luteolysis
- hsd3b1
- 5alpha-dihydrotestosterone
- 17beta-hsds
-
enzalutamide
-
flufenamic
-
17beta
- ketosteroid
- allopregnanolone
- 3beta-hsd
-
17alpha
- 17alpha-hydroxyprogesterone
-
hydrogenans
-
pgf2alpha
- hsd17b3
-
pre-receptor
-
intracrine
- 3-ketosteroids
- dihydrodiol
-
scarb1
- analysis
- biotechnology
- food industry
- medicine
- environmental protection
Reaction
Synonyms
20-alpha-HSD, 20-alpha-hydroxysteroid dehydrogenase, 20alpha-HSD, 20alpha-HSDH, 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxysteroid dehydrogenase, 20alpha-hydroxysteroid oxidoreductase, 20alpha-OH-SDH, 20beta-HSDH, 20beta-hydroxysteroid dehydrogenase, 3alpha-HSOR, 3alpha-hydroxysteroid oxidoreductase, AKR1C1, AKR1C14, AKR1C23, AKR1C3, AKR1C5, AKR1C9, aldo-keto reductase family 1 member C1, HSD1, More
ECTree
1.1.1.149 20alpha-hydroxysteroid dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.1.149 - 20alpha-hydroxysteroid dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S183A
the kcat/Km-value for cortisol is 56% compared to wild-type enzyme
S183A
-
the kcat/Km-value for cortisol is 56% compared to wild-type enzyme
-
F311A
-
mutation results in increased Ki values for 3-chloro-5-phenylsalicylic acid and 3,5-dichlorosalicylic acid compared to the wild-type enzyme
F311L
-
mutation results in equal Ki value for 3-chloro-5-phenylsalicylic acid and increased Ki value for 3,5-dichlorosalicylic acid compared to the wild-type enzyme
H222S
L306
the mutation in AKR1C1 results in a 46fold reduction in the potency of the inhibitor 3,5-dicholorosalicylic acid
L306A
-
mutation results in 81fold increase Ki values for 3-chloro-5-phenylsalicylic acid compared to the wild-type enzyme
L308A
L308V
L54V
additional information
H222S
the mutation in AKR1C1 results in a 10fold reduction in the potency of the inhibitor 3,5-dicholorosalicylic acid
L308A
the mutation in AKR1C1 results in a 470fold reduction in the potency of the inhibitor 3,5-dicholorosalicylic acid
L308A
mutation renders the enzyme inactive towards the two substrates 5alpha-pregnane-3alpha,20alpha-diol and 5beta-pregnan-3alpha-ol-20-one
L308A
mutation results in 473-fold and 27fold reductions in the inhibitory potencies of 3,5-dichlorosalicylic acid and 3-bromo-5-phenylsalicylic acid, respectively
L308A
-
mutation results in increased Ki values for 3-chloro-5-phenylsalicylic acid and 3,5-dichlorosalicylic acid compared to the wild-type enzyme
L308V
crystallization data. Mutation results in 13-fold and 3fold reductions in the inhibitory potencies of 3,5-dichlorosalicylic acid and 3-bromo-5-phenylsalicylic acid, respectively
L308V
mutation improves the catalytic efficiency towards the two substrates 5alpha-pregnane-3alpha,20alpha-diol and 5beta-pregnan-3alpha-ol-20-one
L308V
-
mutation results in increased Ki values for 3-chloro-5-phenylsalicylic acid and 3,5-dichlorosalicylic acid compared to the wild-type enzyme
L54V
the mutation in AKR1C1 results in a 14fold reduction in the potency of the inhibitor 3,5-dicholorosalicylic acid
L54V
-
mutation results in increased Ki values for 3-chloro-5-phenylsalicylic acid and 3,5-dichlorosalicylic acid compared to the wild-type enzyme
additional information
important role of the 38-residue extended N-terminus in protein stability as deletion of the first 21 residues effectively abolishes enzyme activity with a 1.45 °C shift in Tm
additional information
-
important role of the 38-residue extended N-terminus in protein stability as deletion of the first 21 residues effectively abolishes enzyme activity with a 1.45 °C shift in Tm
-
additional information
-
construction of 20alpha-HSD knockout animals, 20alpha-HSD is not required for the regulation of X-zone growth
additional information
-
construction of gene disruption mutants by homologous recombination lacking enzyme expression and activity, the mutant female mice lack parturition on day 20 of pregnancy, overview
additional information
-
targeted disruption of 20alpha-hydroxysteroid dehydrogenase gene results in complete loss of catalytic activity and lack of increase in serum concentrations of 20alpha-dihydroprogesterone during pseudopregnancy or pregnancy. The durations of the estrious cycle, pseudopregnancy, and pregnancy are significantly prolonged in the mutant mice, and the number of pups, espcially live pups, is markedly decreased
additional information
-
construction of 20alpha-HSD knockout animals, 20alpha-HSD is not required for the regulation of X-zone growth
-
additional information
-
loops of 3alpha-hydroxysteroid dehydrogenase exchanged by PCR generate 20alpha-hydroxysteroid dehydrogenase, loops A, B and C yields total 20alpha-hydroxysteroid dehydrogenase activity, replacement of A and C yields bifunctional enzyme, several point mutations in the pocket of 3alpha-hydroxysteroid dehydrogenase show no 20alpha-hydroxysteroid dehydrogenase activity
additional information
-
a deletion mutant lacking residues R320 to L337 shows higher conversion rates of steroid hormones than wild-type. Especially 5alpha-dihydrotestosterone is more readily reduced
