Cloned (Comment) | Organism |
---|---|
heterologously overexpressed in Escherichia coli | Agathobaculum desmolans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0008 | - |
cortisone | pH and temperature not specified in the publication | Agathobaculum desmolans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
134500 | - |
gel filtration | Agathobaculum desmolans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Agathobaculum desmolans | - |
- |
- |
Agathobaculum desmolans ATCC 43058 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Agathobaculum desmolans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
11-deoxycortisol + NADH + H+ | i.e. 4-pregnen-17,21-diol-3,20-dione, 49.8% of the activity compared to cortisone | Agathobaculum desmolans | ? + NAD+ | - |
? | |
11-deoxycortisol + NADH + H+ | i.e. 4-pregnen-17,21-diol-3,20-dione, 49.8% of the activity compared to cortisone | Agathobaculum desmolans ATCC 43058 | ? + NAD+ | - |
? | |
20beta-hydroxycortisone + NADH + H+ | under in vitro conditions, the enzyme catalyzes reductive reaction far more readily than oxidative reaction | Agathobaculum desmolans | cortisone + NADH + H+ | - |
r | |
20beta-hydroxycortisone + NADH + H+ | under in vitro conditions, the enzyme catalyzes reductive reaction far more readily than oxidative reaction | Agathobaculum desmolans ATCC 43058 | cortisone + NADH + H+ | - |
r | |
corticosterone + NADH + H+ | i.e. 4-pregnen-11beta,21-diol-3,20-dione, 39.8% of the activity compared to cortisone | Agathobaculum desmolans | ? + NAD+ | - |
? | |
corticosterone + NADH + H+ | i.e. 4-pregnen-11beta,21-diol-3,20-dione, 39.8% of the activity compared to cortisone | Agathobaculum desmolans ATCC 43058 | ? + NAD+ | - |
? | |
cortisone + NADH + H+ | the equilibrium for the recombinant enzyme clearly favors the reductive direction. Cortisol is the preferred substrate, as it is more rapidly converted to 20beta-dihydrocortisol relative to other structurally similar steroids tested | Agathobaculum desmolans | 20beta-hydroxycortisone + NAD+ | - |
r | |
cortisone + NADH + H+ | the equilibrium for the recombinant enzyme clearly favors the reductive direction. Cortisol is the preferred substrate, as it is more rapidly converted to 20beta-dihydrocortisol relative to other structurally similar steroids tested | Agathobaculum desmolans ATCC 43058 | 20beta-hydroxycortisone + NAD+ | - |
r | |
tetrahydrocortisol + NADH + H+ | i.e. 5beta-pregnan-3alpha,11beta,17,21-tetrol-20-one, 49.2% of the activity compared to cortisone | Agathobaculum desmolans | ? + NAD+ | - |
? | |
tetrahydrocortisol + NADH + H+ | i.e. 5beta-pregnan-3alpha,11beta,17,21-tetrol-20-one, 49.2% of the activity compared to cortisone | Agathobaculum desmolans ATCC 43058 | ? + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 33800, SDS-PAGE | Agathobaculum desmolans |
Synonyms | Comment | Organism |
---|---|---|
20beta-HSDH | - |
Agathobaculum desmolans |
desE | - |
Agathobaculum desmolans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 7.5 | reductive direction | Agathobaculum desmolans |
8.5 | 9.25 | oxidative direction | Agathobaculum desmolans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 10 | steroid reduction is observed within the pH range 4.0-10, retaining 19.9% of maximal activity at pH 4.0 and 29.5% of maximal activity at pH 10.0 | Agathobaculum desmolans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Agathobaculum desmolans | |
NADH | - |
Agathobaculum desmolans |