EC Number | Application | Comment | Organism |
---|---|---|---|
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Pseudomonas sp. |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Pimelobacter simplex |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Mycobacterium sp. |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Nocardia sp. |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Rhodococcus sp. |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Rhodococcus erythropolis |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces sp. |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Nocardia rhodochrous |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Nocardia erythropolis |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Rhodococcus equi |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces lividans |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Schizophyllum commune |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces hygroscopicus |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces griseocarneus |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces lavendulae |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Streptomyces violascens |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Brevibacterium sterolicum |
1.1.3.6 | medicine | determination of cholesterol in various sample types, determination of cholesterol in gall stones, determination of cholesterol on the cell membrane of erythrocytes, other cells and cellular compartments | Corynebacterium cholesterolicum |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.3.6 | expression in Streptomyces lividans | Brevibacterium sterolicum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.6 | fenpropimorph | irreversible inhibition; morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition | Comamonas testosteroni | |
1.1.3.6 | fenpropimorph | morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive | Nocardia erythropolis | |
1.1.3.6 | fenpropimorph | morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible non-competitive | Schizophyllum commune | |
1.1.3.6 | fenpropimorph | morpholine derivative, 50 mg/l, 50% inhibition, instantenous inhibition; reversible competitive mechanism | Streptomyces sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.3.6 | 60000 | - |
x * 60000, SDS-PAGE | Rhodococcus equi |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.6 | cholesterol + O2 | Pseudomonas sp. | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Pimelobacter simplex | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Mycobacterium sp. | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Comamonas testosteroni | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Nocardia sp. | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Rhodococcus sp. | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Rhodococcus erythropolis | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces sp. | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Nocardia rhodochrous | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Nocardia erythropolis | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Rhodococcus equi | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces lividans | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Schizophyllum commune | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces hygroscopicus | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces griseocarneus | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces lavendulae | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Streptomyces violascens | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Brevibacterium sterolicum | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Corynebacterium cholesterolicum | - |
cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | Rhodococcus sp. GK1 | - |
cholest-5-en-3-one + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.6 | Brevibacterium sterolicum | - |
- |
- |
1.1.3.6 | Comamonas testosteroni | - |
- |
- |
1.1.3.6 | Corynebacterium cholesterolicum | - |
- |
- |
1.1.3.6 | Mycobacterium sp. | - |
- |
- |
1.1.3.6 | Nocardia erythropolis | - |
- |
- |
1.1.3.6 | Nocardia rhodochrous | - |
- |
- |
1.1.3.6 | Nocardia sp. | - |
- |
- |
1.1.3.6 | Pimelobacter simplex | - |
- |
- |
1.1.3.6 | Pseudomonas sp. | - |
- |
- |
1.1.3.6 | Rhodococcus equi | - |
- |
- |
1.1.3.6 | Rhodococcus erythropolis | - |
- |
- |
1.1.3.6 | Rhodococcus sp. | - |
solated from soil | - |
1.1.3.6 | Rhodococcus sp. GK1 | - |
solated from soil | - |
1.1.3.6 | Schizophyllum commune | - |
- |
- |
1.1.3.6 | Streptomyces griseocarneus | - |
- |
- |
1.1.3.6 | Streptomyces hygroscopicus | - |
- |
- |
1.1.3.6 | Streptomyces lavendulae | - |
- |
- |
1.1.3.6 | Streptomyces lividans | - |
- |
- |
1.1.3.6 | Streptomyces sp. | - |
- |
- |
1.1.3.6 | Streptomyces violascens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.3.6 | ammonium sulfate, ion-exchange chromatography, gel filtration | Rhodococcus equi |
1.1.3.6 | choleterylglycine-CM-cellulose | Pseudomonas sp. |
1.1.3.6 | DEAE-cellulose, cholesterol affinity column, Sephadex G-150 | Pseudomonas sp. |
1.1.3.6 | partially purified by precipitation with ammonium sulfate | Rhodococcus sp. |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Pseudomonas sp. | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Pimelobacter simplex | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Mycobacterium sp. | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Nocardia sp. | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Rhodococcus sp. | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Rhodococcus erythropolis | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces sp. | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Nocardia rhodochrous | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Nocardia erythropolis | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Rhodococcus equi | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces lividans | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Schizophyllum commune | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces hygroscopicus | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces griseocarneus | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces lavendulae | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Streptomyces violascens | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Brevibacterium sterolicum | |
1.1.3.6 | cholesterol + O2 = cholest-5-en-3-one + H2O2 | bifunctional enzyme, catalyzes both the oxidation of DELTA5-ene-3beta hydroxysteroids with a trans A-B ring junction to the corresponding DELTA5-3-ketosteroid with the reduction of oxygen to hydrogen peroxide, and the isomerization to the DELTA4-3-ketosteroid | Corynebacterium cholesterolicum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.6 | cholesterol + O2 | - |
Pseudomonas sp. | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Pimelobacter simplex | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Mycobacterium sp. | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Comamonas testosteroni | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia sp. | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus sp. | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus erythropolis | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces sp. | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia rhodochrous | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia erythropolis | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus equi | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces lividans | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Schizophyllum commune | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces hygroscopicus | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces griseocarneus | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces lavendulae | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces violascens | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Brevibacterium sterolicum | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Corynebacterium cholesterolicum | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus sp. GK1 | cholest-4-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Pseudomonas sp. | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Pimelobacter simplex | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Mycobacterium sp. | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Comamonas testosteroni | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia sp. | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus sp. | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus erythropolis | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces sp. | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia rhodochrous | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Nocardia erythropolis | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus equi | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces lividans | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Schizophyllum commune | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces hygroscopicus | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces griseocarneus | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces lavendulae | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Streptomyces violascens | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Brevibacterium sterolicum | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Corynebacterium cholesterolicum | cholest-5-en-3-one + H2O2 | - |
? | |
1.1.3.6 | cholesterol + O2 | - |
Rhodococcus sp. GK1 | cholest-5-en-3-one + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.3.6 | ? | x * 60000, SDS-PAGE | Rhodococcus equi |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.3.6 | 6 | 8.2 | membrane bound enzyme | Rhodococcus sp. |
1.1.3.6 | 7 | 7.5 | extracellular enzyme | Rhodococcus sp. |