EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.3.6 | structure of the F359W mutant enzyme, hanging drop vapor diffusion method. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation | Streptomyces sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.3.6 | F359W | kcat for the F359W mutant-catalyzed reaction decreases 13fold relative to that of the wild-type-catalyzed reaction. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme. In the atomic-resolution structure of F359W, the indole ring of the tryptophan completely fills the tunnel and is observed in only a single conformation. The size of the indole is proposed to limit conformational rearrangement of residue 359 that leads to tunnel opening in the wild-type enzyme | Streptomyces sp. |
1.1.3.6 | G347N | mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme | Streptomyces sp. |
1.1.3.6 | N485D | mutant can not be saturated with oxygen. Transfer of hydride from the sterol to the flavin prosthetic group is no longer rate-limiting for the mutant enzyme. Kinetic cooperativity with respect to molecular oxygen is observed with the tunnel mutant, but not with the wild-type enzyme | Streptomyces sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.3.6 | O2 | - |
Streptomyces sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.6 | 0.0015 | - |
cholesterol | mutant enzyme G347N, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 0.0027 | - |
cholesterol | mutant enzyme F359W, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 0.0027 | - |
cholesterol | wild-type enzyme, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 0.0027 | - |
cholesterol | wild-type enzyme, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.004 | - |
cholesterol | mutant enzyme F359W, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.005 | - |
cholesterol | mutant enzyme G347N, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.0062 | - |
cholesterol | mutant enzyme N485D, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.007 | - |
cholesterol | mutant enzyme N485D, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 0.3 | - |
O2 | wild-type enzyme | Streptomyces sp. | |
1.1.3.6 | 0.617 | - |
O2 | mutant enzyme F359W | Streptomyces sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.3.6 | Streptomyces sp. | P12676 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.3.6 | - |
Streptomyces sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.3.6 | cholesterol + O2 | - |
Streptomyces sp. | cholest-4-en-3-one + H2O2 | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.6 | 0.035 | - |
cholesterol | mutant enzyme N485D, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.073 | - |
cholesterol | mutant enzyme N485D, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 0.85 | - |
cholesterol | mutant enzyme G347N, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 0.86 | - |
cholesterol | mutant enzyme F359W, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 1 | - |
cholesterol | mutant enzyme G347N, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 1.3 | - |
cholesterol | mutant enzyme F359W, determined by H2O2 detection | Streptomyces sp. | |
1.1.3.6 | 42 | - |
cholesterol | wild-type enzyme, determined by cholest-4-en-3-one detection | Streptomyces sp. | |
1.1.3.6 | 47 | - |
cholesterol | wild-type enzyme, determined by H2O2 detection | Streptomyces sp. |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.3.6 | 1.381 | - |
O2 | mutant enzyme F359W | Streptomyces sp. | |
1.1.3.6 | 1.383 | - |
O2 | wild-type enzyme | Streptomyces sp. |