EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.15.8 | expression in Escherichia coli | Priestia megaterium |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.15.8 | A395L | Vmax/Km for progesterone is 2fold lower than wild-type value | Priestia megaterium |
1.14.15.8 | E90V/D185G | Vmax/Km for progesterone is 1.3fold higher than wild-type value | Priestia megaterium |
1.14.15.8 | G397P | the mutant exhibits 2% of the wild-type activity, Vmax/Km for progesterone is 51.7fold lower than wild-type value | Priestia megaterium |
1.14.15.8 | I86T | Vmax/Km for progesterone is 2fold higher than wild-type value | Priestia megaterium |
1.14.15.8 | K27R/I71T/I215T | Vmax/Km for progesterone is 2.5fold higher than wild-type value | Priestia megaterium |
1.14.15.8 | Q398S | Vmax/Km for progesterone is 5fold lower than wild-type value | Priestia megaterium |
1.14.15.8 | S394I | Vmax/Km for progesterone is 7.5fold lower than wild-type value | Priestia megaterium |
1.14.15.8 | T396R | mutant does not produce any hydroxylated product up to an adrenodoxin concentration of 0.1 mM | Priestia megaterium |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.15.8 | 0.0007 | - |
progesterone | pH 7.4, 30°C, mutant K27R/I71T/I215T | Priestia megaterium | |
1.14.15.8 | 0.0009 | - |
progesterone | pH 7.4, 30°C, mutant I86T | Priestia megaterium | |
1.14.15.8 | 0.001 | - |
progesterone | pH 7.4, 30°C, mutant E90V/D185G | Priestia megaterium | |
1.14.15.8 | 0.0012 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant I86T | Priestia megaterium | |
1.14.15.8 | 0.0015 | - |
progesterone | pH 7.4, 30°C, wild-type enzyme | Priestia megaterium | |
1.14.15.8 | 0.0015 | - |
deoxycorticosterone | pH 7.4, 30°C, wild-type enzyme | Priestia megaterium | |
1.14.15.8 | 0.0019 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant E90V/D185G | Priestia megaterium | |
1.14.15.8 | 0.0024 | - |
progesterone | pH 7.4, 30°C, mutant A395L | Priestia megaterium | |
1.14.15.8 | 0.0024 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant K27R/I71T/I215T | Priestia megaterium | |
1.14.15.8 | 0.0042 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant A395L | Priestia megaterium | |
1.14.15.8 | 0.0043 | - |
progesterone | pH 7.4, 30°C, mutant S394I | Priestia megaterium | |
1.14.15.8 | 0.0046 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant G397P | Priestia megaterium | |
1.14.15.8 | 0.0047 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant S394I | Priestia megaterium | |
1.14.15.8 | 0.0049 | - |
progesterone | pH 7.4, 30°C, mutant Q398S | Priestia megaterium | |
1.14.15.8 | 0.005 | - |
progesterone | pH 7.4, 30°C, mutant G397P | Priestia megaterium | |
1.14.15.8 | 0.0056 | - |
deoxycorticosterone | pH 7.4, 30°C, mutant Q398S | Priestia megaterium |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.8 | Priestia megaterium | Q06069 | ATCC 13368 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.15.8 | - |
Priestia megaterium |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.8 | 11-deoxycorticosterone + reduced adrenodoxin + O2 | adrenodoxin is a [2Fe-2S] ferredoxin involved in electron transfer from NADPH+ (via a reductase) to cytochrome P-450 in the adrenal gland, 15beta-hydroxy-deoxycorticosterone is the only product that is observed, both in the case of wild-type CYP106A2 and all the mutants (except T396R) | Priestia megaterium | 15beta-hydroxy-11-deoxycorticosterone + oxidized adrenodoxin + H2O | - |
? | |
1.14.15.8 | progesterone + reduced adrenodoxin + O2 | adrenodoxin is a [2Fe-2S] ferredoxin involved in electron transfer from NADPH+ (via a reductase) to cytochrome P-450 in the adrenal gland, 15beta-hydroxy-progesterone is the main product of wild-type enzyme and all mutants. In order to gain insights into the structure and function of CYP106A2, whose crystal structure is unknown, a homology model has been created. The substrate progesterone is then docked into the active site to predict which residues might affect substrate binding. The model is substantiated by using a combination of theoretical and experimental investigations | Priestia megaterium | 15beta-hydroxy-progesterone + oxidized adrenodoxin + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.8 | CYP106A2 | - |
Priestia megaterium |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.15.8 | 30 | - |
assay at | Priestia megaterium |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.15.8 | 7.4 | - |
assay at | Priestia megaterium |