Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | 119% activity at 1 mM | Rhodococcus sp. | |
additional information | the enzyme displays 25% higher activity in 50 mM phosphate buffer than 50 mM Tris/HCl at the same pH | Rhodococcus sp. |
Cloned (Comment) | Organism |
---|---|
gene camK, cloning and expression in Escherichia coli XL1 Blue | Rhodococcus sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-hydroxymercuribenzoate | 14% inhibition at 1 mM | Rhodococcus sp. | |
Cu2+ | 72% inhibition at 1 mM | Rhodococcus sp. | |
Hg2+ | 98% inhibition at 1 mM | Rhodococcus sp. | |
N-ethylmaleimide | 68% inhibition at 1 mM | Rhodococcus sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.05 | - |
6-oxocamphor | pH 7.0, 25°C | Rhodococcus sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | Zn2+ has a poor influence on enzyme activity, no effect by 1 M NaCl | Rhodococcus sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28488 | - |
3 * 28488, mass spectrometry | Rhodococcus sp. |
83000 | - |
gel filtration | Rhodococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus sp. | Q93TU6 | gene camK | - |
Rhodococcus sp. NCIMB 9784 | Q93TU6 | gene camK | - |
Purification (Comment) | Organism |
---|---|
native enzyme 35.7fold from strain NCIMB 9784 | Rhodococcus sp. |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | strain NCIMB 9784 is grown on (1R)-(+)-camphor as the sole carbon source | Rhodococcus sp. | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
357.5 | - |
purified native enzyme, substrate 6-oxocamphor, pH 7.0, 25°C | Rhodococcus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-oxocamphor + H2O | the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview | Rhodococcus sp. | (2R,4S)-alpha-campholinic acid | - |
? | |
6-oxocamphor + H2O | the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview | Rhodococcus sp. NCIMB 9784 | (2R,4S)-alpha-campholinic acid | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | 3 * 28488, mass spectrometry | Rhodococcus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Rhodococcus sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
167 | - |
6-oxocamphor | pH 7.0, 25°C | Rhodococcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Rhodococcus sp. |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Rhodococcus sp. | isoelectric focusing | - |
8.5 |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the TetR/AcrR family of the crotonase superfamily | Rhodococcus sp. |