Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Streptomyces sp. K30 |
Crystallization (Comment) | Organism |
---|---|
sitting-drop vapour diffusion method | Streptomyces sp. K30 |
Protein Variants | Comment | Organism |
---|---|---|
K167A | specific activity of polyisoprene oxidation is reduced to 20%, the product spectrum is unchanged | Streptomyces sp. K30 |
K167H | specific activity of polyisoprene oxidation is reduced to 12%, the product spectrum is unchanged | Streptomyces sp. K30 |
R164A | mutant enzyme contains the heme cofactor, but shows no detectable activity | Streptomyces sp. K30 |
T168A | mutant enzyme contains the heme cofactor, but shows only 2% residual activity compared to the wild type | Streptomyces sp. K30 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. K30 | Q3L8N0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Streptomyces sp. K30 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cis-1,4-polyisoprene + O2 | the enzyme acts as an endo-type dioxygenase producing C20 and higher oligo-isoprenoids that differ in the number of isoprene units but have the same terminal functions, CHO-CH2- and -CH2-COCH3 | Streptomyces sp. K30 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
latex clearing protein | - |
Streptomyces sp. K30 |
Lcp | - |
Streptomyces sp. K30 |
rubber oxygenase | - |
Streptomyces sp. K30 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Streptomyces sp. K30 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Streptomyces sp. K30 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome | b-type cytochrome. The haem group of LcpK30 is ligated to the polypeptide by a proximal histidine (His198) and by a lysine residue (Lys167) as the distal axial ligand | Streptomyces sp. K30 |