Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leucaena leucocephala | Q08GL0 | - |
- |
Subunits | Comment | Organism |
---|---|---|
More | the native protein possesses four Trp residues exposed on the surface and 66% of helical structure, analysis of different enzyme structures by UV-circular dichroism and Rayleigh light scattering, detailed overview | Leucaena leucocephala |
Synonyms | Comment | Organism |
---|---|---|
cinnamoyl CoA reductase 1 | - |
Leucaena leucocephala |
Ll-CCRH1 | - |
Leucaena leucocephala |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Leucaena leucocephala |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 90 | the native enzyme undergoes rapid structural transitions at and above 45°C and starts forming aggregates at 55°C, the acid induced molten globule state state of the enzyme structure is stable up to 90°C, overview | Leucaena leucocephala |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Leucaena leucocephala |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
2 | 8 | Ll-CCRH1 is transformed into acid induced (pH 2.0) molten globule like structure, exhibiting altered secondary structure, diminished tertiary structure and exposed hydrophobic residues. The molten globule like structure is examined for the thermal and chemical stability. The altered secondary structure of L1-CCRH1 at pH 2.0 is stable up to 90°C. In presence of 0.25 M guanidine hydrochloride (GdnHCl), it gets transformed into different structure which is stable in the vicinity of 2 M GdnHCl (as compared to drastic loss of native structure in 2 M GdnHCl) as seen in far UV-CD spectra. The structural transition of Ll-CCRH1 at pH 2.0 followed another transition after readjusting the pH to 8.0, forming a structure with hardly any similarity to that of native protein | Leucaena leucocephala |