Cloned (Comment) | Organism |
---|---|
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are expressed in Escherichia coli | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH | Oryctolagus cuniculus |
General Stability | Organism |
---|---|
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH | Oryctolagus cuniculus |
the transition midpoints, 50% activity after 1 h incubation in guanidine HCl, are 0.77 M for the mutant enzyme with a deletion of 10 N-terminal amino acids, 0.92 M for the mutant with a deletion of 5 N-terminal amino acids and 1.7 M for the wild-type enzyme | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Oryctolagus cuniculus |
Renatured (Comment) | Organism |
---|---|
denaturation in 6 M guanudine HCl for 2 min, then dilution 100fold in 0.1 M phosphate buffer, pH 7.5, containing 10 mM beta-mercaptoethanol. After standing for 1 h 18% of the wild-type activity is regained, 20% is regained after 12 h. The mutant enzyme with a deletion of 5 N-terminal amino acids is restored to 15% and 17% after 1 h and 12 h renaturation. The mutant with a deletion of 10 N-terminal amino acids can only be restored to 3% of the original activity after 1 h renaturation and at most 7% after 12 h | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate + NADH + H+ | - |
Oryctolagus cuniculus | (S)-lactate + NAD+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | wild-type enzyme and N-terminal deletion mutants lacking the first 5 or the first 10 amino acids | Oryctolagus cuniculus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
46 | - |
1 h, 25°C, 50% loss of activity, mutant enzyme with a deletion of 10 N-terminal amino acids | Oryctolagus cuniculus |
50 | - |
1 h, 25°C, 50% loss of activity, mutant enzyme with a deletion of 5 N-terminal amino acids | Oryctolagus cuniculus |
68 | - |
1 h, 25°C, 50% loss of activity, wilde-type enzyme | Oryctolagus cuniculus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3.8 | 7 | 1 h, 25°C, pH 3.8: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 10 N-terminal amino acids | Oryctolagus cuniculus |
5.5 | 7 | 1 h, 25°C, pH 5.5: 50% loss of activity, pH 7.0: stable, wilde-type enzyme | Oryctolagus cuniculus |
5.7 | 7 | 1 h, 25°C, pH 5.7: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 5 N-terminal amino acids | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Oryctolagus cuniculus |