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Literature summary for 1.1.1.27 extracted from

  • Zheng, Y.; Guo, S.; Guo, Z.; Wang, X.
    Effects of N-terminal deletion mutation on rabbit muscle lactate dehydrogenase (2004), Biochemistry (Moscow), 69, 401-406.
    View publication on PubMed

Cloned(Commentary)

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

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

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

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Renatured (Commentary)

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

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + NADH + H+
-
Oryctolagus cuniculus (S)-lactate + NAD+
-
?

Subunits

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 [°C]

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 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

Cofactor Comment Organism Structure
NADH
-
Oryctolagus cuniculus