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Literature summary for 3.4.14.11 extracted from

  • Meyer, J.; Jordi, R.
    Purification and characterization of X-prolyl-dipeptidyl-aminopeptidase from Lactobacillus lactis and from Streptococcus thermophilus (1987), J. Dairy Sci., 70, 738-745.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Lactobacillus delbrueckii subsp. lactis
-
-
-
Streptococcus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptococcus thermophilus
-
Lactobacillus delbrueckii subsp. lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-Pro-7-amido-4-methylcoumarin + H2O
-
Streptococcus thermophilus Gly-Pro + 7-amino-4-methylcoumarin
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the enzyme from Streptococcus thermophilus is more sensitive to heat than the corresponding enzyme from Lactobacillus lactis Streptococcus thermophilus
additional information
-
the enzyme from Streptococcus thermophilus is more sensitive to heat than the corresponding enzyme from Lactobacillus lactis Lactobacillus delbrueckii subsp. lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8.2 hydrolysis of Gly-Pro-7-amido-4-methylcoumarin Streptococcus thermophilus
7
-
-
Lactobacillus delbrueckii subsp. lactis

pH Stability

pH Stability pH Stability Maximum Comment Organism
5
-
unstable below, the enzyme from Streptococcus thermophilus is more rapidly denatured than the enzyme from Lactobacillus lactis Streptococcus thermophilus
5
-
unstable below, the enzyme from Streptococcus thermophilus is more rapidly denatured than the enzyme from Lactobacillus lactis Lactobacillus delbrueckii subsp. lactis

pI Value

Organism Comment pI Value Maximum pI Value
Streptococcus thermophilus
-
-
4.5
Lactobacillus delbrueckii subsp. lactis
-
-
4.5