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Literature summary for 3.4.21.96 extracted from

  • Exterkate, F.A.
    Structural changes and interactions involved in the Ca(2+)-triggered stabilization of the cell-bound cell envelope proteinase in Lactococcus lactis subsp. cremoris SK11 (2000), Appl. Environ. Microbiol., 66, 2021-2028.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
nutrition cheese making, cheese starter organism, dairy industry Lactococcus lactis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Lactococcus lactis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ triggers stabilization, removal of weakly bound Ca2+ from the native cell-bound enzyme is coupled with a significant reversible decrease in specific activity and a dramatic reversible reduction in thermal stability Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
mature active enzyme Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
subsp. cremoris SK11
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Suc-Ala-Glu-Pro-Phe-p-nitroanilide + H2O
-
Lactococcus lactis ?
-
?

Synonyms

Synonyms Comment Organism
cell envelope proteinase
-
Lactococcus lactis
cell-bound cell envelope proteinase
-
Lactococcus lactis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
Ca-free cell-bound enzyme is extremely unstable, lose 99% of its potential activity within 20 min Lactococcus lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.8 6 Ca-free enzyme Lactococcus lactis
6.4
-
Ca-loaded enzyme Lactococcus lactis

pH Range

pH Minimum pH Maximum Comment Organism
4 8
-
Lactococcus lactis
5.8 7 Ca-free enzyme Lactococcus lactis