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Literature summary for 3.4.21.96 extracted from

  • Exterkate, F.A.; Alting, A.C.
    Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase (1999), Appl. Environ. Microbiol., 65, 1390-1396.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant MG 1363 strains containg plasmid-located hybrid proteinase genes constructed from SK11 and Wg2 Lactococcus lactis

Localization

Localization Comment Organism GeneOntology No. Textmining

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
Cd2+ can replace Ca2+ Lactococcus lactis
additional information Mn2+ is much less efficient, Zn2+, Mg2+, Ba2+, Ni2+, Co2+, Cu2+, and Sn2+ have no significant effect Lactococcus lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
145000
-
Ca-free enzyme, gel filtration Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
subsp. cremoris SK11, subsp. cremoris Wg2, MG1363
-

Storage Stability

Storage Stability Organism
0°C, Ca-free enzyme, storage on ice results in a gradual loss of potential activity, 20% reduction in activity after 4 h Lactococcus lactis

Synonyms

Synonyms Comment Organism
lactococcal 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