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Literature summary 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)

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.96 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
3.4.21.96 Cd2+ can replace Ca2+ Lactococcus lactis
3.4.21.96 additional information Mn2+ is much less efficient, Zn2+, Mg2+, Ba2+, Ni2+, Co2+, Cu2+, and Sn2+ have no significant effect Lactococcus lactis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.96 145000
-
 Ca-free enzyme, gel filtration Lactococcus lactis

Organism

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

Storage Stability

EC Number Storage Stability Organism
3.4.21.96 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

EC Number Synonyms Comment Organism
3.4.21.96 lactococcal cell envelope proteinase
-
 Lactococcus lactis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.96 25
-
 Ca-free cell-bound enzyme is extremely unstable, lose 99% of its potential activity within 20 min Lactococcus lactis