Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase

Article Abstract:

A large C-terminal extension in the mature lactococcal cell envelope proteinase (CEP) plays an essential role with regard to the ultimate distinct Ca2+ dependence of the proteinase domain. Specifically, removal of relatively weakly bound calcium in CEP triggers a structural rearrangement in the proteinase domain. This rearrangement results in an enzyme that has a lower specific activity aside from being susceptible to autoproteolytic release. In the case of the SK11 CEP, the enzyme is destabilized against thermal denaturation, due to which no activity can be detected at 25 degrees C and pH 6.5.

Calcium ions, Bacterial cell walls, Calcium-binding proteins, Calcium binding proteins

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Regulation of proteolytic enzyme activity in Lactococcus lactis

Article Abstract:

A high peptide medium decreases the activity of the proteolytic enzyme, the extracellular serine proteinase (PrtP), in batch and continuous cultures of the anaerobic bacteria Lactococcus lactis. The activity of PrtP is high in cells grown in milk which has a low peptide content. The activity of the intracellular aminopeptidase (PepN) and the X-prolyl-dipeptidyl aminopeptidase (PepXP) is similar to that of PrtP in the strain MG1363. In the strain SK1128, PepN and PepXP are unaffected by the peptide content.

Physiological aspects, Observations, Proteases, Peptides, Anaerobic bacteria, Enzyme regulation

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Molecular and functional analyses of the metC gene of Lactococcus lactis, encoding cystathionine beta-lyase

Article Abstract:

The enzyme coded by the metC gene in Lactococcus lactis can degrade cystathionine. These enzymes are used to create flavor in cheese.

Lactobacillus

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