3.4.21.96: Lactocepin

This is an abbreviated version!
For detailed information about Lactocepin, go to the full flat file.

Word Map on EC 3.4.21.96

Reaction

Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain =

Synonyms

CEP, Extracellular lactococcal proteinase, Lactococcal cell wall-associated proteinase, Lactococcal cell envelope-associated proteinase, Lactococcal proteinase, PrtP, Cell-envelope-located serine proteinase, Cell-envelope proteinase, Cell-wall-bound proteinase, Lactocepin I, Lactococcal proteinase PI, Lactococcal PI-type proteinase, Lactococcal PIII-type poteinase, Cell wall-associated serine proteinase, Lactocepin, LP151, PrtP proteinase, cell envelope associated proteinase, lactococcal cell envelope proteinase, cell envelope proteinase, cell-bound cell envelope proteinase, cell wall anchored proteinase, PrtH, PrtH2

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.96 Lactocepin

Application

Application on EC 3.4.21.96 - Lactocepin

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
conversion of lactocepin substrate binding regions by allele exchange can effectively alter lactocepin specificity in industrial strains of Lactococcus lactis without significantly affecting other important strain properties. The methodology can be used to alter lactocepin specificity in commercial starter cultures with a propensity for bitter flavour defect
food industry
industry
nutrition
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cheese making, cheese starter organism, dairy industry
synthesis
additional information
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exposure of PrtP, and not its proteolytic activity, is responsible for greater cell hydrophobicity and adhesion. The increased bacterial affinity to polar and apolar solvents indicates that exposure of PrtP on lactococcal cell surface can enhance the capacity to exchange attractive van der Waals interactions, and consequently increase their adhesion to different types of solid surfaces and solvents. PrtP or its derivatives may be used as a tool to construct strains with increased adhesion that form protective biofilms