Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.4.3 extracted from

  • Slepkov, E.R.; Pavinski Bitar, A.; Marquis, H.
    Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes (2010), Biochem. J., 432, 557-563.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.3

Protein Variants

Protein Variants Comment Organism
C28A/C29A/D30A site-directed mutagenesis, the mutation has no effect on PC-PLC maturation Listeria monocytogenes
D30A/E31A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 75% of wild-type level Listeria monocytogenes
E31A site-directed mutagenesis, the mutation has no effect on PC-PLC maturation Listeria monocytogenes
E31A/Y32A/L33A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 42% of wild-type level Listeria monocytogenes
L33A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 54% of wild-type level Listeria monocytogenes
additional information construction and generation of PC-PLC propeptide deletion mutants Listeria monocytogenes
P36A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 82% of wild-type level Listeria monocytogenes
Q34A/T35A site-directed mutagenesis, the mutation has no effect on PC-PLC maturation Listeria monocytogenes
Q34A/T35A/P36A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 79% of wild-type level Listeria monocytogenes
Q34K/T35P site-directed mutagenesis, the mutation has no effect on PC-PLC maturation Listeria monocytogenes
Y32A site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 68% of wild-type level Listeria monocytogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information phosphatidylcholine phospholipase C compartmentalization and enzymatic activity is regulated by a 24-amino-acid propeptide, Cys28-Ser51. During intracytosolic multiplication, bacteria accumulate the proform of PC-PLC at their membrane-cell-wall interface, whereas during cell-to-cell spread vacuolar acidification leads to maturation and rapid translocation of PCPLC across the cell wall in a manner that is dependent on Mpl, the metalloprotease of Listeria Listeria monocytogenes
-
-

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
-
 several strains
-

Synonyms

Synonyms Comment Organism
PC-PLC
-
 Listeria monocytogenes
phosphatidylcholine phospholipase C
-
 Listeria monocytogenes

General Information

General Information Comment Organism
additional information PC-PLC maturation between bacterial plasma membrane and bacterial cell wall, translocation across the bacterial cell wall, and activity in the host cell, schematic overview. The N-terminus of the PC-PLC propeptide regulates the compartmentalization of PC-PLC. Enzyme enzymatic activity is regulated by a 24-amino-acid propeptide Cys28-Ser51. Individual amino acid residues within the N-terminus of the PC-PLC propeptide regulate Mpl-mediated maturation of PC-PLC. A single amino acid propeptide is sufficient to inhibit PC-PLC activity, whereas a six-residue propeptide is sufficient for Mpl to mediate the proteolytic maturation of PC-PLC Listeria monocytogenes