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

BRENDA support

Literature summary for 3.1.4.3 extracted from

  • Rossignol, G.; Merieau, A.; Guerillon, J.; Veron, W.; Lesouhaitier, O.; Feuilloley, M.G.; Orange, N.
    Involvement of a phospholipase C in the hemolytic activity of a clinical strain of Pseudomonas fluorescens (2008), BMC Microbiol., 8, 189.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.3

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pseudomonas fluorescens

Protein Variants

Protein Variants Comment Organism
additional information plcC-deficient mutants to determine whether PlcC contributes to the hemolytic activity of MFN1032. Construction of a plcC-overexpressing MFN1032 clone: MFN1036 Pseudomonas fluorescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 SDS-PAGE Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens Q1RQG7 biovar I, MFN1032
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + H2O substrate from egg yolk Pseudomonas fluorescens 1,2-diacylglycerol + phosphorylcholine
-
 ?

Synonyms

Synonyms Comment Organism
Lecithinase
-
 Pseudomonas fluorescens
phospholipase C
-
 Pseudomonas fluorescens
PLC
-
 Pseudomonas fluorescens
PlcC protein
-
 Pseudomonas fluorescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 comparison of the secreted hemolytic activities of MFN1032 and the plcC mutants at various growth temperatures Pseudomonas fluorescens