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Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase.
Monturiol-Gross, Laura; Villalta-Romero, Fabian; Flores-Díaz, Marietta; Alape-Girón, Alberto.
Affiliation
  • Monturiol-Gross L; Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
  • Villalta-Romero F; Centro de Investigación en Biotecnología, Escuela de Biología, Instituto Tecnológico de Costa Rica, Cartago, Costa Rica.
  • Flores-Díaz M; Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
  • Alape-Girón A; Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica.
FEBS Open Bio ; 11(12): 3262-3275, 2021 12.
Article in En | MEDLINE | ID: mdl-34709730
ABSTRACT
Bacterial phospholipases and sphingomyelinases are lipolytic esterases that are structurally and evolutionarily heterogeneous. These enzymes play crucial roles as virulence factors in several human and animal infectious diseases. Some bacterial phospholipases C (PLCs) have both phosphatidylcholinesterase and sphingomyelinase C activities. Among them, Listeria monocytogenes PlcB, Clostridium perfringens PLC, and Pseudomonas aeruginosa PlcH are the most deeply understood. In silico predictions of substrates docking with these three bacterial enzymes provide evidence that they interact with different substrates at the same active site. This review discusses structural aspects, substrate specificity, and the mechanism of action of those bacterial enzymes on target cells and animal infection models to shed light on their roles in pathogenesis.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Type C Phospholipases / Sphingomyelin Phosphodiesterase Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: FEBS Open Bio Year: 2021 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Type C Phospholipases / Sphingomyelin Phosphodiesterase Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: FEBS Open Bio Year: 2021 Document type: Article Affiliation country:
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