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Literature summary for 3.1.1.32 extracted from

  • Gaspar, A.H.; Machner, M.P.
    VipD is a Rab5-activated phospholipase A1 that protects Legionella pneumophila from endosomal fusion (2014), Proc. Natl. Acad. Sci. USA, 111, 4560-4565.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.32

Activating Compound

Activating Compound Comment Organism Structure
Rab22 a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding Legionella pneumophila
Rab5 a guanine nucleotide binding protein, activates the VipD phospholipase A1, C-terminal binding, enzyme activity with constitutively active conformation of Rab5, Rab5a Q79L or Rab5c Q80L, is compared with the constitutively inactive forms Rab5a S34N or Rab5c S35N. Active Rab5 stimulates phospholipase activity only in full-length VipD, not in the truncated enzyme comprising residues 2-621 Legionella pneumophila

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in COS-1 cells, recombinant expression in Saccharomyces cerevisiae strain INVSc1, Rab5 enhances the growth defect of yeast cells producing VipD Legionella pneumophila

Protein Variants

Protein Variants Comment Organism
D286A site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD Legionella pneumophila
G288A site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD Legionella pneumophila
G43S site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD Legionella pneumophila
G75A site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD Legionella pneumophila
additional information truncated enzyme mutant VipD2-621 is inactive with a primarily cytosolic localization, the loss of enzyme activity is likely not because of a folding defect of the VipD2–621 point mutants because they still interact with Rab5c(Q80L) Legionella pneumophila
S73A site-directed mutagenesis, the active site mutant shows highly reduced activity compared to the wild-type enzyme VipD Legionella pneumophila

Inhibitors

Inhibitors Comment Organism Structure
methyl arachidonyl fluorophosphonate blocks phospholipase A1 as well as phospholipase A2 activity Legionella pneumophila

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Legionella pneumophila the enzyme VipD possesses phospholipase A1 but not phospholipase A2 activity, EC 3.1.1.4 ?
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 ?

Organism

Organism UniProt Comment Textmining
Legionella pneumophila
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme VipD possesses phospholipase A1 but not phospholipase A2 activity, EC 3.1.1.4 Legionella pneumophila ?
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 ?

Synonyms

Synonyms Comment Organism
PLA1
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 Legionella pneumophila
Rab5-activated phospholipase A1
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 Legionella pneumophila
VipD
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 Legionella pneumophila

General Information

General Information Comment Organism
physiological function the T4SS-translocated effector protein VipD exhibits phospholipase A1 activity that is activated only upon binding to endosomal Rab5 or Rab22, VipD protects Legionella pneumophila from endosomal fusion, that way, the pathogen Legionella pneumophila bypasses the microbicidal endosomal compartment of mammalian macrophages. By catalyzing phosphatidylinositol 3-phosphate depletion in a Rab5-dependent manner, VipD alters the protein composition of endosomes thereby blocking fusion with Legionella-containing vacuoles, implicated molecular mechanism, overview. The enzyme VipD alters the endosomal protein and lipid composition Legionella pneumophila