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Literature summary extracted from

  • Ichimasa, M.; Morooka, T.; Niimura, T.
    Purification and properties of a membrane-bound phospholipase B from baker's yeast (Saccharomyces cerevisiae) (1984), J. Biochem., 95, 137-145.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.5 sodium deoxycholate 0.1%, strongly stimulates phospholipase B activity Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.5 Al3+
-
 Saccharomyces cerevisiae
3.1.1.5 deoxycholate
-
 Saccharomyces cerevisiae
3.1.1.5 Fe3+
-
 Saccharomyces cerevisiae
3.1.1.5 Hg2+ 5 mM, inhibits phospholipase B activity by 67%, no inhibition of lysophospholipase activity Saccharomyces cerevisiae
3.1.1.5 SDS
-
 Saccharomyces cerevisiae
3.1.1.5 Triton X-100
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.5 0.18
-
 phosphatidylcholine
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.5 membrane tightly bound to membrane Saccharomyces cerevisiae 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.5 330000
-
 gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.5 Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.5 side-chain modification
-
 Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.5
-
 Saccharomyces cerevisiae

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.5 40
-
 phospholipase B activity Saccharomyces cerevisiae
3.1.1.5 193
-
 lysophospholipase activity Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.5 1-acyl-sn-glycero-3-phosphocholine + H2O
-
 Saccharomyces cerevisiae fatty acid + glycero-3-phosphocholine
-
 ?
3.1.1.5 2-acylglycerophosphocholine + H2O 2-acyl-sn-glycero-3-phosphocholine Saccharomyces cerevisiae fatty acid + glycerylphosphocholine
-
 ?
3.1.1.5 phosphatidylcholine + H2O phospholipase B activity, hydrolyzes the acyl ester bonds sequentially, first the 2-acyl group and then the 1-acyl group Saccharomyces cerevisiae lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.5 3.5 4
-
 Saccharomyces cerevisiae