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Literature summary for 3.1.1.5 extracted from

  • Oishi, H.; Morimoto, T.; Watanabe, Y.; Tamai, Y.
    Purification and characterization of phospholipase B from Kluyveromyces lactis, and cloning of phospholipase B gene (1999), Biosci. Biotechnol. Biochem., 63, 83-90.
    View publication on PubMed
Search for more literature for 3.1.1.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Kluyveromyces lactis

Protein Variants

Protein Variants Comment Organism
D406A loss of enzymatic activity Kluyveromyces lactis
R112A loss of enzymatic activity Kluyveromyces lactis

Metals/Ions

Metals/Ions Comment Organism Structure
Al3+ Ca2+, Fe3+ or Al3+ required Kluyveromyces lactis
Ca2+ Ca2+, Fe3+ or Al3+ required Kluyveromyces lactis
Fe3+ Ca2+, Fe3+ or Al3+ required Kluyveromyces lactis

Organism

Organism UniProt Comment Textmining
Kluyveromyces lactis O59863
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Kluyveromyces lactis

Purification (Commentary)

Purification (Comment) Organism
-
 Kluyveromyces lactis

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Kluyveromyces lactis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lysophosphatidylcholine + H2O
-
 Kluyveromyces lactis glycerophosphorylcholine + unesterified fatty acid
-
 ?
phosphatidylcholine + H2O
-
 Kluyveromyces lactis lysophosphatidylcholine + glycerophosphorylcholine + a carboxylate
-
 ?

Synonyms

Synonyms Comment Organism
PLB
-
 Kluyveromyces lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2
-
 and a second optimum at pH 7.5 Kluyveromyces lactis
7.5
-
 and a second optimum at pH 2.0 Kluyveromyces lactis