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Literature summary for 3.1.1.32 extracted from

  • Scandella, C.J.; Kornberg, A.
    A membrane-bound phospholipase A1 purified from Escherichia coli (1971), Biochemistry, 10, 4447-4456.
    View publication on PubMed
Search for more literature for 3.1.1.32

General Stability

General Stability Organism
stable in 3% SDS Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
SDS Triton enhances the inhibitory effect Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0003
-
 phosphatidylglycerol
-
 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane bound to Escherichia coli 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 x * 29000, SDS-PAGE Escherichia coli
60000
-
 sucrose density gradient sedimentation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + H2O hydrolysis of L-phosphatidylcholine and not D-phosphatidylcholine Escherichia coli ?
-
 ?
phosphatidylethanolamine + H2O
-
 Escherichia coli ?
-
 ?
phosphatidylglycerol + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
? x * 29000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
5.2 8.4 pH 5.2: 10% of maximal activity, pH 6.5: about 50% of maximal activity, pH 8.4: optimum Escherichia coli