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Literature summary for 3.1.1.4 extracted from

  • Kishimura, H.; Ando, S.
    Characteristics of phospholipase A2 mutant of the starfish Asterina pectinifera (2007), Enzyme Microb. Technol., 40, 461-465.
No PubMed abstract available
Search for more literature for 3.1.1.4

Activating Compound

Activating Compound Comment Organism Structure
sodium deoxycholate optimal at 2-4 mM Patiria pectinifera

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli Patiria pectinifera

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis, insertion of Lys between Cys62 and Gly63, the mutant shows highly reduced activity compared to the wild-type enzyme, the ratio of specific activity of the PLA2 mutant for phosphatidylcholine to phosphatidylethanolamine is highly lower than that of wild-type PLA2 Patiria pectinifera

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Patiria pectinifera
Hg2+
-
 Patiria pectinifera
Zn2+
-
 Patiria pectinifera

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required at 1 mM or above by the wild-type and mutant enzyme Patiria pectinifera
Co2+ activates Patiria pectinifera
Mg2+ activates Patiria pectinifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + H2O Patiria pectinifera
-
 1-acylglycerophosphocholine + a carboxylate
-
 ?

Organism

Organism UniProt Comment Textmining
Patiria pectinifera O96100
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes, after solubilization from Escherichia coli inclusion bodies, by anion exchange chromatography and gel filtration to homogeneity Patiria pectinifera

Renatured (Commentary)

Renatured (Comment) Organism
PLA2 mutant, produced in inclusion bodies in Escherichia coli, dissociated with 8 M urea and 10 mM 2-mercaptoethanol and renatured by dialyzing against 10 mM Tris-HCl buffer, pH 8.0 Patiria pectinifera

Source Tissue

Source Tissue Comment Organism Textmining
pyloric cecum
-
 Patiria pectinifera
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
950
-
 purified mutant enzyme Patiria pectinifera
119000
-
 purified wild-type enzyme Patiria pectinifera

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dipalmitoyl-phosphatidylcholine + H2O substrate from egg yolk Patiria pectinifera 1-palmitoyl-glycerophosphocholine + palmitate
-
 ?
1,2-dipalmitoyl-phosphatidylethanolamine + H2O substrate from egg yolk Patiria pectinifera 1-palmitoyl-glycerophosphoethanolamine + palmitate
-
 ?
additional information relationship between polar-group specificity and structure of the pancreatic loop region, overview Patiria pectinifera ?
-
 ?
phosphatidylcholine + H2O
-
 Patiria pectinifera 1-acylglycerophosphocholine + a carboxylate
-
 ?

Subunits

Subunits Comment Organism
More relationship between polar-group specificity and structure of the pancreatic loop region, overview Patiria pectinifera

Synonyms

Synonyms Comment Organism
PLA2
-
 Patiria pectinifera

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Patiria pectinifera

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Patiria pectinifera