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Literature summary extracted from

  • Karray, A.; Frikha, F.; Ben Bacha, A.; Ben Ali, Y.; Gargouri, Y.; Bezzine, S.
    Biochemical and molecular characterization of purified chicken pancreatic phospholipase A2 (2009), FEBS J., 276, 4545-4554.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.4 sodium taurodeoxycholate maximum phospholipase activity at 1 mm sodium taurodeoxycholate. Displays 50% of its maximum activity in the absence of bile salt dependent Gallus gallus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.4 ligated into PCR-Blunt vector and transformed into Escherichia coli DH5alpha cells Gallus gallus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.4 Ca2+ essential for both catalysis and enzyme binding to the substrate. The catalytic Ca2+ may be coordinated in a tetrahedral environment formed by the oxygen atoms of Tyr28, Gly30, Gly32 and Asp49. Second Ca2+-binding site is conserved and is formed by four residues: Glu71, Ile72, Asn89, and Glu92. Optimal Ca2+ concentration is about 4 mM Gallus gallus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.4 14000
-
gel filtration Gallus gallus
3.1.1.4 14170
-
calculated from sequence Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.4 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.4 by ammonium sulfate and ethanol precipitation, followed by gel filtration and gel filtration, to homogeneity, with a yield of 16%, 2000fold Gallus gallus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.4 pancreas
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.4 0.2
-
extraction at pH 8.5, in 10 mM Tris/HCl buffer, 10 mM CaCl2, 0.15 M NaCl Gallus gallus
3.1.1.4 400
-
2000fold purified enzyme, at pH 9.5, 37°C, in the presence of 1 mM sodium taurodeoxycholate, 4 mM CaCl2 with phosphatidylcholine as substrate Gallus gallus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.4 phosphatidylcholine + H2O in the presence of substrate, the enzyme binds to the interface as an active form. This crucial step is mediated by a planar surface region of the protein. The corresponding hydrophobic surface involves hydrophobic residues (Leu2, Trp3, Phe19, Leu20, Leu31, Ile64, Leu65, Tyr69, Ile72, Tyr75, and Leu118), hydrophobic surface involved in lipid binding increases Gallus gallus 1-acylglycerophosphocholine + a carboxylate
-
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Subunits

EC Number Subunits Comment Organism
3.1.1.4 monomer non-glycosylated protein, SDS-PAGE Gallus gallus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.4 group IB PLA2
-
Gallus gallus
3.1.1.4 phospholipase A2
-
Gallus gallus
3.1.1.4 PLA2
-
Gallus gallus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.4 37
-
with phosphatidylcholine as substrate in the presence of 4 mM Ca2+ and 1 mM sodium taurodeoxycholate Gallus gallus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.4 37 40 loses ca. 80% of its activity after 20 min of incubation at 40°C Gallus gallus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.4 9.5
-
with phosphatidylcholine as substrate in the presence of 4 mM Ca2+ and 1 mM sodium taurodeoxycholate Gallus gallus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.4 4 9.5
-
Gallus gallus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.4 4
-
is inactivated after incubation for 30 min at pH values lower than 4 Gallus gallus