Transformation of PL to AA

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Reaction

Catalysed by cPLA2α (3.1.1.4).

Chemical equation

Phospholipid \rightleftharpoons Arachidonic Acid

Rate equation

cPLA2a Parameters

Michaelis-Menten Constants
Value Units Species Notes Reference
2.50E-03 mM Mouse Fibroblasts Cytosolic PLA2 [1]
5.00E-02 mM Human Recombinant PLA2 (Phosphatidylcholine as the substrate) [2]
2.00E-02 mM Human Recombinant PLA2 (Phosphatidylethanolamine as the substrate) [2]
4.13E-01 ± 2.80E-02 mM Rat PMN Neutrophils [3]


Enzyme Turnover Numbers
Value Units Species Notes Reference
2.6E+03± 0.1E+03 per minute Bos taurus Organism: Bovine

Expression Vector: Bovine pancreatic PLA2 pH: 7.5 Temperature:25'C


Substrate - 1,2-diheptanoyl-sn-glycero-3-phosphorylcholine. "From the molecular weight, 13,795, the catalytic center activity for the micellar substrate, Kcat{app}, was calculated."

[4]
3000 per minute Porcine Organism: Porcine

Expression Vector: Porcine Enzme: Pancreatic phospholipase A, Substrate: 1,2-dipalmitoyl-phosphatidylcholine, Enzyme concentration: 0.2 mg/ml, pH: 8.0. Temperature: 41 C

[5]
11220 per minute Stingray Expression Vector: Stingray

Enzyme: Secreted pH:8.5 Temperature: 40 °C

[6]
8400 per minute Camel Expression Vector: Camel

Enzyme: Pancreatic pH: 8.5 Temperature: 40 °C

[6]
Enzyme Concentrations
Value Units Species Notes Reference
1 mM Porcine Pancreatic phospholipase A, Substrate: 1,2-dipalmitoyl-phosphatidylcholine, Enzyme concentration: 0.2 mg/ml, pH 8.0. [5]
3.7 mM Camel 18kDa protein, 20g of enzyme in 300ml solution.

Pancreatic, 4 mM NaTDC, 8 mM, CaCl2, pH 8,5 and 40 °C

[6]
0.004 mM Plant sPLA2 with 1,2-diheptanoyl-sn-glycero-3-phosphocholine as the substrate [7]

References

  1. ↑ Spaargaren M. “Characterization and identification of an epidermal-growth-factor-activated phospholipase A2.” Biochem J. 1992 Oct 1; 287(Pt 1): 37–43.
  2. ↑ 2.0 2.1 Kawauchi Y. “Preparation and characterization of human rheumatoid arthritic synovial fluid phospholipase A2 produced by recombinant baculovirus-infected insect cells.” J Biochem. 1994 Jul;116(1):81-7.
  3. ↑ Kawauchi Y. “Changes in kinetic properties of cytosolic phospholipase A2 in activated rat neutrophils.” Adv Exp Med Biol. 1997;433:439-42.
  4. ↑ [www.ncbi.nlm.nih.gov/pubmed/8454568 Hada S. “Hydrolysis of Micellar Diheptanoylphosphatidylcholine Catalyzed byBovine Pancreatic Phospholipase A2: Kinetic Characterization of Group I and II Enzymes1” J Biochem (1993) 113 (1): 13-17.]
  5. ↑ 5.0 5.1 [http://www.jbc.org/content/261/12/5328.long Menashe M. “Hydrolysis of Dipalmitoylphosphatidylcholine Small Unilamellar Vesicles by Porcine Pancreatic Phospholipase A2” J Biochem (1986) 261, 5328-5333.] Cite error: Invalid <ref> tag; name "Menashe1986" defined multiple times with different content
  6. ↑ 6.0 6.1 6.2 Bacha B. “Purification and biochemical characterization of pancreatic phospholipase A2 from the common stingray Dasyatis pastinaca” Lipids Health Dis. 10, 32 (2011)
  7. ↑ Mansfield J. “Secretory phospholipase A2- from Arabidopsis thaliana:functional parameters and substrate preference” Chemistry and Physics of Lipids 150 (2007) 156–166

Related Reactions

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