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
2.60E+00 mM Human PMN [1]
2.50E-03 mM Mouse Fibroblasts Cytosolic PLA2 [2]
5.00E-02 mM Human Recombinant PLA2 (Phosphatidylcholine as the substrate) [3]
2.00E-02 mM Human Recombinant PLA2 (Phosphatidylethanolamine as the substrate) [3]
4.13E-01 ± 2.80E-02 mM Rat PMN Neutrophils [4]


Enzyme Turnover Numbers
Value Units Species Notes Reference
3600 Failed to parse (Cannot store math image on filesystem.): minute{-1} Human PMN [1]
2.6E+03± 0.1E+03 Failed to parse (Cannot store math image on filesystem.): minute{-1} Bos taurus 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."

[5]

References

  1. ↑ 1.0 1.1 Yang K. “Finding multiple target optimal intervention in disease-related molecular network.” Mol Syst Biol 2008, (4):228
  2. ↑ Spaargaren M. “Characterization and identification of an epidermal-growth-factor-activated phospholipase A2.” Biochem J. 1992 Oct 1; 287(Pt 1): 37–43.
  3. ↑ 3.0 3.1 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.
  4. ↑ Kawauchi Y. “Changes in kinetic properties of cytosolic phospholipase A2 in activated rat neutrophils.” Adv Exp Med Biol. 1997;433:439-42.
  5. ↑ [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.]

Related Reactions

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