Difference between revisions of "Transformation of PL to AA"
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Revision as of 11:17, 13 April 2016
Contents
Reaction
Catalysed by cPLA2α (3.1.1.4).
Chemical equation
Rate equation
cPLA2a Parameters
| Value | Units | Species | Notes | Reference |
|---|---|---|---|---|
| 2.50E-03 | 
|
Mouse | Fibroblasts Cytosolic PLA2 | [1] |
| 5.00E-02 |
|
Human | Recombinant PLA2 (Phosphatidylcholine as the substrate) | [2] |
| 2.00E-02 |
|
Human | Recombinant PLA2 (Phosphatidylethanolamine as the substrate) | [2] |
| 4.13E-01 ± 2.80E-02 |
|
Rat | PMN Neutrophils | [3] |
| Value | Units | Species | Notes | Reference |
|---|---|---|---|---|
| 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." |
[4] |
References
- ↑ Spaargaren M. “Characterization and identification of an epidermal-growth-factor-activated phospholipase A2.” Biochem J. 1992 Oct 1; 287(Pt 1): 37–43.
- ↑ 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.
- ↑ Kawauchi Y. “Changes in kinetic properties of cytosolic phospholipase A2 in activated rat neutrophils.” Adv Exp Med Biol. 1997;433:439-42.
- ↑ [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.]
