Difference between revisions of "Transformation of PL to AA"

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(cPLA2a Parameters)
(cPLA2a Parameters)
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|<ref name="Wilhelm2014"> [http://www.nature.com/nature/journal/v509/n7502/pdf/nature13319.pdf M. Wilhelm ''Mass-spectrometry-based draft of the human proteome'' Nature, 2014 509, 582–587]</ref>
 
|<ref name="Wilhelm2014"> [http://www.nature.com/nature/journal/v509/n7502/pdf/nature13319.pdf M. Wilhelm ''Mass-spectrometry-based draft of the human proteome'' Nature, 2014 509, 582–587]</ref>
 
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{|class="wikitable sortable"
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|+  style="text-align: left;" | Gibbs Free Energy Change
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! Value
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! Species
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! Notes
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! Reference
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|(-13.03833)
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|kcal/mol
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|Not stated
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|Estimated
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Enzyme: cPLA2
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Substrate: Phosphatidylcholine
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Product: 1-acyl-sn-glycero-3-phosphocholine and a long-chain fatty acid
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pH: 7.3
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ionic strength: 0.25
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|<ref name="MetaCyc”>[http://metacyc.org/META/NEW-IMAGE?type=REACTION&object=PHOSPHOLIPASE-A2-RXN Caspi et al 2014, "The MetaCyc database of metabolic pathways and enzymes and the BioCyc collection of Pathway/Genome Databases," Nucleic Acids Research 42:D459-D471]</ref>
 
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Revision as of 15:29, 18 August 2016

Return to overview

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]
cPLA2 Abundance
Value Units Species Notes Reference
8.26  ppm Human Expression Vector: Lung

Enzyme: cPLA2 pH: 7.5 Temperature: 37 °C

[7]
42.8  ppm Human Expression Vector: Uterine cervix

Enzyme: 5-LOX pH: 7.5 Temperature: 37 °C

[8]
111  ppm Human Expression Vector: Oral Cavity

Enzyme: cPLA2 pH: 7.5 Temperature: 37 °C

[8]
30.8  ppm Human Expression Vector: Liver

Enzyme: cPLA2 pH: 7.5 Temperature: 37 °C

[8]
Gibbs Free Energy Change
Value Units Species Notes Reference
(-13.03833) kcal/mol Not stated Estimated

Enzyme: cPLA2 Substrate: Phosphatidylcholine Product: 1-acyl-sn-glycero-3-phosphocholine and a long-chain fatty acid pH: 7.3 ionic strength: 0.25

[9]

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. [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.]
  6. 6.0 6.1 Bacha B. “Purification and biochemical characterization of pancreatic phospholipase A2 from the common stingray Dasyatis pastinaca” Lipids Health Dis. 10, 32 (2011)
  7. M. Kim A draft map of the human proteome Nature, 2014 509, 575–581
  8. 8.0 8.1 8.2 M. Wilhelm Mass-spectrometry-based draft of the human proteome Nature, 2014 509, 582–587
  9. Caspi et al 2014, "The MetaCyc database of metabolic pathways and enzymes and the BioCyc collection of Pathway/Genome Databases," Nucleic Acids Research 42:D459-D471

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