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Coenzyme A-dependent transacylation system in rabbit liver microsomes.
T Sugiura1, Y Masuzawa, K Waku
1Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
The Journal of Biological Chemistry
|November 25, 1988
Summary
Cofactor-independent and CoA-dependent transacylation activities were studied in rabbit tissues. Liver microsomes showed high CoA-dependent activity, crucial for selective lysophospholipid acylation.
Area of Science:
- Biochemistry
- Lipid Metabolism
Background:
- Transacylation reactions are vital for phospholipid remodeling.
- Understanding cofactor requirements and tissue specificity is key to elucidating these pathways.
Purpose of the Study:
- To investigate and compare cofactor-independent and CoA-dependent transacylation activities in rabbit tissues.
- To characterize the kinetic properties and fatty acid specificity of CoA-dependent transacylation.
Main Methods:
- Enzyme assays on rabbit tissue microsomes.
- Determination of kinetic parameters (Km, Vmax) for CoA-dependent transacylation.
- Fatty acid transfer experiments using radiolabeled phospholipids.
Main Results:
- Liver microsomes exhibited high CoA-dependent transacylation and low cofactor-independent activity.
- CoA-dependent transacylation showed specificity for certain fatty acids (18:2, 20:4, 18:0) and formed acyl-CoA without ATP.
- Kinetic parameters (Km, Vmax) were determined for 1-acyl-GPC and 1-acyl-GPE acceptors.
Conclusions:
- CoA-dependent transacylation is likely important for selective lysophospholipid acylation in vivo.
- This pathway may involve acyl-CoA:lysophospholipid acyltransferase cooperation for CoA generation.