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Lysolecithin:lysolecithin acyltransferase from rabbit lung. A conformational study
International Journal of Peptide and Protein Research
|May 1, 1984
Summary
Rabbit lung lysolecithin:lysolecithin acyltransferase shows conformational changes affecting its transacylase activity. Ionic strength and lipids influence enzyme structure and function, suggesting two distinct conformations.
Area of Science:
- Biochemistry
- Enzymology
- Protein Conformation
Background:
- Lysolecithin:lysolecithin acyltransferase (LLAT) is an enzyme found in rabbit lung.
- Enzyme structure and conformation are critical for catalytic activity.
Purpose of the Study:
- To investigate the conformational properties of rabbit lung LLAT.
- To understand the relationship between enzyme conformation, ionic strength, and catalytic activity.
Main Methods:
- Studied enzyme conformation in solutions of varying ionic strength.
- Assessed transacylase and hydrolytic activities under different conditions.
- Investigated effects of pH and lipid addition on enzyme structure and function.
Main Results:
- High ionic strength induced a disordered conformation, while low ionic strength promoted structural ordering.
- Transacylase activity was linked to the disordered conformation and increased with NaCl addition.
- Lipids stabilized the disordered conformation, similar to NaCl.
- Acid denaturation indicated ionization groups (pK 5.9-6.4) are crucial for denaturation.
Conclusions:
- LLAT likely exists in two conformations, impacting lysolecithin binding during deacylation.
- Conformational states are influenced by ionic strength and lipids.
- The enzyme's properties suggest it may be a peripheral membrane protein.