Evidence of a pH-dependent conformational change at the active site of lysolecithin:lysolecithin acyltransferase from rabbit lung.
It has been shown that both activities, hydrolysis and transacylation, of lysolecithin:lysolecithin acyltransferase, as well as the conformation of the polypeptide are critically dependent on a pK around 5.8, but the question remains if the same residue(s) is responsible for the conformational change and the loss of activity. In this paper, ultrasonic cavitation is used to study the pH-dependent inactivation. The results show that there are two first-order inactivation constants which depend on pH and that the transition between them has a pK of 5.9. As the constants of ultrasonic inactivation are very dependent on the accessibility of the residues it is concluded that the conformational change modifies the accessibility of the active site.
Pérez-Gil
J
J
Departamento de Bioquímica, Universidad Complutense, Facultad de Química, Madrid, Spain.
Martín
J J
JJ
Mancheño
J M
JM
Acebal
C
C
Arche
R
R
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000378:metabolism*; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008168:Lung / Q000201:enzymology*; D008433:Mathematics; D011487:Protein Conformation; D011817:Rabbits
D000217:Acyltransferases; D008243:1-Acylglycerophosphocholine O-Acyltransferase