Kinetic study of alpha-chymotrypsin-catalyzed synthesis of kyotorphin.
A kinetic analysis of reaction-rate data obtained during a series of optimization experiments of the alpha-chymotrypsin-catalyzed synthesis of kyotorphin has been performed. The kinetic data have been fitted to a model equation derived from a proposed sequential mechanism, which has been further simplified to a first-order equation as a function of the substrate consumption. Statistical tests performed validate the model, since the fitted constants were statistically significant. In addition, the activation energy of the process has been calculated and resulted to be 32.5 +/- 2.3 kJ/mol which is within the range of other enzymatic reactions.
Clapés
P
P
Biological Organic Chemistry Department, CSIC, Barcelona, Spain.
Valencia
G
G
Torres
J L
JL
Reig
F
F
García-Antón
J M
JM
Mata-Alvarez
J
J
D002918:Chymotrypsin / Q000378:metabolism*; D004723:Endorphins / Q000096:biosynthesis*; D007700:Kinetics
D004723:Endorphins; C019448:kyotorphin; D002918:Chymotrypsin