Abstract:
:The kinetics of AMP-aminohydrolase, which under steady state conditions shows a typical sigmoid dependence of initial velocities versus substrate concentration, have been examined by rapid mixing methods. Using this technique it was observed that when substrate or substrate plus activator (K(+)) were mixed with enzyme, the rate of appearance of product markedly increased during the first few tenths of a second. The time course of this change in rate was taken to reflect the progress of activation by substrate or by K(+). On the other hand, addition of activator to enzyme prior to mixing with substrate gave process curves for the formation of product consistent with normal Michaelis-Menten behaviour.Under the conditions where the reaction was examined, the enzyme at time zero had less than 10% of the activity of the fully active enzyme. The time course for activation with K(+) followed a first order process with a rate constant of 10.6 sec(-1) at 20 degrees C. A simple mechanism consistent with the data and capable of explaining the sigmoid dependence of initial velocities versus substrate concentrations observed in steady state kinetics was proposed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Suelter CH,Kovacs AL,Antonini Edoi
10.1016/0014-5793(68)80102-4keywords:
subject
Has Abstractpub_date
1968-11-01 00:00:00pages
65-68issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(68)80102-4journal_volume
2pub_type
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