Time dependence of activation of muscle AMP-aminohydrolase by substrate and potassium ion.

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 Lett

journal_title

FEBS letters

authors

Suelter CH,Kovacs AL,Antonini E

doi

10.1016/0014-5793(68)80102-4

keywords:

subject

Has Abstract

pub_date

1968-11-01 00:00:00

pages

65-68

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(68)80102-4

journal_volume

2

pub_type

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