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Title: Some Catalytic and Regulatory Properties of Pyruvate Kinase from the Spadix and Retractor Muscles of Nautilus pompilius 
Author: Fields, Jeremy HA
Date: 1982-07
Publisher: University of Hawai'i Press
Citation: Fields JHA. 1982. Some catalytic and regulatory properties of pyruvate kinase from the spadix and retractor muscles of Nautilus pompilius. Pac Sci 36(3): 315-324.
Abstract: Pyruvate kinase was partially purified from the spadix and retractor
muscles of Nautilus pompilius. In both cases, the enzyme was activated by
magnesium and potassium ions with similar affinities (apparent Ka values were
0.63 ± 0.04 mM and 5.8 ± 0.4 mM, respectively, for the enzyme from the
spadix; and 0.77 ± 0.06 mM and 6.7 ± 0.8 mM, respectively, for the enzyme
from the retractor muscle). The enzymes showed normal hyperbolic saturation
kinetics for the substrates adenosine Y-diphosphate and phosphoenolpyruvate,
and the apparent Km values were identical when measured at saturating concentrations
of the cosubstrate (apparent Km values were 0.28 ± 0.01 mM and
0.063 ± 0.005 mM, respectively, for the spadix). Adenosine 5'-triphosphate,
alanine, and citrate were found to be inhibitors. The enzyme from the spadix was
more susceptible to inhibition by alanine than that from the retractor muscle.
For the latter enzyme, inhibition by alanine was noncompetitive with respect to
phosphoenolpyruvate, but the inhibition was nonlinear; it also decreased the
affinity for Mg2+. For the enzyme from the spadix, inhibition by alanine changed
the saturation kinetics for phosphoenolpyruvate to sigmoidal form. The affinity
for Mg2+ was also decreased by alanine. For both enzymes, fructose-I,
6-bisphosphate at a concentration of 0.05 mM partially reversed the inhibition
by alanine, but not that by adenosine Y-triphosphate. The sigmoidal kinetics
observed for phosphoenolpyruvate could also be reversed by increasing the
concentration of Mg2 +. In general, the properties were found to be similar to
those of other pyruvate kinases from the mantle muscle of squid and octopus,
except for the observation of inhibition by alanine. These regulatory properties
are discussed with respect to potential control of glycolytic flux during muscle
activity.
ISSN: 0030-8870
URI: http://hdl.handle.net/10125/464

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