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Title: The Properties and Functions of Alanopine Dehydogenase and Octopine Dehydrogenase from the Pedal Retractor Muscle of Strombidae (Class Gastropoda)
Authors: Baldwin, J.
England, W.R.
Issue Date: Jul-1982
Publisher: University of Hawai'i Press
Citation: Baldwin J, England WR. 1982. The properties and functions of alanopine dehydogenase and octopine dehydrogenase from the Pedal Retractor Muscle of Strombidae (class gastropoda). Pac Sci 36(3): 381-394.
Abstract: The pedal retractor muscles of Strombidae contain high activities
of both alanopine dehydrogenase and octopine dehydrogenase, raising questions
as to the functions of these two enzymes during muscle anoxia associated with
locomotion. Alanopine dehydrogenase and octopine dehydrogenase were isolated
from the pedal retractor muscle of Strombus luhuanus, and their structural
and kinetic properties investigated. Alanopine dehydrogenase occurs as a single
electrophoretic form with a molecular weight of approx. 42,000. Octopine dehydrogenase
was electrophoretically polymorphic, existing as three alleles in the
population of animals studied. The major form of the enzyme had a molecular
weight of approx. 39,000. Both enzymes displayed similar pH optima for the
forward (pyruvate reduction) reaction and similar Km values for the common
substrates pyruvate and NADH.
During bursts of leaping, both octopine and strombine/alanopine accumulated
in the pedal retractor muscles of Strombidae. However, during recovery
from exercise, only strombine/alanopine accumulated. Octopine was a potent
inhibitor of the forward reaction catalyzed by octopine dehydrogenase, and may
act to prevent further octopine production during the recovery phase. The results
of this study show that both alanopine dehydrogenase and octopine dehydrogenase
are functioning to catalyze the terminal step of anaerobic glycolysis
during muscle anoxia associated with locomotion.
ISSN: 0030-8870
Appears in Collections:Pacific Science Volume 36, Number 3, 1982

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