The adaptation of enzymes to temperature: catalytic characterization of glucosephosphate isomerase homologues isolated from Mytilus edulis and Isognomon alatus, bivalve molluscs inhabiting different thermal environments |
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Authors: | Hall JG |
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Institution: | Department of Ecology and Evolution, State University of New York, Stony Brook. |
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Abstract: | Homologues of glucosephosphate isomerase (GPI, EC 5.3.1.9) were purified to
homogeneity and kinetically characterized from Mytilus edulis and Isognomon
alatus, two bivalve molluscs experiencing contrasting thermal environments.
The enzyme isolated from I. alatus functions at warmer temperatures (25-35
C) than GPI from M. edulis, a species that inhabits colder marine littoral
habitats (5-20 C). The former exhibits apparent first-order (with respect
to substrate) catalytic rate constants (Vmax/KM) in vitro that become
progressively greater than the mussel enzyme as the assay temperature is
raised. Apparent zero-order catalytic rate constants (Vmax) are relatively
less differentiated. Catalytic efficiency, defined as the rate at which a
catalytic event occurs in either reaction direction for reference standard
states (substrate concentrations), is greater for the enzyme from the
tropical species (I. alatus) at all realistic combinations of temperature
and substrate concentration except for the lowest temperatures and highest
substrate concentrations, where the GPI from the boreal/temperate M. edulis
is more efficient. This pattern of catalytic divergence appears to be due
primarily to differentiation in Vmax/KM. These results and other published
data are reviewed and shown to be inconsistent with claims that adaptation
of enzymes to higher cell temperatures requires a loss in catalytic
efficiency.
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