Influence of possible in situ ionic environment on kinetics of purified citrate synthase from an osmoconformer sea anemone, Bunedosoma cavernata.
Kinetics of utilization of acetyl coenzyme A by citrate synthase of a sea anemone, an osmoconformer, were compared with those of citrate synthases of various osmoregulators. The Kms of the latter enzymes were substantially increased by higher concentrations of salt and the enzyme exhibited hyperbolic substrate saturation curves. Citrate synthase from sea anemone, on the other hand, exhibited allosteric kinetics and minimal effects of salt on its Km. We suggest that the adaptive advantage of this enzymic property to a sedentary osmoconforming organism such as sea anemone is obvious since the osmoregulating creatures are apparently unable to maintain an appropriate low ionic environment in situ and thus probably the Km of their citrate synthases at a low level.
D000494:Allosteric Regulation; D000818:Animals; D002417:Cattle; D002950:Citrate (si)-Synthase / Q000378:metabolism*; D003063:Cnidaria / Q000201:enzymology*; D033364:Decapoda / Q000201:enzymology; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D012615:Sea Anemones / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine; D014882:Water-Electrolyte Balance
D002950:Citrate (si)-Synthase; D007652:Oxo-Acid-Lyases