Thermal resistance of pantetheine hydrolase.
Pantetheine hydrolase from pig kidney shows a very high resistance to denaturation with chemical denaturants, being unfolded at concentrations of guanidinium chloride higher than 6.5 M. On the contrary, chemical inactivation, followed by recording catalytic activity, occurs before conformational changes can be detected by fluorimetric or spectroscopic measurements. The enzyme resists temperatures as high as 80 degrees C, as monitored by second derivative spectroscopy and circular dichroism. Activity increases with temperature to an optimum of about 70 degrees C recording the initial velocity. The enzyme behaves very differently against chemical denaturants or against temperature denaturation. These results are unusual for a mesophilic protein.
Pitari
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Dipartimento di Biologia di Base e Applicata, Università degli Studi L'Aquila, Italy.
Antonini
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Mancini
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Duprè
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D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D002942:Circular Dichroism; D004795:Enzyme Stability / Q000502:physiology*; D058851:GPI-Linked Proteins; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D011489:Protein Denaturation; D013552:Swine; D013696:Temperature
D058851:GPI-Linked Proteins; D006146:Guanidines; D000581:Amidohydrolases; C022314:pantetheinase; D019791:Guanidine