Detail of "13171-93-2"

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Kinetic properties of crystalline enzymes

Kinetic properties of crystalline enzymes. Carboxypeptidase A. Spilburg, Curtis A.; Bethune, J. L.; Vallee, Bert L. (Dep. Biol. Chem., Harvard Med. Sch., Boston, Mass., USA). Biochemistry, 16(6), 1142-50 (English) 1977. CODEN: BICHAW. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The conformations of carboxypeptidase A (I) differ in soln. and in the crystal. Kinetic studies of I crystals and solns. show that the phys. state is also a crit. parameter that affects function. For all substrates examd., crystn. of I markedly reduces catalytic efficiency 200-1000-fold. In addn., substrate inhibition, present in soln. for some small substrates, is abolished with crystals, while larger substrates with normal kinetics in soln. may exhibit activation with the crystals. The phys. state of I also affects the action of known modifiers of peptidase activity of I. In soln., addn. of benzoylglycine or cinnamic acid markedly increases the rate of hydrolysis of Z-Gly-Phe (Z = benzyloxycarbonyl), but with cryst. I, their addn. 11075-17-5 and 13171-93-2 which are cas registry numbers of substances are two of reagents here. hardly alters the activity. This is in accord with the weakening or absence of inhibitory I-substrate binding modes. Kinetic studies on crystals were carried out over a range of I concns., substrate concns., and crystal sizes and in all instances the results are in good agreement with previous theory for enzymes insolubilized by other means. The differences in the kinetic behavior of I crystals, and of their solns. bear importantly on efforts to interpret the function of I in structural terms. .