Protein Design and the Development of New Therapeutics and by Dagmar Ringe, Steven C. Almo, Gregory K. Farber, Janos

By Dagmar Ringe, Steven C. Almo, Gregory K. Farber, Janos Hajdu, P. Lynne Howell (auth.), Jerry B. Hook, George Poste, Judy Schatz (eds.)

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Both pH- and temperature-jump triggering require that the crystal survive the change in environment. -cases. Metal atom triggering represents a good alternative when a metalloenzyme is being studied. Many metalloenzymes require a loosely held metal (Mg is common) for catalysis, but still bind their substrates tightly. In these cases, the crystal of the apoprotein can be loaded with substrate and then mother liquor containing the catalytic metal can be flowed in to initiate the reaction. Metal ions diffuse through protein crystals in seconds and make very good chemical triggers.

Acharya, K. , Stuart, D. , and Johnson, L. , 1988, Catalysis in enzyme crystals, Trends Biochem. Sci. 13:104-109. Kantrowitz, E. , and Lipscomb, W. , 1988, E. coli aspartate transcarbamylase: The relation between structure and function, Science 241:669-674. , and McCammon, J. , 1983, Dynamics of proteins: Elements and functions, Annu. Rev. Biochem. 52:263-300. , and Fink, A. , 1977, Reactivity and cryoenzymology of enzymes in the crystalline state, Annu. Rev. Biophys. Bioeng. 6:301-342. , Szebenyi, D.

An alternative is to cripple the enzyme by site-directed mutagenesis. Protein engineering of improved enzymes has proven a difficult goal to achieve, but most molecular biologists have had no trouble producing mutant enzymes with reduced catalytic activity! In many cases, this reduction is substantial-three or four orders of magnitude in rate. 1 sec for the wild-type enzyme, but 600 sec for an active-site mutant, then crystals of the mutant are suitable for time-resolved study of the reaction by Laue diffraction.

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