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By Nathan P. Kaplan, William B. Jakoby, Meir Wilchek

The significantly acclaimed laboratory commonplace, tools in Enzymology, is without doubt one of the such a lot hugely revered guides within the box of biochemistry. seeing that 1955, each one quantity has been eagerly awaited, usually consulted, and praised by means of researchers and reviewers alike. The sequence includes a lot fabric nonetheless proper this present day - actually a necessary booklet for researchers in all fields of lifestyles sciences.

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M. Vratsanos, M. Wasserman, and A. G. Cooper, Biochem. Biophys. Res. Commun. 23, 243 (1966); T. G. Rajogopalan, W. H. Stein, and S. Moore, J. Biol. Chem. 241, 4295 (1966). lJ M. Brockhaus and J. Lehmann, FEBS Lett. 62, 154 (1976). 'ell. Chaimovich, R. J. Vaughan, and F. H. Westheimer, J. Am. Chem. Soe. 90, 4088 (1968) ; J. Sharer, P. Baronowsky, R. Lawsen, F. Finn, and F. H. Westheimer, J. Biol. Chem. 241, 421 (1966). [3] 37 MECHANISM-BASED IRREVERSIBLE INHIBITORS These compounds are thought to function by undergoing elimination reaction with certain enzymes to give rise to reactive Michael acceptors.

D. Lane, and M. C. Scrutton, J. Biol. Chem. 245, 4939 (1970). aa K. D. Collins, J. Biol. Chem. 249, 136 (1974). T. G. Spring and F. Wold, Biochemistry 10, 4655 (1971). cc G. J. Cardinale and R. H. Abeles, Bioehemislry 7, 397 (1968). dd S. Wang, F. S. Kawahara, and P. Talalay, J. Biol. Chem. 238, 576 (1973). ee R. Wolfenden, Biochemistry 9, 3404 (1970). / / J . M. Chirgwin and E. A. Noltmann, Fed. Proc. 32, 667 (1973). gg D. Cassio, F. LeMoine, J. P. Waller, E. Sandrin, and R. A. Boissonas, Biochemistry 6, 827 (1967).

J. Wilson, W. Birchmeier, and P. Christen, Eur. J. Biochem. 41, 471 (1974). < 0 Z ~ o ¢; ~a <'-. ©~,, ~ ~N + ° o o • °~ 44 GENERAL METHODOLOGY ~] enzyme the rate of modification of Cys-390 is at a minimum. The rate increases as the enzyme passes through the consecutive enzyme-substrate intermediates and decreases again when the free pyridoxamine form is reached. The rate of Cys-390 modification is fastest when, in the presence of a substrate pair (glutamate plus 2-ketoglutarate or aspartate plus oxaloacetate), covalent enzyme-substrate intermediates are formed.

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