Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin.

作者：T.L. Poulos, Richard A. Alden, Stephan T. Freer, Jens J. Birktoft, Joseph Kraut · 发表于：Journal of Biological Chemistry · 年份：1976 · DOI：10.1016/s0021-9258(17)33806-1 · 被引用次数：114 · 研究领域：Peptidase Inhibition and Analysis、Enzyme Structure and Function、Enzyme Production and Characterization

1. A detailed study of cytochrome C oxidse activity with Keilin-Hartree particles and purified beef heart enzyme, at low ionic strength and low cytochrome C concentrations, showed biphasic kinetics with apparent Km1 = 5 x 10(-8) M, and apparent Km2 = 0.35 to 1.0 x 10(-6) M. Direct binding studies with purified oxidase, phospholipid-containing as well as phospholipid-depleted, demonstrated two sites of interaction of cytochrome c with the enzyme, with KD2 less than or equal to 10(-7) M, and KD2 = 10(-6) M. 2...