PMID: 1249069Feb 25, 1976

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

The Journal of Biological Chemistry
T L PoulosJ Kraut

Abstract

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...

Related Concepts

Beef heart preparation
Plain X-ray
Analog
Oxidase
Ketone Bodies Measurement, Quantitative
Subtilisins
Plasma Protein Binding Capacity
Serine Endopeptidases
Lysine
Fourier Transform

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