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.
J Biol Chem
; 251(4): 1097-103, 1976 Feb 25.
Article
en En
| MEDLINE
| ID: mdl-1249069
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...
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Subtilisinas
/
Cetonas
Idioma:
En
Revista:
J Biol Chem
Año:
1976
Tipo del documento:
Article