Prolyl oligopeptidase catalysis Reactions with thiono substrates reveal substrate-induced conformational change to be the rate-limiting step

Prolyl oligopeptidase, a member of the new family of serine proteases, exhibits significant mechanistic differences compared with the enzymes of the chymotrypsin and subtilisin families. Our kinetic study using the thiono substrate, benzyloxycarbonyl-Gly-Pro[CS-NH]-2-naphthylamide suggests that the...

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Veröffentlicht in:	FEBS letters 1993-05, Vol.322 (3), p.227-230
Hauptverfasser:	Polgár, László, Kollát, Emma, Hollósi, Miklós
Format:	Artikel
Sprache:	eng
Schlagworte:	2-naphthylamide Animals benzyloxycarbonyl Binding Sites Boc Conformational change dithioerythritol DTE Enzyme mechanism Glyt and Prot Hydrogen Bonding Hydrogen-Ion Concentration Kinetics Nap Oxygen - metabolism Protein Conformation Rate-limiting step represent Gly and Pro, respectively, containing a sulfur atom in place of the carbonyl oxygen Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Subsite specificity Substrate Specificity Swine t-butyloxycarbonyl Thiones - metabolism Thiono substrate
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