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Titolo:
DISTINCTIVE CATALYTIC ACTIONS OF CARP DIPEPTIDASES FROM ORDINARY MUSCLE AND INTESTINE
Autore:
ARANISHI F; WATANABE T; OSATOMI K; CAO M; HARA K; ISHIHARA T;
Indirizzi:
NATL RES INST FISHERIES SCI YOKOHAMA KANAGAWA 236 JAPAN NAGASAKI UNIV,FAC FISHERIES NAGASAKI 852 JAPAN NAGASAKI UNIV,GRAD SCH MARINE SCI & ENGN NAGASAKI 852 JAPAN
Titolo Testata:
Journal of marine biotechnology
fascicolo: 3, volume: 6, anno: 1998,
pagine: 157 - 162
SICI:
0941-2905(1998)6:3<157:DCAOCD>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN RENAL DIPEPTIDASE; PROTEIN DIGESTION; PURIFICATION; GLUTATHIONE; INHIBITION; ABSORPTION; HYDROLYSIS; PEPTIDASES; ENZYMES; ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
F. Aranishi et al., "DISTINCTIVE CATALYTIC ACTIONS OF CARP DIPEPTIDASES FROM ORDINARY MUSCLE AND INTESTINE", Journal of marine biotechnology, 6(3), 1998, pp. 157-162

Abstract

Although carp muscular and intestinal dipeptidases are metalloenzymesacting only on dipeptides, some structural and enzymatic differences occur between them. The present study verifies distinctive actions during dipeptide hydrolysis by these enzymes in terms of their kinetic characterization. The intestinal enzyme was differentially inhibited by EDTA and 1,10-phenanthroline, whereas these compounds induced a similar level inhibition of the muscular kenzyme. The K-m and V-max values of both enzymes for L-leucine-glycine hydrolysis varied during incubations with 1,10-phenanthroline and EDTA, and the K-m or V-max values of the intestinal enzyme increased or remained the same with increasing concentrations of 1,10-phenanthroline, respectively. Analysis of the kinetic parameters indicated that Co2+ and Mn2+ had noncompetitive effects on the muscular enzyme and that a noncompetitive activation on the intestinal enzyme was stimulated by 1.5 mM of Mg2+ and with increasingconcentrations of Mn2+ The muscular enzyme acted on a wide range of L-configuration dipeptides, whereas the intestinal enzyme acted only ona select range of dipeptides with a hydrophobic amino acid at the N-terminal position. The K-cat/K-m values of both enzymes for dipeptide hydrolysis showed that highly hydrophobic dipeptides served as their preferential substrates. Other kinetic parameters demonstrated distinctive hydrolytic action of the two enzymes on these dipeptides: a strong affinity of the low catalytic rate muscular enzyme, and a weak affinity of the high catalytic rate intestinal enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 21:29:54