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Titolo:
Alteration of rat dipeptidyl peptidase III by site-directed mutagenesis: Cysteine(176) is a regulatory residue for the enzyme activity
Autore:
Li, YH; Maeda, T; Yamane, T; Ohkubo, I;
Indirizzi:
Shiga Univ Med Sci, Dept Med Biochem, Otsu, Shiga 5202192, Japan Shiga Univ Med Sci Otsu Shiga Japan 5202192 m, Otsu, Shiga 5202192, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 276, anno: 2000,
pagine: 553 - 558
SICI:
0006-291X(20000924)276:2<553:AORDPI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUINEA-PIG BRAIN; AMINOPEPTIDASE-III; PURIFICATION;
Keywords:
dipeptidyl peptidase III; expression; mutagenesis; rat liver;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Ohkubo, I Shiga Univ Med Sci, Dept Med Biochem, Otsu, Shiga 5202192, JapanShiga Univ Med Sci Otsu Shiga Japan 5202192 higa 5202192, Japan
Citazione:
Y.H. Li et al., "Alteration of rat dipeptidyl peptidase III by site-directed mutagenesis: Cysteine(176) is a regulatory residue for the enzyme activity", BIOC BIOP R, 276(2), 2000, pp. 553-558

Abstract

To comprehend the importance of cysteine residues for the regulation of enzyme activity, me replaced each of seven cysteine residues in rat dipeptidyl peptidase III cDNA with alanine, glycine, or glutamic acid residue using site-directed mutagenesis. Each mutated cDNA was expressed in E. coli (BL21), and each expressed DPP III was purified to apparent homogeneity on SDS-polyacrylamide gel electrophoresis. Six of the mutant proteins had similar activity to that of the wild-type enzyme, whereas the activity of the Cys(176) --> Ala mutant enzyme was only 25-35% of that of the wild-type enzyme activity. This mutant enzyme was resistant against both PCMB and NEM. Furthermore, both Cys(176) --> Gly and Cys(176) --> Glu mutated enzymes showed no DPP LII activity. These seven mutated enzymes contained significant amountsof zinc, as determined by atomic absorption spectrometry. The results indicate that Cys(176) is essential for the regulation of DPP III activity. (C)2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 09:54:06