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Titolo:
A secreted aminopeptidase of Pseudomonas aeruginosa - Identification, primary structure, and relationship to other aminopeptidases
Autore:
Cahan, R; Axelrad, I; Safrin, M; Ohman, DE; Kessler, E;
Indirizzi:
Tel Aviv Univ, Sackler Fac Med, Sheba Med Ctr, Maurice & Gabriela Goldschleger Eye Res Inst, IL-52621 Tel Hashomer, Israel Tel Aviv Univ Tel Hashomer Israel IL-52621 IL-52621 Tel Hashomer, Israel Virginia Commonwealth Univ, Med Coll Virginia, Richmond, VA 23298 USA Virginia Commonwealth Univ Richmond VA USA 23298 , Richmond, VA 23298 USA McGuire Dept Vet Affairs Med Ctr, Richmond, VA 23249 USA McGuire Dept Vet Affairs Med Ctr Richmond VA USA 23249 mond, VA 23249 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 47, volume: 276, anno: 2001,
pagine: 43645 - 43652
SICI:
0021-9258(20011123)276:47<43645:ASAOPA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
STREPTOMYCES-GRISEUS AMINOPEPTIDASE; AEROMONAS-CAVIAE T-64; INTRAMOLECULAR CHAPERONE; VIBRIO-PROTEOLYTICUS; MOLECULAR-CLONING; ELASTASE ACTIVITY; SENSITIVE METHOD; GENE; PURIFICATION; LASA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Kessler, E Tel Aviv Univ, Sackler Fac Med, Sheba Med Ctr, Maurice & Gabriela Goldschleger Eye Res Inst, IL-52621 Tel Hashomer, Israel Tel Aviv Univ Tel Hashomer Israel IL-52621 l Hashomer, Israel
Citazione:
R. Cahan et al., "A secreted aminopeptidase of Pseudomonas aeruginosa - Identification, primary structure, and relationship to other aminopeptidases", J BIOL CHEM, 276(47), 2001, pp. 43645-43652

Abstract

Using leucine-p-nitroanilide (Leu-pNA) as a substrate, we demonstrated aminopeptidase activity in the culture filtrates of several Pseudomonas aeruginosa strains. The aminopeptidase was partially purified by DEAE-cellulose chromatography and found to be heat stable. The apparent molecular mass of the enzyme was similar to 56 kDa; hence, it was designated AP(56). Heating (70 degreesC) of the partially purified aminopeptidase preparations led to the conversion of AP56 to a similar to 28-kDa protein (AP(28)) that retainedenzyme activity, a reaction that depended on elastase (LasB). The pH optimum for Leu-pNA hydrolysis by AP(28) was 8.5. This activity was inhibited byZn chelators but not by inhibitors of serine- or thiol-proteases, suggesting that AP(28) is a Zn-dependent enzyme. Of several amino acid p-nitroanilide derivatives examined, Leu-pNA was the preferred substrate. The sequencesof the first 20 residues of AP(56), and AP(28) were determined. A search of the P. aeruginosa genomic data base revealed a perfect match of these sequences with positions 39-58 and 273-291, respectively, in a 536-amino acid residue open reading frame predicted to encode an aminopeptidase. A search for sequence similarities with other proteins revealed 52% identity with Streptomyces griseus aminopeptidase, similar to 35% identity with Saccharomyces cerevisiae aminopeptidase Y and a hypothetical aminopeptidase from Bacillus subtilis, and 29-32% with Aeromonas caviae, Vibrio proteolyticus, and Vibrio cholerae aminopeptidases. The residues potentially involved in zinc coordination were conserved in all these proteins. Thus, P. aeruginosa aminopeptidase may belong to the same family (M28) of metalloproteases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 04:37:03