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Titolo:
Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase
Autore:
Banbula, A; Yen, J; Oleksy, A; Mak, P; Bugno, M; Travis, J; Potempa, J;
Indirizzi:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 Biochem & Mol Biol, Athens, GA 30602 USA Jagiellonian Univ, Inst Mol Biol, PL-34120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-34120 l Biol, PL-34120 Krakow, Poland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 9, volume: 276, anno: 2001,
pagine: 6299 - 6305
SICI:
0021-9258(20010302)276:9<6299:PGDRAN>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEQUENCE-ANALYSIS; BIOCHEMICAL-CHARACTERIZATION; BACTEROIDES-GINGIVALIS; GEL-ELECTROPHORESIS; PROTEASE GENE; PEPTIDASE-IV; PURIFICATION; PROTEINS; COLLAGENASE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Potempa, J Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA Univ Georgia Athens GA USA 30602 ol Biol, Athens, GA 30602 USA
Citazione:
A. Banbula et al., "Porphyromonas gingivalis DPP-7 represents a novel type of dipeptidylpeptidase", J BIOL CHEM, 276(9), 2001, pp. 6299-6305

Abstract

A novel dipeptidylpeptidase (DPP-7) was purified from the membrane fraction of Porphyromonas gingivalis. This enzyme, with an apparent molecular massof 76 kDa, has the specificity for both aliphatic and aromatic residues inthe P1 position. Although it belongs to the serine class of peptidases, itdoes not resemble other known dipeptidylpeptidases. Interestingly, the amino acid sequence around the putative active site serine residue shows significant similarity to the C-terminal region of the Staphylococcus aureus V-8endopeptidase. The genes encoding homologues of DPP-7 were found in genomes of Xylella fastidiosa, Shewanella putrefaciens, and P. gingivalis. It is likely that at least in P. gingivalis, DPP-7 and its homologue, in concert with other di- and tripeptidases, serve nutritional functions by providing dipeptides to this asaccharolytic bacterium.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:44:21