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Titolo:
Prolyl tripeptidyl peptidase from Porphyromonas gingivalis - A novel enzyme with possible pathological implications for the development of periodontitis
Autore:
Banbula, A; Mak, P; Bugno, M; Silberring, J; Dubin, A; Nelson, D; 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-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 l Biol, PL-31120 Krakow, Poland Jagiellonian Univ, Fac Chem, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 c Chem, PL-31120 Krakow, Poland Jagiellonian Univ, Reg Lab, PL-31120 Krakow, Poland Jagiellonian Univ Krakow Poland PL-31120 eg Lab, PL-31120 Krakow, Poland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 14, volume: 274, anno: 1999,
pagine: 9246 - 9252
SICI:
0021-9258(19990402)274:14<9246:PTPFPG>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; CYSTEINE PROTEINASES; GLYCYLPROLYL PROTEASE; ESCHERICHIA-COLI; GENE; PURIFICATION; GENERATION; EXPRESSION; ACTIVATION; GINGIPAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
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., "Prolyl tripeptidyl peptidase from Porphyromonas gingivalis - A novel enzyme with possible pathological implications for the development of periodontitis", J BIOL CHEM, 274(14), 1999, pp. 9246-9252

Abstract

Porphyromonas gingivalis possesses a complex proteolytic system, which is essential for both its growth and evasion of host defense mechanisms, In this report we characterized, both at a protein and genomic level, a novel peptidase of this system with prolyl tripeptidyl peptidase activity. The enzyme was purified to homogeneity, and its enzymatic activity and biochemical properties were investigated The amino acid sequence at the amino terminus and of internal peptide fragments enabled identification of the gene encoding this enzyme, which we refer to as PtpA for prolyl tripeptidyl peptidase A. The gene encodes an 82-kDa protein, which contains a GWSYGG motif, characteristic for members of the S9 prolyl oligopeptidase family of serine proteases. However, it does not share any structural similarity to Other tripeptidyl peptidases, which, belong to the subtilisin family. The production ofprolyl tripeptidyl peptidase may contribute to the pathogenesis of periodontal tissue destruction through the mutual interaction of this enzyme, hostand bacterial collagenases, and, dipeptidyl peptidases in the degradation of collagen during the course of infection.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 04:22:40