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Titolo:
CLONING AND SEQUENCING OF THE GENE ENCODING A NOVEL LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN) IN PORPHYROMONAS-GINGIVALIS - STRUCTURAL RELATIONSHIP WITH THE ARGININE-SPECIFIC CYSTEINE PROTEINASE (ARG-GINGIPAIN)
Autore:
OKAMOTO K; KADOWAKI T; NAKAYAMA K; YAMAMOTO K;
Indirizzi:
KYUSHU UNIV,FAC DENT,DEPT PHARMACOL,HIGASHI KU FUKUOKA 81282 JAPAN KYUSHU UNIV,FAC DENT,DEPT PHARMACOL,HIGASHI KU FUKUOKA 81282 JAPAN KYUSHU UNIV,FAC DENT,DEPT MICROBIOL,HIGASHI KU FUKUOKA 81282 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 2, volume: 120, anno: 1996,
pagine: 398 - 406
SICI:
0021-924X(1996)120:2<398:CASOTG>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; TRYPSIN-LIKE PROTEASE; COLLAGENOLYTIC ACTIVITY; CULTURE SUPERNATANT; ESCHERICHIA-COLI; OUTER-MEMBRANE; PURIFICATION; DEGRADATION; COMPLEMENT; STRAINS;
Keywords:
ARG-GINGIPAIN; LYS-GINGIPAIN; LYSINE-SPECIFIC CYSTEINE PROTEINASE; PORPHYROMONAS GINGIVALIS; PRECURSOR STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
K. Okamoto et al., "CLONING AND SEQUENCING OF THE GENE ENCODING A NOVEL LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN) IN PORPHYROMONAS-GINGIVALIS - STRUCTURAL RELATIONSHIP WITH THE ARGININE-SPECIFIC CYSTEINE PROTEINASE (ARG-GINGIPAIN)", Journal of Biochemistry, 120(2), 1996, pp. 398-406

Abstract

Lys-gingipain (KGP), so termed due to its peptide cleavage specificity for lysine residues, is a cysteine proteinase produced by the Gram-negative anaerobic bacterium Porphyromonas gingivalis. Mixed oligonucleotide primers designed from the NH2-terminal sequence of the purified enzyme mere used to clone the RGP-encoding gene (kgp) from the organism. The nucleotide sequence of kgp had a 5,169-bp open reading frame encoding 1,723 amino acids with a calculated molecular mass of 218 kDa. As the extracellular mature enzyme had an apparent molecular mass of 51 kDa in gels, the precursor of KGP was found to comprise at least four domains, the signal peptide, the NH2-terminal prodomain, the mature proteinase domain, and the COOH-terminal hemagglutinin domain, and to be proteolytically processed during its transport. Importantly, the COOH-terminal region contained three direct repeats of two different amino acid sequences, LKWD(or E)AP and YTYTVYRDGTKI, and the subdomains located between the two repeats exhibited strong similarity to those ofArg-ginspain (RGP), another major cysteine proteinase produced by theorganism and having cleavage specificity for arginine residues, although the arrangement of the subdomains was not necessarily identical inthe two enzymes. Since the RGP activity was greatly decreased in RGP-deficient mutants and since the most probable site of the propeptide cleavage was present in the homologous sequence highly susceptible to proteolysis by RGP, the precursor of KGP is likely to be processed by RGP to form the mature enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:58:12