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Titolo:
Hydrolysis of glycine-containing elastin pentapeptides by LasA, a metalloelastase from Pseudomonas aeroginosa
Autore:
Vessillier, S; Delolme, F; Bernillon, J; Saulnier, J; Wallach, J;
Indirizzi:
Univ Lyon 1, Lab Biochim Analyt & Synth Bioorgan, UFR Chim Biochim, F-69622 Villeurbanne, France Univ Lyon 1 Villeurbanne France F-69622 im, F-69622 Villeurbanne, France CNRS, Serv Cent Anal, F-69390 Vernaison, France CNRS Vernaison France F-69390 Serv Cent Anal, F-69390 Vernaison, France
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 4, volume: 268, anno: 2001,
pagine: 1049 - 1057
SICI:
0014-2956(200102)268:4<1049:HOGEPB>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONDUCTIMETRIC ASSAY; AERUGINOSA LASA; PROTEASE; SPECIFICITY; SEQUENCE; PURIFICATION; PEPTIDES; STRAINS;
Keywords:
elastin; hydrolysis; LasA protease, peptides; Pseudomonas aeruginosa;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Wallach, J Univ Lyon 1, Lab Biochim Analyt & Synth Bioorgan, UFR Chim Biochim, Bat 303,43 Blvd 11 Novembre 1918,EA 1659, F-69622 Villeurbanne, FranceUniv Lyon 1 Bat 303,43 Blvd 11 Novembre 1918,EA 1659 Villeurbanne France F-69622
Citazione:
S. Vessillier et al., "Hydrolysis of glycine-containing elastin pentapeptides by LasA, a metalloelastase from Pseudomonas aeroginosa", EUR J BIOCH, 268(4), 2001, pp. 1049-1057

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen that causes severe infections in vulnerable hosts. It may produce various virulence factors including proteases. Among them, LasA possesses both elastolytic and staphylolytic (hydrolysis of pentaglycine cross-links in the cell wall peptidoglycan) activities. To understand if its elastolytic activity results from a preference for glycine-rich substrates, we studied its ability to hydrolyse the 65 pentapeptides of human tropoelastin containing at least three glycines. As demonstrated by capillary electrophoresis (CE), 22 of these peptides werehydrolysed by LasA, generally at a single peptide bond and the catalytic ratio k(cat)/K-M was determined for most of them. The highest value was obtained for LGGGA, 59 +/- 9 min(-1).mmol(-1).L. The specificity of hydrolysis was elucidated by CE, liquid secondary ion mass spectrometry and, in some cases, collision activated dissociation-mass analysis of ion kinetic energy. The preferred cleavage sites are GG and GA peptide bonds, the sequence GGIA being especially sensitive to hydrolysis. Both positions P-2 and P'(2) must be occupied for hydrolysis and the presence of an amino acid in P-3 (butnot in P'(3)) significantly increases the catalytic ratio. Considering these results, about 30 GGX sequences (X: G, A or Y) of human tropoelastin could be susceptible to LasA elastolysis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:44:31