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Titolo:
Plant chitinase/lysozyme isoforms show distinct substrate specificity and cleavage site preference towards lipochitooligosaccharide Nod signals
Autore:
Schultze, M; Staehelin, C; Brunner, F; Genetet, I; Legrand, M; Fritig, B; Kondorosi, E; Kondorosi, A;
Indirizzi:
CNRS, Inst Sci Vegetales, F-91198 Gif Sur Yvette, France CNRS Gif Sur Yvette France F-91198 tales, F-91198 Gif Sur Yvette, France CNRS, Inst Biol Mol Plantes, F-67084 Strasbourg, France CNRS Strasbourg France F-67084 l Mol Plantes, F-67084 Strasbourg, France Hungarian Acad Sci, Biol Res Ctr, H-6701 Szeged, Hungary Hungarian Acad Sci Szeged Hungary H-6701 Res Ctr, H-6701 Szeged, Hungary
Titolo Testata:
PLANT JOURNAL
fascicolo: 5, volume: 16, anno: 1998,
pagine: 571 - 580
SICI:
0960-7412(199812)16:5<571:PCISDS>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PATHOGENESIS-RELATED PROTEINS; ACID-SEQUENCE SIMILARITIES; SOMATIC EMBRYO MUTANT; RHIZOBIUM-MELILOTI; TRANSGENIC TOBACCO; NODULATION FACTORS; OLIGOSACCHARIDE SIGNAL; NICOTIANA-SYLVESTRIS; ANTIFUNGAL ACTIVITY; RHIZOCTONIA-SOLANI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Schultze, M CNRS, Inst Sci Vegetales, Ave Terrasse, F-91198 Gif Sur Yvette, France CNRS Ave Terrasse Gif Sur Yvette France F-91198 vette, France
Citazione:
M. Schultze et al., "Plant chitinase/lysozyme isoforms show distinct substrate specificity and cleavage site preference towards lipochitooligosaccharide Nod signals", PLANT J, 16(5), 1998, pp. 571-580

Abstract

The ability of 16 chitinases from seven different plant species to hydrolyze a collection of several structurally related lipochitooligosaccharides (LCOs) of Rhizobium was analyzed. It was found that the enzymes differed to a large extent in their activity on different LCOs. Differences were attributed to (i) the relative activity on different LCOs as substrate (e.g, sulfated versus non-sulfated LCOs); (ii) the relative cleavage site preference on a given LCO molecule (hydrolysis of either the second, third or fourth glycosidic bond from the non-reducing end of the molecule); and (iii) the stereochemistry of the reaction (retention or inversion of the anomeric configuration). A graphic representation of the different substrate specificities resulted in a 'fingerprint' that is characteristic for a given enzyme or a family of related enzymes. By comparing the LCO-fingerprint of unknown enzymes with those obtained for already characterized proteins, it is possible to identify new glycosyl hydrolases. The high diversity of substrate specificity found among plant chitinases may reflect variations in the natural substrates of the enzymes, such as substitutions on the chitin moiety of fungal cell walls or, in plants, the presence of putative endogenous substrates related to LCOs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 16:30:21