Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: differences in beta-glucan binding withinfamily CBM4
Autore:
Zverlov, VV; Volkov, IY; Velikodvorskaya, GA; Schwarz, WH;
Indirizzi:
Tech Univ Munich, Res Grp Microbial Biotechnol, D-85350 Freising, Germany Tech Univ Munich Freising Germany D-85350 nol, D-85350 Freising, Germany Russian Acad Sci, Inst Mol Genet, Moscow 123182, Russia Russian Acad Sci Moscow Russia 123182 t Mol Genet, Moscow 123182, Russia
Titolo Testata:
MICROBIOLOGY-UK
, volume: 147, anno: 2001,
parte:, 3
pagine: 621 - 629
SICI:
1350-0872(200103)147:<621:TBPOTC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELLULOMONAS-FIMI CENC; THERMOSTABILIZING DOMAIN; RHODOTHERMUS-MARINUS; XYLANASE; ENZYMES; POLYSACCHARIDES; PURIFICATION; SPECTROSCOPY; DEGRADATION; EXPRESSION;
Keywords:
Thermotoga neapolitana; 1,3-beta-glucanase; substrate-binding module CBM4; binding specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Schwarz, WH Tech Univ Munich, Res Grp Microbial Biotechnol, Hochanger 4, D-85350 Freising, Germany Tech Univ Munich Hochanger 4 Freising Germany D-85350 Germany
Citazione:
V.V. Zverlov et al., "The binding pattern of two carbohydrate-binding modules of laminarinase Lam16A from Thermotoga neapolitana: differences in beta-glucan binding withinfamily CBM4", MICROBIO-UK, 147, 2001, pp. 621-629

Abstract

Carbohydrate-binding modules (CBMs) are often part of the complex hydrolytic extracellular enzymes from bacteria and may modulate their catalytic activity. The thermostable catalytic domain of laminarinase Lam16A from Thermotoga neapolitana (glycosyl hydrolase family 16) is flanked lay two CBMs, 148 and 161 aa long. They share a sequence identity of 30%, are homologous tofamily CBM4 and are thus called CBM4-1 and CBM4-2 respectively. Recombinant Lam16A proteins deleted for one or both binding modules and the isolated module CBM4-1 were characterized. Proteins containing the N-terminal moduleCBM4-1 bound to the soluble polysaccharides laminarin (1,3-beta -glucan) and barley 1,3/1,4-beta -glucan, and proteins containing the C-terminal module CBM4-2 bound additionally to curdlan (1,3-beta -glucan) and pustulan (1,6-beta -glucan), and to insoluble yeast cell wall P-glucan. The activity ofthe catalytic domain on soluble 1,3-beta -glucans was stimulated by the presence of CBM4-1, whereas the presence of CBM4-2 enhanced the Lam16A activity towards gelatinized and insoluble or mixed-linkage 1,3-beta -glucan. Thermostability of the catalytic domain was not affected by the truncations. Members of family CBM4 can be divided into four subfamilies, members of which show different polysaccharide-binding specificities corresponding to the catalytic specificities of the associated hydrolytic domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 13:02:22