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Titolo:
Structure-function relationships of beta-D-glucan endo- and exohydrolases from higher plants
Autore:
Hrmova, M; Fincher, GB;
Indirizzi:
Univ Adelaide, Dept Plant Sci, Glen Osmond, SA 5064, Australia Univ Adelaide Glen Osmond SA Australia 5064 en Osmond, SA 5064, Australia
Titolo Testata:
PLANT MOLECULAR BIOLOGY
fascicolo: 1-2, volume: 47, anno: 2001,
pagine: 73 - 91
SICI:
0167-4412(2001)47:1-2<73:SROBEA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
BARLEY HORDEUM-VULGARE; WALL-BOUND EXO-1,3-BETA-D-GLUCANASE; SITE-DIRECTED INHIBITION; CATALYTIC AMINO-ACIDS; CELL-WALL; ACTIVE-SITE; GLYCOSYL HYDROLASES; SUBSTRATE-BINDING; 1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASES; 3-DIMENSIONAL STRUCTURES;
Keywords:
catalytic mechanism; cell wall hydrolysis; monocotyledons; protein modelling; substrate binding; subsite mapping;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
105
Recensione:
Indirizzi per estratti:
Indirizzo: Fincher, GB Univ Adelaide, Dept Plant Sci, Waite Campus, Glen Osmond, SA 5064, Australia Univ Adelaide Waite Campus Glen Osmond SA Australia 5064 ralia
Citazione:
M. Hrmova e G.B. Fincher, "Structure-function relationships of beta-D-glucan endo- and exohydrolases from higher plants", PLANT MOL B, 47(1-2), 2001, pp. 73-91

Abstract

(1 -->3),(1 -->4)-beta -D-Glucans represent an important component of cellwalls in the Poaceae family of higher plants. A number of glycoside endo- and exohydrolases is required for the depolymerization of (1 -->3),(1 -->4)-beta -D-glucans in germinated grain or for the partial hydrolysis of the polysaccharide in elongating vegetative tissues. The enzymes include (1 -->3),(1 -->4)-beta -D-glucan endohydrolases (EC 3.2.1.73), which are classified as family 17 glycoside hydrolases, (1 -->4)-beta -D-glucan glucohydrolases (family 1) and beta -D-glucan exohydrolases (family 3). Kinetic analyses of hydrolytic reactions enable the definition of action patterns, the thermodynamics of substrate binding, and the construction of subsite maps. Mechanism-based inhibitors and substrate analogues have been used to study the spatial orientation of the substrate in the active sites of the enzymes, at the atomic level. The inhibitors and substrate analogues also allow us to define the catalytic mechanisms of the enzymes and to identify catalytic amino acid residues. Three-dimensional structures of (1 -->3),(1 -->4)-beta -D-glucan endohydrolases, (1 -->4)-beta -D-glucan glucohydrolases and beta -D-glucan exohydrolases are available or can be reliably modelled from the crystal structures of related enzymes. Substrate analogues have been diffusedinto crystals for solving of the three-dimensional structures of enzyme-substrate complexes. This information provides valuable insights into potential biological roles of the enzymes in the degradation of the barley (1 -->3),(1 -->4)-beta -D-glucans during endosperm mobilization and in cell elongation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/08/20 alle ore 04:56:27