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Titolo:
The action of starch synthase II on 6 '''-alpha-maltotriosyl-maltohexaose comprising the branch point of amylopectin
Autore:
Damager, T; Denyer, K; Motawia, MS; Moller, BL; Blennow, A;
Indirizzi:
Royal Vet & Agr Univ, Ctr Mol Plant Physiol PLaCe, Copenhagen, Denmark Royal Vet & Agr Univ Copenhagen Denmark siol PLaCe, Copenhagen, Denmark Royal Vet & Agr Univ, Dept Plant Biol, Copenhagen, Denmark Royal Vet & AgrUniv Copenhagen Denmark Plant Biol, Copenhagen, Denmark John Innes Ctr Plant Sci Res, Norwich NR4 7UH, Norfolk, England John InnesCtr Plant Sci Res Norwich Norfolk England NR4 7UH olk, England
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 18, volume: 268, anno: 2001,
pagine: 4878 - 4884
SICI:
0014-2956(200109)268:18<4878:TAOSSI>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PISUM-SATIVUM L; BETA-AMYLASE; WAXY MAIZE; GRANULE; BIOSYNTHESIS; BIOGENESIS; POTATO; TUBERS;
Keywords:
starch biosynthesis; starch synthase II; synthetic oligosaccharides; primer specificity; glucosyl transferase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Blennow, A Royal Vet & Agr Univ, Dept Plant Biol, Plant Biochem Lab, 40 Thorvaldsensvej, DK-1871 Frederiksberg C, Denmark Royal Vet & Agr Univ 40 Thorvaldsensvej Frederiksberg Denmark C
Citazione:
T. Damager et al., "The action of starch synthase II on 6 '''-alpha-maltotriosyl-maltohexaose comprising the branch point of amylopectin", EUR J BIOCH, 268(18), 2001, pp. 4878-4884

Abstract

The principle of using a chemically synthesized, well-defined branched oligosaccharide to provide a more detailed knowledge of the substrate specificity of starch synthase II (SSII) is demonstrated. The branched nonasaccharide, 6"'-alpha -maltotriosyl-maltohexaose, was investigated as a primer for particulate SSII using starch granules prepared from the low-amylose pea mutant lam as the enzyme source. The starch granule preparation from the lam pea mutant contains no starch synthases other than SSII and is devoid of alpha -amylase, beta -amylase and phosphorylase activity. SSII was demonstrated to catalyse a specific nonprocessive elongation of the nonreducing end of the shortest unit chain of 6"'-alpha -maltotriosyl-maltohexaose, i.e. themaltotriose chain. Maltotriose and maltohexaose, representing the two linear building units of the branched nonasaccharide, were also tested as primers for SSII. Maltotriose was elongated more efficiently than 6"'-alpha -maltotriosyl-maltohexaose and maltohexaose was used less efficiently. Comparedto the surface exposed alpha -glucan chains of the granule bound amylopectin molecules, all three soluble oligosaccharides tested were poor primers for SSII. This indicates that in vivo, the soluble oligosaccharides supposedly released as result of amylopectin trimming reactions are not re-introduced into starch biosynthetic reactions via the action of the granule bound fraction of SSII.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 13:35:00