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beta amylase/pomme de terre
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Dose- and tissue-specific interaction of monoterpenes with the gibberellin-mediated release of potato tuber bud dormancy, sprout growth and induction of α-amylases and β-amylases.
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Gibberellins (GA) are involved in bud dormancy release in several species. We show here that GA-treatment released bud dormancy, initiated bud sprouting and promoted sprout growth of excised potato tuber bud discs ('eyes'). Monoterpenes from peppermint oil (PMO) and S-(+)-carvone (CAR) interact with
A nuclear factor that binds to a dyad-symmetric sequence with a CGTCA motif in the 5'-upstream region of the sweet potato beta-amylase gene.
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A nuclear extract from petioles of sweet potato protected several sites in the 5'-upstream region of a gene for beta-amylase from DNase I digestion. One of these sites, located at a region around 800-base pairs upstream from the transcription start site, having an imperfect palindromic sequence of
A nuclear gene encoding beta-amylase of sweet potato.
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A nuclear AmyB gene from sweet potato encoding beta-amylase (beta Amy) that is abundant in tuberous roots and inducible in other organs by an exogenous supply of sucrose or polygalacturonic acid, was isolated and characterized. Genomic Southern blot hybridization, restriction maps of independently
Chemical Modification of Sweet Potato β-amylase by Mal-mPEG to Improve Its Enzymatic Characteristics.
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The sweet potato β-amylase (SPA) was modified by 6 types of methoxy polyethylene glycol to enhance its specific activity and thermal stability. The aims of the study were to select the optimum modifier, optimize the modification parameters, and further investigate the characterization of the
A new method for the preparation of beta-amylase from sweet potato.
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A simple method for the preparation of sweet potato beta-amylase by thymol amylose adsorption is described. The method is far more efficient and gives higher recovery of the enzyme. The crystalline enzyme thus obtained is found to be homogeneous by gel chromatography, polyacrylamide gel
Preliminary crystallographic analysis of sweet potato beta amylase.
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Beta amylase from sweet potato has been crystallized in a form suitable for high resolution X-ray diffraction analysis from a mixture of polyethylene glycol 400 and ammonium sulfate at room temperature. The crystals are rectangular prisms and occasionally reach a size of 1 mm on an edge. The space
Unexpected mode of action of sweet potato β-amylase on maltooligomer substrates.
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β-Amylase (EC 3.2.1.2), one of the main protein of the sweet potato, is an exo-working enzyme catalyzing the hydrolysis of α(1,4) glycosidic linkages in polysaccharides and removes successively maltose units from the non-reducing ends. The enzyme belongs to glycoside hydrolase GH14 family and
Induction of Expression of Genes Coding for Sporamin and beta-Amylase by Polygalacturonic Acid in Leaf-Petiole Cuttings of Sweet Potato.
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Sporamin and beta-amylase are two major proteins of tuberous storage root of sweet potato (Ipomoea batatas) and their accumulation can be induced concomitantly with the accumulation of starch in leaves and petioles by sucrose (K Nakamura, M Ohto, N Yoshida, K Nakamura [1991] Plant Physiol 96:
Hydrolysis of aryl beta-maltotriosides by sweet potato beta-amylase and soybean beta-amylase.
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Sweet potato beta-amylase [EC 3.2.1.2, alpha 1,4-D-glucan maltohydrolase]-catalyzed hydrolyses of aryl beta-maltotriosides with substituents, NO2-, Cl-, and Br- at the o-, m-, and p-positions in the phenyl ring were studied at pH 4.8 and 25 degrees C. The hydrolyses of a few of the maltotriosides by
Sweet potato beta-amylase. Primary structure and identification of the active-site glutamyl residue.
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The complete amino acid sequence of a subunit of sweet potato beta-amylase, a homotetramer, was established by sequence analysis of peptides obtained by digestions with Achromobacter protease I and Staphylococcus aureus V8 protease and by cyanogen bromide cleavage of the S-carboxymethylated subunit.
Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato beta-amylase.
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Tuberous roots of the sweet potato are unusually rich in beta-amylase, and the beta-amylase polypeptides account for about 5% of the total soluble protein of the organ. Unlike beta-amylases from other origins, the sweet potato beta-amylase is a tetramer of identical subunits, and it also bears
Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato.
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Sweet potato beta-amylase is a tetramer of identical subunits, which are arranged to exhibit 222 molecular symmetry. Its subunit consists of 498 amino acid residues (Mr 55,880). It has been crystallized at room temperature using polyethylene glycol 1500 as precipitant. The crystals, growing to
Sucrose-Induced Accumulation of beta-Amylase Occurs Concomitant with the Accumulation of Starch and Sporamin in Leaf-Petiole Cuttings of Sweet Potato.
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beta-Amylase of sweet potato (Ipomoea batatas L.), which constitutes about 5% of the total soluble protein of the tuberous root, is absent or is present in only small amounts in organs other than the tuberous roots of the normal, field-grown plants. However, when leaf-petiole cuttings from such
A [beta]-Amylase in Potato Tubers Is Induced by Storage at Low Temperature.
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A new starch-degrading enzyme activity is induced by storage of potato (Solanum tuberosum L.) tubers at low temperatures (L. Hill, R. Reimholz, R. Schroder, T.H. Nielsen, M. Stitt [1996] Plant Cell Environ 14: 1223-1237). The cold-induced activity was separated from other amylolytic activities in
Sugar-responsible elements in the promoter of a gene for beta-amylase of sweet potato.
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Expression of genes coding for sporamin and beta-amylase, the two most abundant proteins in storage roots of sweet potato, is coordinately inducible in atypical vegetative tissues by sugars. A sweet potato gene for beta-amylase (beta-Amy) with introns as well as a beta-Amy::GUS fusion gene composed
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