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alpha glucan/kentang
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Synthesis and kinetic evaluation of 4-deoxymaltopentaose and 4-deoxymaltohexaose as inhibitors of muscle and potato alpha-glucan phosphorylases.
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alpha-Glucan phosphorylases degrade linear or branched oligosaccharides via a glycosyl transfer reaction, occurring with retention of configuration, to generate alpha-glucose-1-phosphate (G1P). We report here the chemoenzymic synthesis of two incompetent oligosaccharide substrate analogues,
Alpha-glucan binding of potato-tuber starch-branching enzyme I as determined by tryptophan fluorescence quenching, affinity electrophoresis and steady-state kinetics.
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The affinity of potato tuber starch-branching enzyme-I (PSBE-I) for various linear malto-oligosaccharides, cyclodextrins, (CDs) and macromolecular alpha-glucans was investigated by alpha-glucan induced fluorescence quenching of intrinsic PSBE-I tryptophan residues and by affinity electrophoresis.
Cumulative effect of amino acid replacements results in enhanced thermostability of potato type L alpha-glucan phosphorylase.
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The thermostability of potato type L alpha-glucan phosphorylase (EC 2.4.1.1) was enhanced by random and site-directed mutagenesis. We obtained three single-residue mutations-Phe39-->Leu (F39L), Asn135-->Ser (N135S), and Thr706-->Ile (T706I)-by random mutagenesis. Although the wild-type enzyme was
Measurement of active-site homology between potato and rabbit muscle alpha-glucan phosphorylases through use of a linear free energy relationship.
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The Michaelis-Menten parameters (Vmax and Km) for turnover of an extensive series of deoxy and deoxyfluoro derivatives of alpha-D-glucopyranosyl phosphate by the alpha-glucan phosphorylase from potato tuber have been determined. Very large rate reductions are observed as a consequence of each
Alpha-glucan phosphorylase from sweet potato: isolation and properties of the partially degraded enzyme.
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Alpha-Glucan phosphorylase (EC 2.4.1.1.) was purified from sweet potato roots. Apparently homogeneous preparations obtained are partially degraded products from phosphorylase, as judged from the results of molecular weight determination, NH-2-termini analysis and pyridoxal-5'-P assay. Phosphorylase
Photooxidation of alpha-glucan phosphorylases from rabbit muscle and potato tubers.
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Photooxidation of alpha-glucan phosphorylases from rabbit muscle and potato tubers in the presence of rose bengal leads to a rapid loss of enzymatic activity which follows first-order kinetics. The process is pH dependent, being more rapid at higher pH. The inactivation is closely related to the
High expression of a synthetic gene encoding potato alpha-glucan phosphorylase in Aspergillus niger.
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We describe the successful heterologous expression of the Solanum tuberosum alpha-glucan phosphorylase (GP) gene in Aspergillus niger. Special attention was paid to the influence of different codon usage and A+T content in the coding region on GP protein expression. Use of A. niger-preferred codon
Functional domain organization of the potato alpha-glucan, water dikinase (GWD): evidence for separate site catalysis as revealed by limited proteolysis and deletion mutants.
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The potato tuber (Solanum tuberosum) GWD (alpha-glucan, water dikinase) catalyses the phosphorylation of starch by a dikinase-type reaction mechanism in which the beta-phosphate of ATP is transferred to the glucosyl residue of amylopectin. GWD shows sequence similarity to bacterial pyruvate, water
Biocatalytic role of potato starch synthase III for α-glucan biosynthesis in Synechocystis sp. PCC6803 mutants.
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A potato starch synthase III (PSSIII) was expressed in the Synechocystis mutants deficient in either glycogen synthase I (M1) or II (M2) to replenish α-(1,4) linkage synthesizing activity, resulting in new mutants, PM1 and PM2, respectively. These mutants were applied to study the role of exogenous
The complete amino acid sequence of potato alpha-glucan phosphorylase.
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The complete amino acid sequence of potato alpha-glucan phosphorylase has been determined. The monomer contains 916 amino acids with a molecular weight of 103,916. About one-fourth of the amino-terminal threonine is blocked by an acetyl group. Sequence comparison among phosphorylases from potato
Molecular cloning of cDNA encoding potato amyloplast alpha-glucan phosphorylase and the structure of its transit peptide.
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The type L isozyme of potato tuber alpha-glucan phosphorylase [EC 2.4.1.1], a dimer of 104-kDa subunits, is compartmentalized in the amyloplast. We have cloned a nearly full-length cDNA encoding this isozyme from a cDNA library of immature potato tuber. The sequence was supplemented by a partial
Affinity of glucose analogs for alpha-glucan phosphorylases from rabbit muscle and potato tubers.
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The action of phosphorylase b from rabbit muscle and potato phosphorylase was inhibited to various extents by several glucose analogs. Like glucose itself, all of the glucosidic oxygen-substituted analogs tested in kinetic experiments showed a nonlinear competitive inhibition for muscle
Pyridoxal 5'-phosphate in alpha-glucan phosphorylase from the potato.
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Potato alpha-glucan phosphorylase: crystallization, amino acid composition and enzymatic reaction in the absence of added primer.
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The subunit structure of alpha-glucan phosphorylase from potato.
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