phosphorylase/pòm tè

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A role of phosphorylase in the potato minituber function under altered gravity.

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The goal of our work was a role of phosphorylase (EC. 2.4.1.1) in starch accumulation in plastids of storage parenchyma cells in potato minitubers forming under clinorotation. An increased enzyme activity under the influence of simulated microgravity has been revealed by using the biochemical and

Potato phosphorylase catalyzed synthesis of amylose-lipid complexes.

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On-line size-exclusion chromatography monitoring of potato phosphorylase catalyzed amylose synthesis--starting from alpha-D-glucose-1-P and maltohexaose--revealed rather monodisperse amylose populations. In the presence of lipids, amylose-lipid complexes spontaneously formed and precipitated. They

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,

Structural similarities in the active-site region between potato and rabbit muscle phosphorylases: a lysyl residue located close to the pyridoxal 5'-phosphate.

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P1,P2-bis(5'-pyridoxal)diphosphate crosslinks between the original cofactor (pyridoxal 5'-phosphate) linking residue and Lys-573 in rabbit muscle phosphorylase (Shimomura, S., Nakano, K., & Fukui, T. (1978) Biochem. Biophys. Res. Commun. 82, 462-468). We have applied the same technique to potato

Potato and rabbit muscle phosphorylases: comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes.

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Phosphorylases (EC 2.4.1.1) from potato and rabbit muscle are similar in many of their structural and kinetic properties, despite differences in regulation of their enzyme activity. Rabbit muscle phosphorylase is subject to both allosteric and covalent controls, while potato phosphorylase is an

The starch phosphorylase gene is subjected to different modes of regulation in starch-containing tissues of potato.

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Analysis of the levels of starch phosphorylase mRNA and its product in the various organs of the potato plant indicates that the gene is differentially regulated, leading to a high accumulation of the gene product in tubers. The amount of phosphorylase transcripts synthesized in nuclei isolated from

A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis.

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In potato tubers two starch phosphorylase isozymes, types L and H, have been described and are believed to be responsible for the complete starch breakdown in this tissue. Type L has been localized in amyloplasts, whereas type H is located within the cytosol. In order to investigate whether the same

Amino acid sequence around the pyridoxal 5'-phosphate binding site in potato phosphorylase.

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The amino acid sequence around the pyridoxal 5'-phosphate binding site in potato phosphorylase was determined in order to compare it with those in phosphorylases from other sources having different regulatory properties. The potato enzyme was reduced by NaBH4 in the presence of urea,

Amino acid sequence of cyanogen bromide fragments of potato phosphorylase.

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Amino acid sequence analysis of the cyanogen bromide peptides of potato alpha-glucan phosphorylase was undertaken for comparison with rabbit muscle glycogen phosphorylase and for elucidation of the structural bases for the differences in the catalytic and regulatory properties between the animal and

Actions of Aspergillus oryzae alpha-amylase, potato phosphorylase, and rabbit muscle phosphorylase a and b on phosphorylated (1----4)-alpha-D-glucan.

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Aspergillus oryzae alpha-amylase [(1----4)-alpha-D-glucan glucanohydrolase, EC 3.2.1.1] produced O-(6-phosphoryl-alpha-D-glucopyranosyl)-(1----4)-O-alpha-D-glucopyran osy l-(1----4)-D-glucopyranose (6(3)-phosphorylmaltotriose) and

Inhibition of potato starch phosphorylase by alpha-D-glucopyranose-1,2-cyclic phosphate.

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alpha-D-Glucopyranose-1.2-cyclic phosphate is a potent inhibitor of potato starch phosphorylase-catalyzed (1,4-alpha-D-glucan:orthophosphate alpha-glucosyltransferase, EC 2.4.1.1) starch elongation. The inhibition is competitive with respect to alpha-D-glucopyranose 1-phosphate (Glc-1-P) with Ki

Tissue distribution and change in potato starch phosphorylase mRNA levels in wounded tissue and sprouting tubers.

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Starch phosphorylase has been cloned from a lambda gt10 cDNA library of potato tuber mRNA. Selected recombinants have been used to demonstrate that phosphorylase mRNA is most abundant in tubers but is also detectable in stolon, root, stem and leaf tissue. The level of phosphorylase mRNA was greatly

Biochemical properties of potato phosphorylase change with its intracellular localization as revealed by immunological methods.

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Phosphorylase was purified from young and senescent potato tubers. Antibodies raised against the enzyme from young tubers crossreacted with phosphorylase from old tissue, although the latter exhibited different physico-chemical properties. In polyacrylamide gel electrophoresis it migrated with

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

Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli.

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Higher plant tissues contain two alpha-glucan phosphorylase isozymes (EC 2.4.1.1), types L and H, localized in the plastid and the cytoplasm, respectively. We already isolated and sequenced a cDNA clone encoding the type L isozyme. Presently, a cDNA clone encoding the type H counterpart was isolated

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