Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay.

Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Research Abstract Details 

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Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Abstract Text:

Corbin J Zea,Stephen W MacDonell,Nicola L Pohl,

Starch and its analogue glycogen are biosynthesized by enzymes that have been classified by sequence similarities into two families that have no significant sequence overlap: the animal/fungal glycogen synthases and the plant/bacterial glycogen (starch) synthases. Recent gene sequence analysis of putative archaea enzymes implicates them as a third family that links the structural and functional features of the other two classes. Herein, we present the first rapid electrospray ionization mass spectrometry-based assay to quantify any carbohydrate-polymerizing activity, the first cloning and recombinant expression as well as verification of the putative function of a glycogen synthase from the hyperthermophilic archaea Pyrococcus furiosus, and the characterization of a variety of glycogen synthases with the new assay. The new assay allowed the determination of Km and Vmax values for the rabbit, yeast, and P. furiosus glycogen synthases. Most surprisingly, unlike the synthases from rabbit or yeast and in contradiction to what would be expected from structural studies of other nucleotide-sugar binding proteins, the synthase from the archaea source accepts both uridine- and adenine-diphosphate activated glucose competitively and with comparable affinities to form a glucose polymer. This loose substrate specificity implicates this protein as the chemical link between the two branches of glycogen synthases that have evolved to accept primarily one or the other nucleotide as well as a good source enzyme for polymer bioengineering efforts.

Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Publishing Authors By Initials

CJ Zea,SW MacDonell,NL Pohl,

For similar heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidine nucleotides: uracil nucleotides: uridine diphosphate: uridine diphosphate sugars: uridine diphosphate glucose research abstracts see: heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidine nucleotides: uracil nucleotides: uridine diphosphate: uridine diphosphate sugars: uridine diphosphate glucose research

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Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Chemical Society

VOLUME: 125

Page Numbers: 13666-7

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 12

MONTH: Nov

YEAR: 2003

Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Keywords Mesh Terms:

KEYWORDS: Uridine Diphosphate Glucose

MESH TERMS: metabolism

Chemical & Substance for Abstract: Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay. Information

Substance Name: Glycogen Synthase

Registry Number: EC 2.4.1.11

Grant and Affiliation Information for Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay.

AFFILIATION: Department of Chemistry and the Plant Sciences Institute, Gilman Hall, Iowa State University, Ames, Iowa 50011-3111, USA.

Country: United States

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MEDLINETA: J Am Chem Soc

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