Diastereomers of the nucleoside phosphorothioates as probes of the structure of the metal nucleotide substrates and of the nucleotide binding site of yeast hexokinase.-Reference-Cited by-同舟云学术

Diastereomers of the nucleoside phosphorothioates as probes of the structure of the metal nucleotide substrates and of the nucleotide binding site of yeast hexokinase.

Published:1979-11 Issue:21 Volume:254 Page:10839-10845
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Jaffe E.K.,Cohn M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference12 articles.

1. Divalent cation-dependent stereospecificity of adenosine 5‘-O-(2-thiotriphosphate) in the hexokinase and pyruvate kinase reactions. The absolute stereochemistry of the diastereoisomers of adenosine 5‘-O-(2-thiotriphosphate).

2. X-ray crystal and molecular structure and absolute configuration of (dihydrogen tripolyphosphato)tetraamminecobalt(III) monohydrate, Co(NH3)4H2P3O10·H2O. A model for a metal-nucleoside polyphosphate complex

3. Substrate activity of (adenosine triphosphato)tetraamminecobalt(III) with yeast hexokinase and separation of diastereomers using the enzyme

4. Use of chromium-adenosine triphosphate and lyxose to elucidate the kinetic mechanism and coordination state of the nucleotide substrate for yeast hexokinase

5. Synthesis and properties of diastereoisomers of adenosine 5'-(O-1-thiotriphosphate) and adenosine 5'-(O-2-thiotriphosphate)

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