Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of Cr(III)ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates.-Reference-Cited by-同舟云学术

Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of Cr(III)ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates.

Published:1982-07 Issue:13 Volume:257 Page:7650-7656
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Jaffe E K,Nick J,Cohn M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 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. Diastereomers of the nucleoside phosphorothioates as probes of the structure of the metal nucleotide substrates and of the nucleotide binding site of yeast hexokinase.

3. Mechanistic studies on deoxyribonucleic acid dependent ribonucleic acid polymerase from Escherichia coli using phosphorothioate analogs. 2. The elongation reaction

4. A study of the mechanism of DNA polymerase I from Escherichia coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate.

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