The structure of the metal-nucleotide complex substrate for yeast hexokinase
| Autor: | Cecil Cooper |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Stereochemistry
Biophysics Saccharomyces cerevisiae Glucosephosphate Dehydrogenase Biology Biochemistry Metal Enzyme activator chemistry.chemical_compound Adenosine Triphosphate Drug Stability Nickel Hexokinase Magnesium Pyrroles Nucleotide Binding site Purine Nucleotides Molecular Biology chemistry.chemical_classification Binding Sites Temperature Cell Biology Ribonucleotides Yeast Enzyme Activation Kinetics Enzyme chemistry visual_art visual_art.visual_art_medium Adenosine triphosphate Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 57:434-437 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(74)90949-8 |
| Popis: | A comparison has been made of the kinetic parameters obtained with yeast hexokinase using Mg 2+ or Ni 2+ as metal ion activator and ATP or tubercidin-5′-triphosphate as nucleotide substrate. It is concluded that the relative specificity of the enzyme for MgATP 2− does not involve a contribution arising from an interaction of the metal ion with the purine ring of the nucleotide. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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