Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotides
| Autor: | Lloyd R. Finch, Richard I. Christopherson |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
endocrine system diseases
Sodium chemistry.chemical_element Cytosine Nucleotides Biology medicine.disease_cause Adenosine Triphosphate In vivo Aspartate Carbamoyltransferase Escherichia coli medicine Magnesium Nucleotide Aspartate carbamoyltransferase activity chemistry.chemical_classification Effector nutritional and metabolic diseases General Medicine Enzyme Activation Aspartate carbamoyltransferase Biochemistry chemistry Guanosine Triphosphate hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 481:80-85 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(77)90139-5 |
| Popis: | Purified aspartate carbamoyltransferase from Escherichia coli K12 (carbamoylphosphate: l -aspartate carbamyltransferase, EC 2.1.3.2) shows greater activity with nucleotide effectors as the magnesium nucleotide complex than with similar amounts of the sodium nucleotide. Regulation of aspartate carbamoyltransferase activity in vivo may occur by changes in the total concentration of regulatory nucleotides or, under conditions of magnesium-limited growth, by variation of the saturation of the nucleotides with magnesium. |
| Databáze: | OpenAIRE |
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