51. Incorporation of amino acid analogs during the biosynthesis of Escherichia coli aspartate transcarbamylase.
- Author
-
Gueguen P, Padron M, Perbal B, and Hervé G
- Subjects
- Alanine analogs & derivatives, Alanine metabolism, Ethionine metabolism, Macromolecular Substances, Methylhistidines metabolism, Phenylalanine analogs & derivatives, Phenylalanine metabolism, Triazoles metabolism, Tryptophan analogs & derivatives, Tryptophan metabolism, p-Fluorophenylalanine metabolism, Amino Acids metabolism, Aspartate Carbamoyltransferase biosynthesis, Escherichia coli enzymology
- Abstract
Amino acid-requiring mutants capable of producing derepressed levels of aspartate transcarbamylase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) were obtained and used for the incorporation in this enzyme of eight different amino acid analogs. These amino acid replacements enabled the biosynthesis of a series of modified aspartate transcarbamylases altered in their catalytic or regulatory properties. The enzyme in which phenylalanine was rereplaced by 2-fluorophenylalanine was purified to homogeneity and appeared to have the same specific activity as normal asparate transcarbamylase but lacking both homotropic and heterotropic interactions.
- Published
- 1980
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