A single mutation affects L-serine deaminase, L-leucyl-, L-phenylalanyl-tRNA protein transferase, and proline oxidase activity in Escherichia coli K-12

Author:

Tam A,Herrington M B,Kapoor V,Newman E B

Abstract

A mutation at a single locus, wyb, results in several phenotypic changes in Escherichia coli K-12. The Wyb- phenotype includes: (i) an increase in L-serine deaminase activity, together with a loss of inducibility by L-leucine; (ii) an absence of L-leucyl-, L-phenylalanyl-tRNA protein transferase activity; (iii) inducibility of proline oxidase by proline; and (iv) a loss of ability to use maltose as a carbon and energy source.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference9 articles.

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2. Pleiotropic phenotype of an Escherichia coli mutant lacking leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase;Deutch C. E.;J. Bacteriol.,1977

3. Regulation of proline catabolism by leucyl, phenylalanyl-tRNA protein transferase;Deutch C. E.;Proc. Natl. Acad. Sci. U.S.A.,1975

4. Studies on Lserine deaminase in Escherichia coli K-12;Isenberg S.;J. Bacteriol.,1974

5. Enzymatic modification of proteins. m. Purification and properties of a leucyl, phenylalanyl-transfer ribonucleic acid-protein transferase from E. coli;Leibowitz M. J.;J. Biol. Chem.,1970

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