Regulation of Proline Catabolism by Leucyl,Phenylalanyl-tRNA-Protein Transferase

A mutant of Escherichia coli lacking leucyl,phenylalanyl-tRNA-protein transferase (L-leucyl-tRNA:protein leucyltransferase, EC 2.3.2.6) exhibited several abnormal growth characteristics relative to the wild type or a revertant when grown with glycerol as a carbon source. All three strains were auxot...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1975-01, Vol.72 (1), p.405-408
Main Authors: Deutch, Charles E., Soffer, Richard L.
Format: Article
Language:English
Subjects:
Acyltransferases - metabolism
Amino Acid Oxidoreductases - metabolism
Bacterial Proteins - metabolism
Carbon
Carbon Radioisotopes
Catabolism
Cell growth
Enzymes
Escherichia coli
Escherichia coli - enzymology
Glucose - metabolism
Glycerol - metabolism
Kinetics
Mutation
Oxidases
Physiological regulation
Proline - metabolism
Protein Biosynthesis
Radioactive decay
Repression
RNA, Transfer - metabolism
Steepest descent method
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A mutant of Escherichia coli lacking leucyl,phenylalanyl-tRNA-protein transferase (L-leucyl-tRNA:protein leucyltransferase, EC 2.3.2.6) exhibited several abnormal growth characteristics relative to the wild type or a revertant when grown with glycerol as a carbon source. All three strains were auxotrophic for proline. The mutant required higher levels of this amino acid than did the other strains to attain a normal growth yield and metabolized exogenous [14C]proline more rapidly. The greater rate of proline utilization was associated with a 4-fold increase in specific activity of proline oxidase. When glucose rather than glycerol was employed as a carbon source, proline oxidase activity was reduced by catabolite repression and the growth characteristics of the mutant were similar to those of the parental and revertant strains. These results suggest that the mutant growth phenotype is due to an altered rate of proline catabolism and constitute evidence for regulation of a specific metabolic pathway by leucyl,phenylalanyl-tRNA-protein transferase.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.72.1.405