delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA

FEMS Microbiology Letters
G P O'NeillD Söll

Abstract

Cell-free extracts of Escherichia coli and Bacillus subtilis catalyzed the tRNA-dependent, RNase A-sensitive formation of delta-aminolevulinic acid (ALA) from glutamate. Cell extracts prepared from cultures of E. coli grown under aerobic or anaerobic conditions had similar levels of ALA biosynthetic activity. Both the tRNA-stimulated conversion of glutamate to ALA and the conversion of glutamate-1-semialdehyde to ALA were inhibited by gabaculin. However, gabaculin had no effect on the growth of either E. coli or B. subtilis. The tRNA-dependent transformation of glutamate to ALA in E. coli and B. subtilis thus appears to be very similar to the pathway found in cyanobacteria, certain obligate anaerobic eubacteria, archaebacteria and in the chloroplasts of algae and higher plant species.

References

Apr 1, 1986·Archives of Biochemistry and Biophysics·T Oh-hamaS Miyachi
May 15, 1985·Archives of Biochemistry and Biophysics·J D Weinstein, S I Beale

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Citations

Jan 1, 1991·Archives of Microbiology·D MajumdarS I Beale
May 10, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Xinhuai LvLiwen Niu
Jun 1, 1993·Molecular & General Genetics : MGG·A V OsorioF Bastarrachea
Oct 7, 2011·Evidence-based Complementary and Alternative Medicine : ECAM·Ulysses Paulino AlbuquerqueCecília de Fátima Castelo Almeida
Aug 1, 1994·Molecular Microbiology·T M Henkin

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