PMID:2651407

Citation	Li, JM, Brathwaite, O, Cosloy, SD and Russell, CS (1989) 5-Aminolevulinic acid synthesis in Escherichia coli. J. Bacteriol. 171:2547-52
Abstract	A hemA mutant of Escherichia coli containing a multicopy plasmid which complemented the mutation excreted 5-aminolevulinic acid (ALA) into the medium. [1-14C]glutamate was substantially incorporated into ALA by this strain, whereas [2-14C]glycine was not. Periodate degradation of labeled ALA showed that C-5 of ALA was derived from C-1 of glutamate. The synthesis of ALA by two sonicate fractions which had been processed by gel filtration and dialysis, respectively, was dependent on glutamate, ATP, NADPH, tRNA(Glu), and pyridoxal phosphate. tRNA(Glu) stimulated ALA synthesis in a concentration-dependent manner. Pretreatment with RNase reduced this stimulation. The amino acid sequence of the cloned insert, derived from the nucleotide sequence (J.-M. Li, C. S. Russell, and S. D. Cosloy, J. Cell Biol. 107:617a, 1988), showed no homology with any ALA synthase sequenced to date. These results suggest that E. coli synthesizes ALA by the C5 pathway from the intact five-carbon chain of glutamate.
Links	PubMed PMC209933
Keywords	Adenosine Triphosphate/metabolism; Aminolevulinic Acid/biosynthesis; Escherichia coli/metabolism; Glutamates/metabolism; Levulinic Acids/biosynthesis; RNA, Transfer, Glu/metabolism; Ribonucleases/pharmacology
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