PMID:2656630

Citation	Avissar, YJ and Beale, SI (1989) Identification of the enzymatic basis for delta-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli. J. Bacteriol. 171:2919-24
Abstract	The hemA mutation of Escherichia coli K-12 confers a requirement for delta-aminolevulinic acid (ALA). Cell extract prepared from the hemA strain SASX41B was incapable of producing ALA from either glutamate or glutamyl-tRNA, whereas extract of the hem+ strain HB101 formed colorimetrically detectable amounts of ALA and transferred label from 1-[14C]glutamate and 3,4-[3H]glutamyl-tRNA to ALA. Extracts of both strains converted glutamate-1-semialdehyde to ALA and were capable of aminoacylating tRNAGlu. Glutamyl-tRNA formed by extracts of both strains could be converted to ALA by the extract of hem+ cells. The extract of hemA cells did not convert glutamyl-tRNA formed by either strain to ALA. However, the hemA cell extract, when supplemented in vitro with glutamyl-tRNA dehydrogenase isolated from Chlorella vulgaris cells, formed about as much ALA as did the unsupplemented hem+ cell extract. We conclude from these observations that the enzyme activity that is lacking in the ALA auxotrophic strain carrying the hemA mutation is that of glutamyl-tRNA dehydrogenase.
Links	PubMed PMC209995
Keywords	Aminolevulinic Acid/biosynthesis; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Genetic Complementation Test; Glutamates/metabolism; Glycine/metabolism; Ketone Oxidoreductases/metabolism; Levulinic Acids/biosynthesis; Mutation; RNA, Transfer, Amino Acyl/metabolism
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