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Murakami, K. et al.

Cloning and characterization of the glutamate 1-semialdehyde aminomutase gene from Xanthomonas campestris pv. phaseoli.

The gene from Xanthomonas campestris pv. phaseoli for glutamate 1-semialdehyde ( GSA) aminomutase, which is involved in the C5 pathway for synthesis of delta-aminolevulinic acid (ALA), was cloned onto a multicopy plasmid, pUC18, by the complementation of an ALA-deficient mutant (hemL) of Escherichia coli. Subcloning of deletion fragments from the initial 3.5-kb chromosomal fragment allowed the isolation of a 1.7-kb fragment which could complement the hemL mutation. Nucleotide sequence analysis of the 1.7-kb DNA fragment revealed an open reading frame (ORF) that is located downstream from a potential promoter sequence and a ribosome-binding site. The ORF encodes a polypeptide of 429 amino acid residues, and the deduced molecular mass of this polypeptide is 45,043 Da. The amino acid sequence shows a high degree of homology to the HemL proteins from other organisms, and a putative binding site for pyridoxal 5'-phosphate is conserved.[1]

References

Cloning and characterization of the glutamate 1-semialdehyde aminomutase gene from Xanthomonas campestris pv. phaseoli. Murakami, K., Korbsrisate, S., Asahara, N., Hashimoto, Y., Murooka, Y. Appl. Microbiol. Biotechnol. (1993) [Pubmed]

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