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

Applied Microbiology and Biotechnology
K MurakamiY Murooka


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.


Jun 1, 1995·Photosynthesis Research·Y J Avissar, P A Moberg
Mar 1, 1994·Proceedings of the National Academy of Sciences of the United States of America·R HöfgenD von Wettstein
May 13, 1997·Proceedings of the National Academy of Sciences of the United States of America·M HennigJ N Jansonius
Sep 4, 2001·Biotechnology & Genetic Engineering Reviews·S Nishikawa, Y Murooka
Sep 26, 2017·The Journal of Clinical Investigation·Natacha ColliouMansour Mohamadzadeh

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