Summary: Metabolites such as diaminopimelate and some aromatic derivatives, not synthesized in mammalian cells, are essential for growth of bacteria. As a first step towards the design of a new human live vaccine that uses attenuated strains of , the and genes, encoding aspartate β-semialdehyde dehydrogenase, 3-dehydroquinase and tetrahydrodipicolinate -succinyltransferase, respectively, were cloned by complementation of mutants. The complete nucleotide sequence of the gene was determined and found to contain an open reading frame capable of encoding a protein of 349 amino acids with a calculated of 38007. Comparison of this deduced aspartate β-semialdehyde dehydrogenase amino acid sequence with those of the same enzyme from and revealed 46% and 36% identity, respectively. By contrast, the identity between the enzyme and the or enzymes was less than 31%. Highly conserved sequences within aspartate semialdehyde dehydrogenase from the five organisms were observed at the amino and carboxyl termini, and around the cysteine of the active site.


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