Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases |
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Authors: | Martin C; Cami B; Yeh P; Stragier P; Parsot C; Patte JC |
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Institution: | Laboratoire de Chimie Bacterienne, Centre National de la Recherche Scientifique, Marseille, France. |
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Abstract: | The lysA gene encodes meso-diaminopimelate (DAP) decarboxylase
(E.C.4.1.1.20), the last enzyme of the lysine biosynthetic pathway in
bacteria. We have determined the nucleotide sequence of the lysA gene from
Pseudomonas aeruginosa. Comparison of the deduced amino acid sequence of
the lysA gene product revealed extensive similarity with the sequences of
the functionally equivalent enzymes from Escherichia coli and
Corynebacterium glutamicum. Even though both P. aeruginosa and E. coli are
Gram-negative bacteria, sequence comparisons indicate a greater similarity
between enzymes of P. aeruginosa and the Gram- positive bacterium C.
glutamicum than between those of P. aeruginosa and E. coli enzymes.
Comparison of DAP decarboxylase with protein sequences present in data
bases revealed that bacterial DAP decarboxylases are homologous to mouse
(Mus musculus) ornithine decarboxylase (E.C.4.1.1.17), the key enzyme in
polyamine biosynthesis in mammals. On the other hand, no similarity was
detected between DAP decarboxylases and other bacterial amino acid
decarboxylases.
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