Diaminopimelate epimerase and decarboxylase

Diaminopimelate decarboxylase catalyzes the final step in lysine biosynthesis in bacteria. The epimerase catalyzes the interconversion of the ll- and meso isomers of diaminopimelate. Because these enzymes are absent in mammals, they are considered to be potential targets for antimicrobial agents. 

The o-phthaldialdehyde derivatives of LL-diaminopimelate, meso-diaminopimelate, norvaline (internal standard), and lysine were separated on a Spherisorb Q8 column (4.5 mm x 250 mm). A linear gradient from 100% solvent A (30 methanol, 70% 50 mAf sodium acetate buffer (pH 5.9) to 30% solvent A and 70% methanol was imposed over 35 minutes. Detection was by fluorescence, with excitation and emission wavelength of 340 and 455 nm, respectively. 

The source of enzyme was cell-free extracts prepared from a lysine-overproducing strain of Bacillus subtilis NCIB 3610. 

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See also in sourсe #XX -- [ ]

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