Cloning and characterization of pcd encoding Δ́-piperideine-6-carboxylate dehydrogenase from Flavobacterium lutescens IFO3084

The pcd gene from Flavobacterium lutescens IFO3084 encoding Δ́-piperideine-6-carboxylate dehydrogenase (PCD) was cloned, sequenced, and expressed in Escherichia coli. The deduced amino acid sequence of PCD from F. lutescens IFO3984 showed strong similarity to that from Streptomyces clavuligerus. The molecular mass of the recombinant PCD was estimated to be approximately 58,000 Da by SDS-PAGE and native PAGE, which indicated that the enzyme molecule is a monomer. The in vitro analysis of L-αaminoadipic acid (L-AAA) production showed that L-AAA is synthesized from L-lysine in two steps catalyzed by L-lysine 6-aminotransferase (LAT) and PCD from F. lutescens IFO3984.