Lysine cyclodeaminase (LCD EC : 4.3.1.28) is a �-nicotinamide adenine dinucleotide dependent enzyme, which catalyses the a-deamination of L-lysine to produce L-pipecolate. L-pipecolate is a non-proteinogenic amino acid that is incorporated into multiple secondary metabolite products, including rapamycin, virginiamycin and pristinamycin. L-lysine cyclodeaminase from Streptomyces pristinaespiralis (spLCD) was identified as key enzyme for the conversion of L-lysine to L-pipecolate in the metabolic pathway to immunosuppressant. However, there is not much report for optimization to produce L-pipecolate from L-lysine. In this study, we optimized an each external reaction factors to increase the conversion rate from L-lysine to L-pipecolate. We accomplished almost 90% of conversion of L-lysine to L-pipecolate. In addition we confirmed that the conversion by spLCD is highly enantioselective for L-lysine, on the while it also showed the conversion for other substrates having similar chemical structures with L-lysine.

Functional expression and characterization of  L-lysine cyclodeaminase from Streptomyces pristinaespiralis

248th National Meeting (2014)

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