Disease relevance of Delta1-piperideine-2-carboxylate

• delta1-piperideine-2-carboxylate reductase of Pseudomonas putida [1].
• An enzymatic system for the synthesis of L-pipecolic acid from L-lysine by commercial L-lysine alpha-oxidase from Trichoderma viride and an extract of recombinant Escherichia coli cells coexpressing Delta(1)-piperideine-2-carboxylate reductase from Pseudomonas putida and glucose dehydrogenase from Bacillus subtilis is described [2].

High impact information on Delta1-piperideine-2-carboxylate

• Turnover is presumed to encompass a reversible oxidation at the alpha-amine, internal cyclization, and subsequent re-reduction of the cyclic delta1-piperideine-2-carboxylate intermediate [3].
• The gene encoding PP3590, called here amaC, forms an operon with dpkA, the gene encoding the enzyme involved in conversion of Delta(1)-piperideine-2-carboxylate to l-pipecolate in the d-lysine catabolic pathway [4].
• The amount of electron flow was estimated by applying the theory of Friedrich and Person [(1966) J. Chem. Phys. 44, 2166-2170] to these complexes; the amounts of charge transfer from reduced FAD and reduced 7,8-Cl(2)-FAD to D1PC were estimated to be about 10 and 8% of one electron, respectively, in the CT complexes of reduced DAO with D1PC [5].
• Enzymatic Synthesis of L-Pipecolic Acid by Delta(1)-Piperideine-2-carboxylate Reductase from Pseudomonas putida [2].

Gene context of Delta1-piperideine-2-carboxylate

• The C=N stretching mode (1,704 cm(-1)) of Delta(1)-piperideine-2-carboxylate (D1PC) downshifted to 1,675 and 1,681 cm(-1) upon complexation with reduced and semiquinoid DAO, respectively [5].

References