tailieunhanh - Báo cáo khoa học: Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway

Insertion of heterologous peptide sequences into a protein carrier may impose structural constraints that could help the peptide to adopt a proper fold. This concept could be the starting point for the development of a new generation of safe subunit vaccines based on the expression of poorly immunogenic epitopes. | ỊFEBS Journal Metabolic fate of L-lactaldehyde derived from an alternative L-rhamnose pathway Seiya Watanabe1 2 3 Sommani Piyanart1 and Keisuke Makino1 2 3 4 1 Institute of Advanced Energy Kyoto University Japan 2 New Energy and IndustrialTechnology Development Organization Kyoto Japan 3 CREST JST Japan Science and Technology Agency Japan 4 Innovative Collaboration Center Kyoto University Japan Keywords Azotobacter vinelandii L-lactaldehyde dehydrogenase L-rhamnose metabolism molecular evolution Pichia stipitis Correspondence S. Watanabe Institute of Advanced Energy Kyoto University Gokasho Uji Kyoto 611-0011 Japan Fax 81 774 38 3524 Tel 81 774 38 3596 E-mail irab@ Received 8 July 2008 revised 9 August 2008 accepted 15 August 2008 doi Fungal Pichia stipitis and bacterial Azotobacter vinelandii possess an alternative pathway of L-rhamnose metabolism which is different from the known bacterial pathway. In a previous study Watanabe S Saimura M Makino K 2008 Eukaryotic and bacterial gene clusters related to an alternative pathway of non-phosphorylated L-rhamnose metabolism. J Biol Chem 283 20372-20382 we identified and characterized the gene clusters encoding the four metabolic enzymes L-rhamnose 1-dehydrogenase LRA1 L-rhamnono-y-lactonase LRA2 L-rhamnonate dehydratase LRA3 and L-2-keto-3-deoxyrhamnonate aldolase LRA4 . In the known and alternative L-rhamnose pathways L-lactaldehyde is commonly produced from L-2-keto-3-deoxyrhamnonate and L-rhamnulose 1-phosphate by each specific aldolase respectively. To estimate the metabolic fate of L-lact-aldehyde in fungi we purified L-lactaldehyde dehydrogenase LADH from P. stipitis cells L-rhamnose-grown to homogeneity and identified the gene encoding this enzyme PsLADH by matrix-assisted laser desorption ionization-quadruple ion trap-time of flight mass spectrometry. In contrast LADH of A. vinelandii AvLADH was clustered with the LRA1-4 gene on the genome. Physiological .

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