TAILIEUCHUNG - Báo cáo khoa học: A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3

Two distinguishable activity bands for dye-linkedl-proline dehydrogenase (PDH1 and PDH2) were detected when crude extract of the hyperthermo-philic archaeonPyrococcus horikoshiiOT-3 was run on a polyacrylamide gel. After purification, PDH1 was found to be composed of two different subunits with molecular masses of 56 and 43 kDa, whereas PDH2 was composed of four different subunits with molecular masses of 52, 46, 20 and 8 kDa. | iFEBS Journal A second novel dye-linked L-proline dehydrogenase complex is present in the hyperthermophilic archaeon Pyrococcus horikoshii OT-3 Ryushi Kawakami1 Haruhiko Sakuraba1 Hideaki Tsuge2 3 Shuichiro Goda1 Nobuhiko Katunuma2 and Toshihisa Ohshima1 1 Department of BiologicalScience and Technology Faculty of Engineering The University of Tokushima Japan 2 Institute for Health Science Tokushima Bunri University Japan 3 The Institutes for Enzyme Research University of Tokushima Japan Keywords ATP-containing dehydrogenase dye-linked L-proline dehydrogenase hyperthermophilic archaeon Pyrococcus horikoshii Correspondence T. Ohshima Department of Biological Science and Technology Faculty of Engineering The University of Tokushima 2-1 Minamijosanjima-cho Tokushima 7708506 Japan Fax 81 88 656 9071 Tel 81 88 656 7518 E-mail ohshima@ Received 7 May 2005 revised 3 June 2005 accepted 8 June 2005 doi Two distinguishable activity bands for dye-linked L-proline dehydrogenase PDH1 and PDH2 were detected when crude extract of the hyperthermo-philic archaeon Pyrococcus horikoshii OT-3 was run on a polyacrylamide gel. After purification PDH1 was found to be composed of two different subunits with molecular masses of 56 and 43 kDa whereas PDH2 was composed of four different subunits with molecular masses of 52 46 20 and 8 kDa. The native molecular masses of PDH1 and PDH2 were 440 and 101 kDa respectively indicating that PDH1 has an a4p4 structure while PDH2 has an abyỗ structure. PDH2 was found to be similar to the dye-linked L-proline dehydrogenase complex from Thermococcus profundus but PDH1 is a different type of enzyme. After production of the enzyme in Escherichia coli high-performance liquid chromatography showed the PDH1 complex to contain the flavins FMN and FAD as well as ATP. Gene expression and biochemical analyses of each subunit revealed that the b subunit bound FAD and exhibited proline dehydrogenase activity .

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