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Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa.: Bacterial D-3-hydroxybutyrate dehydrogenase.

Abstract : To put forward BDH from Pseudomonas aeruginosa's enzymatic properties, we report a two-step purification of BDH and its gene sequencing allowing the investigation of its structural properties. Purification of BDH was achieved, using ammonium sulfate fractionation and Blue Sepharose CL-6B affinity chromatography. SDS-PAGE analysis reveals a MM of 29 kDa, whereas the native enzyme showed a MM of 120 kDa suggesting a homotetrameric structure. BDH encoding gene sequence shows a nucleotide open reading frame sequence of 771 bp encoding a 265 amino acid residues polypeptide chain. The modeling analysis of the three dimensional structure fits with the importance of amino acids in the catalysis reaction especially a strictly conserved tetrad. Amino-acid residues in interaction with the coenzyme NAD(+) were also identified.
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Submitted on : Thursday, September 2, 2010 - 4:10:30 PM
Last modification on : Friday, September 27, 2019 - 11:26:10 AM
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Driss Mountassif, Pierre Andreoletti, Mustapha Cherkaoui-Malki, Norbert Latruffe, M'Hammed Saïd El Kebbaj. Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa.: Bacterial D-3-hydroxybutyrate dehydrogenase.. Current Microbiology, Springer Verlag, 2010, 61 (1), pp.7-12. ⟨10.1007/s00284-009-9568-7⟩. ⟨hal-00514502⟩

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