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Detailed view Article in peer-reviewed journal
Current Microbiology 61, 1 (2010) 7-12
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Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa.
Driss Mountassif1, Pierre ANDREOLETTI2, Mustapha Cherkaoui-Malki3, Norbert Latruffe4, M'Hammed Saïd El Kebbaj1

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.
1:  LBBM - Laboratoire Biochimie et Biologie Moléculaire
2:  MAPMO - Mathématiques - Analyse, Probabilités, Modélisation - Orléans
3:  Lipides - Nutrition - Cancer
4:  LBMC / LBMN - Laboratoire de Biochimie Métabolique et Nutritionnelle