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| HAL : hal-00514502, version 1 |
| PubMed : 20052585 |
| DOI : 10.1007/s00284-009-9568-7 |
| Fiche détaillée |  Récupérer au format |
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| Current Microbiology 61, 1 (2010) 7-12 |
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| Structural and catalytic properties of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas aeruginosa. |
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| Driss Mountassif 1Pierre ANDREOLETTI 2 |
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| (07/2010) |
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| 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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| 1 : | Laboratoire Biochimie et Biologie Moléculaire (LBBM) |
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Université Hassan II |
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| 2 : | Mathématiques - Analyse, Probabilités, Modélisation - Orléans (MAPMO) |
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Université d'Orléans – CNRS : UMR7349 |
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| 3 : | Lipides - Nutrition - Cancer |
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INSERM : U866 – Université de Bourgogne |
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| 4 : | Laboratoire de Biochimie Métabolique et Nutritionnelle (LBMC / LBMN) |
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Université de Bourgogne |
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| Domaine | : | Sciences du Vivant/Biochimie, Biologie Moléculaire |
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| Liste des fichiers attachés à ce document : | |||||
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| hal-00514502, version 1 | |
| http://hal.archives-ouvertes.fr/hal-00514502 | |
| oai:hal.archives-ouvertes.fr:hal-00514502 | |
| Contributeur : Norbert Latruffe | |
| Soumis le : Jeudi 2 Septembre 2010, 16:10:30 | |
| Dernière modification le : Jeudi 2 Septembre 2010, 17:25:57 | |
