TAILIEUCHUNG - Báo cáo khoa học: Aldo-keto reductase from Helicobacter pylori – role in adaptation to growth at acid pH

Pyridine-linked oxidoreductase enzymes ofHelicobacter pylorihave been implicated in the pathogenesis of gastric disease. Previous studies in this laboratory examined a cinnamyl alcohol dehydrogenase that was capable of detoxifying a range of aromatic aldehydes. In the present work, we have extended these studies to identify and characterize an aldoketo reductase (AKR) enzyme present in H. pylori. | ỊFEBS Journal Aldo-keto reductase from Helicobacter pylori - role in adaptation to growth at acid pH Denise Cornally1 Blanaid Mee1 Ciaran MacDonaill1 Keith F. Tipton2 Dermot Kelleher3 Henry J. Windle3 and Gary T. M. Henehan1 1 Schoolof Food Science and EnvironmentalHealth Dublin Institute of Technology Ireland 2 Department of Biochemistry Trinity College Dublin Ireland 3 Department of ClinicalMedicine and Institute of Molecular Medicine Trinity College Dublin Ireland Keywords acid resistance aldo-keto reductase Helicobacter pylori oxidoreductase Correspondence H. J. Windle Institute of Molecular Medicine Dublin Molecular Medicine Centre Trinity College Dublin St James Hospital Dublin 8 Ireland Fax 353 1 4542043 Tel 353 1 8962211 E-mail hjwindle@ Received 20 January 2008 revised 4 April 2008 accepted 9 April 2008 doi Pyridine-linked oxidoreductase enzymes of Helicobacter pylori have been implicated in the pathogenesis of gastric disease. Previous studies in this laboratory examined a cinnamyl alcohol dehydrogenase that was capable of detoxifying a range of aromatic aldehydes. In the present work we have extended these studies to identify and characterize an aldoketo reductase AKR enzyme present in H. pylori. The gene encoding this AKR was identified in the sequenced strain of H. pylori 26695. The gene referred to as HpAKR was cloned and expressed in Escherichia coli as a His-tag fusion protein and purified using nickel chelate chromatography. The gene product HpAKR has been assigned to the AKR13C1 family although it differs in specificity from the two other known members of this family. The enzyme is a monomer with a molecular mass of approximately 39 kDa on SDS PAGE. It reduces a range of aromatic aldehyde substrates with high catalytic efficiency and exhibits dual cofactor specificity for both NADPH and NADH. HpAKR can function over a broad pH range pH 4-9 and has a pH optimum of . It is inhibited by sodium valproate. Its

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