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Please use this identifier to cite or link to this item: http://hdl.handle.net/2262/33847

Title: Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori. An aldehyde dismutating enzyme
Author: KELLEHER, DERMOT P
TIPTON, KEITH
WINDLE, HENRY
Sponsor: Health Research Board
Author's Homepage: http://people.tcd.ie/kellehdp
Keywords: aldehyde • cinnamyl alcohol dehydrogenase • dismutation • Helicobacter pylori • lignin
Issue Date: 2005
Publisher: John Wiley
Citation: B Mee, D Kelleher, J Frias, R Malone, KF Tipton, GT Henehan, HJ Windle ‘Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori. An aldehyde dismutating enzyme’ in FEBS Journal, 272, (5), 2005, pp 1255 - 1264
Series/Report no.: The FEBS Journal
272
5
Abstract: Cinnamyl alcohol dehydrogenases (CAD; 1.1.1.195) catalyse the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants. Outside of plants their role is less defined. The gene for cinnamyl alcohol dehydrogenase from Helicobacter pylori (HpCAD) was cloned in Escherichia coli and the recombinant enzyme characterized for substrate specificity. The enzyme is a monomer of 42.5 kDa found predominantly in the cytosol of the bacterium. It is specific for NADP(H) as cofactor and has a broad substrate specificity for alcohol and aldehyde substrates. Its substrate specificity is similar to the well-characterized plant enzymes. High substrate inhibition was observed and a mechanism of competitive inhibition proposed. The enzyme was found to be capable of catalysing the dismutation of benzaldehyde to benzyl alcohol and benzoic acid. This dismutation reaction has not been shown previously for this class of alcohol dehydrogenase and provides the bacterium with a means of reducing aldehyde concentration within the cell.
Description: PUBLISHED
URI: http://dx.doi.org/10.1111/j.1742-4658.2005.04561.x
http://hdl.handle.net/2262/33847
Appears in Collections:Administrative Staff Authors (Scholarly Publications)

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