Molecular cloning and characterization of cinnamyl alcohol dehydrogenase CDNA from interspecific hybrid Acacia mangium X Acacia auriculiformis

Pang, S. L. and Choong, C. Y. and Wickneswari, R. (2006) Molecular cloning and characterization of cinnamyl alcohol dehydrogenase CDNA from interspecific hybrid Acacia mangium X Acacia auriculiformis. Journal of Tropical Plant Physiology, 1 (1). pp. 89-99.

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Abstract

Cinnamyl alcohol dehydrogenase (CAD; EC 1.1.1.195) is an indicator of lignin biosynthesis because of its specific role in the reduction of hydroxycinnamaldehydes to hydroxycinnamyl alcohols. This protein catalyzes the final step in a branch of phenylpropanoid pathway specific for production of lignin monomers. In this study, a full length cDNA of CAD (AhCAD) from the inner bark tissue of interspecific hybrid Acacia mangium x Acacia auriculiformis was obtained by rapid amplification of cDNA ends (RACE). The full length AhCAD was 1346 bp; containing a 1089 bp open reading frame (ORF), which encodes a polypeptide of 363 amino acids, with a 5' untranslated region of 65 bp and a 3' untranslated region of 192 bp. The deduced protein had a calculated molecular weight of 39.99 kDa and an isoelectric point of 5.9. The AhCAD sequence was compared with deduced polypeptide sequences of other isolated plant CAD enzymes. A conserved zinc-containing alcohol dehydrogenase motif in all plant CADs was found in the encoded AhCAD amino acid sequence. The encoded polypeptide exhibited sequence similarity to CADs from different plants, the highest identities being to CADs from Medicago sativa (69 %) and Nicotiana tabacum (67 %).

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