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GrainGenes Reference Report: PLA-208-31

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Reference	PLA-208-31
Title	Differential induction of cinnamyl alcohol dehydrogenase during defensive lignification in wheat (Triticum aestivum L.): Characterisation of the major inducible form.
Journal	Planta
Year	1999
Volume	208
Pages	31-37
Author	Mitchell HJ Hall SA Stratford R Hall JL Barber MS
Abstract	The induction and substrate specificity of cinnamyl alcohol dehydrogenase, (CAD, EC 1.1.1.195) was investigated in relation to the deposition of a defensive, syringyl-rich lignin at wound margins in wheat (Triticum aestivum L. cv. Brigadier). Column chromatography of untreated, wounded and elicitor-treated tissues revealed three major CAD forms (CAD-A,-B and -C) of which only CAD-C was responsive to elicitors. Examination of the substrate preference of these fractions indicated p-coumaryl alcohol to be the preferred substrate of CAD-A and CAD-B, whereas sinapyl alcohol was favoured by CAD-C. Activity-stained isoelectric focusing gels revealed in untreated and wounded leaves four CAD isoenzymes with esoelectric points of 4.59 (i), 4.67 (ii), 4.81 (iii), 4.93 (iv). Elicitor treatment generally enhanced the staining of all isoenzymes and resulted in the appearance of two new isoenzymes of 5.22 (v) and pI 5.31 (vi). In activity stained non-denaturing PAGE gels, CAD-C further resolved into two distinct zones of CAD activity. Cinnamyl alcohol dehydrogenase-C was purified to apparent homogeneity and characterisation revealed a 45-kDa subunit peptide which in its native form demonstrated a marked substrate preference for sinapyl alcohol. Overall, the differential induction and substrate preference of CAD-C are consistent with a defensive role during defensive lignifications at wound margins in wheat.
External Databases	Agricola: 2010-85060
Keyword	[ Hide all but 1 of 13 ] alcohol oxidoreductases alcohols cell wall components defense mechanisms enzyme activity isoelectric point isoenzyme lignification lignin mechanical damage molecular weight substrate triticum aestivum

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