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Novel characteristics of UDP-glucose dehydrogenase activities in maize: non-involvement of alcohol dehydrogenases in cell wall polysaccharide biosynthesis

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Abstract

UDP-glucose dehydrogenase (UDPGDH) activity was detected in extracts of maize cell-cultures and developing leaves. The reaction product was confirmed as UDP-glucuronate. Leaf extracts from null mutants defective in one or both of the ethanol dehydrogenase genes, ADH1 and ADH2, had similar UDPGDH activities to wild-type, showing that UDPGDH activity is not primarily due to ADH proteins. The mutants showed no defect in their wall matrix pentose:galactose ratios, or matrix:cellulose ratio, showing that ADHs were not required for normal wall biosynthesis. The majority of maize leaf UDPGDH activity had K m (for UDP-glucose) 0.5–1.0 mM; there was also a minor activity with an unusually high K m of >50 mM. In extracts of cultured cells, kinetic data indicated at least three UDPGDHs, with K m values (for UDP-glucose) of roughly 0.027, 2.8 and >50 mM (designated enzymes EL, EM and EH respectively). EM was the single major contributor to extractable UDPGDH activity when assayed at 0.6–9.0 mM UDP-Glc. Most studies, in other plant species, had reported only EL-like isoforms. Ethanol (100 mM) partially inhibited UDPGDH activity assayed at low, but not high, UDP-glucose concentrations, supporting the conclusion that at least EH activity is not due to ADH. At 30 μM UDP-glucose, 20–150 μM UDP-xylose inhibited UDPGDH activity, whereas 5–15 μM UDP-xylose promoted it. In conclusion, several very different UDPGDH isoenzymes contribute to UDP-glucuronate and hence wall matrix biosynthesis in maize, but ADHs are not responsible for these activities.

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Abbreviations

ADH:

Alcohol (ethanol) dehydrogenase

AIR:

Alcohol-insoluble residue

EL, EM and EH :

Isoforms of UDPGDH with respectively low, medium and high Km values for UDP-Glc

TFA:

Trifluoroacetic acid

UDP-Glc:

UDP-d-glucose

UDPGDH:

UDP-d-glucose dehydrogenase

UDP-GlcA:

UDP-d-glucuronic acid

UDP-Xyl:

UDP-d-xylose

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Acknowledgements

We thank the European Community for funding the ‘COPOL’ project, during the tenure of which this work was conducted. Drs A. Murigneux and J.-P. Martinant (Biogemma, France) are thanked for providing the adh mutant seeds. CarboSource Services, Athens, GA, USA are acknowledged for supplying UDP-Xyl. We thank Dr B. Dudley and Mrs J. Miller for help in HPLC analysis.

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  1. Anna Kärkönen

    Present address: Department of Applied Biology, University of Helsinki, P.O. Box 27, 00014, Helsinki, Finland

Authors and Affiliations

  1. The Edinburgh Cell Wall Group, Institute of Molecular Plant Sciences, School of Biological Sciences, The University of Edinburgh, Daniel Rutherford Building, The King’s Buildings, EH9 3JH, Edinburgh, UK

    Anna Kärkönen & Stephen C. Fry

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  1. Anna Kärkönen
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  2. Stephen C. Fry
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Correspondence to Stephen C. Fry.

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Kärkönen, A., Fry, S.C. Novel characteristics of UDP-glucose dehydrogenase activities in maize: non-involvement of alcohol dehydrogenases in cell wall polysaccharide biosynthesis. Planta 223, 858–870 (2006). https://doi.org/10.1007/s00425-005-0207-7

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