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Activity of an atypical Arabidopsis thaliana pectin methylesterase

Abstract : An Arabidopsis thaliana pectin methylesterase that was not predicted to contain any signaling sequence was produced in E. coli and purified using a His tag added at its N-terminus. The enzyme demethylesterified Citrus pectin with a K m of 0.86 mg/ml. The enzyme did not require salt for activity and was found to be relatively temperature-sensitive. The precipitation of enzyme-treated pectin by CaCl2 suggested that the enzyme had a blockwise mode of pectin demethylesterification. A purified kiwi (Actinidia chinensis) pectin methylesterase inhibitor had no effect on the activity of the enzyme whereas it strongly inhibited a flax pectin methylesterase. A model of the protein structure revealed that an extra amino acid sequence in this particular Arabidopsis pectin methylesterase could form a ß-strand outside the core structure, which might be preventing the inhibitor from binding the protein.
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Contributor : Arnaud Lehner Connect in order to contact the contributor
Submitted on : Tuesday, May 14, 2019 - 2:04:58 PM
Last modification on : Friday, October 8, 2021 - 4:28:16 PM

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Sarah Dedeurwaerder, Laurence Menu-Bouaouiche, Alain Mareck, Patrice Lerouge, Francois Guerineau. Activity of an atypical Arabidopsis thaliana pectin methylesterase. Planta, Springer Verlag, 2009, 229 (2), pp.311-321. ⟨10.1007/s00425-008-0831-0⟩. ⟨hal-02128673⟩



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