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Characterization of hydroxycinnamoyl-coenzyme a Shikimate hydroxycinnamoyltransferase from Populus euramericana

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Abstract

Hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase (HCT), PeHCT was cloned from Populus euramericana. The predicted amino acid sequence revealed that PeHCT contained a conserved HXXXDG motif that was found in acyltransferase. The in vitro substrate was determined using recombinant PeHCT. The recombinant PeHCT showed substrate-specificity towards shikimic acid. In addition, PeHCT displayed higher expression in the stem than in the leaf, and its expression increased during the growth stage of the leaf. Results indicate PeHCT could be involved in lignin biosynthesis by formation of p-coumaroyl shikimate.

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Authors and Affiliations

  1. Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul, 143-701, Republic of Korea

    Bong-Gyu Kim, In-Ah Kim & Joong-Hoon Ahn

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  1. Bong-Gyu Kim
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  2. In-Ah Kim
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  3. Joong-Hoon Ahn
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Correspondence to Joong-Hoon Ahn.

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Kim, BG., Kim, IA. & Ahn, JH. Characterization of hydroxycinnamoyl-coenzyme a Shikimate hydroxycinnamoyltransferase from Populus euramericana . J Korean Soc Appl Biol Chem 54, 817–821 (2011). https://doi.org/10.1007/BF03253167

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  • DOI: https://doi.org/10.1007/BF03253167

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