Molecular Diversity of Tuliposide A-Converting Enzyme in the Tulip (2024)

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Volume 77 Issue 5 23 May 2013

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Taiji NOMURA

Biotechnology Research Center, Toyama Prefectural University

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Aya TSUCHIGAMI

Biotechnology Research Center, Toyama Prefectural University

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Shinjiro OGITA

Biotechnology Research Center, Toyama Prefectural University

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Yasuo KATO

Biotechnology Research Center, Toyama Prefectural University

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Bioscience, Biotechnology, and Biochemistry, Volume 77, Issue 5, 23 May 2013, Pages 1042–1048, https://doi.org/10.1271/bbb.130021

Published:

23 May 2013

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Received:

09 January 2013

Accepted:

04 February 2013

Published:

23 May 2013

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Tuliposide A-converting enzyme (TCEA) catalyzes the conversion of 6-tuliposide A to its lactonized aglycon, tulipalin A, in the tulip (Tulipa gesneriana). The TgTCEA gene, isolated previously from petals, was transcribed in all tulip tissues but not in the bulbs despite the presence of TCEA activity, which allowed prediction of the presence of a TgTCEA isozyme gene preferentially expressed in the bulbs. Here, the TgTCEA-b gene, the TgTCEA hom*olog, was identified in bulbs. TgTCEA-b polypeptides showed approximately 77% identity to the petal TgTCEA. Functional characterization of the recombinant enzyme verified that TgTCEA-b encoded the TCEA. Moreover, the TgTCEA-b was found to be localized to plastids, as found for the petal TgTCEA. Transcript analysis revealed that TgTCEA-b was functionally transcribed in the bulb scales, unlike the TgTCEA gene, whose transcripts were absent there. In contrast, TgTCEA-b transcripts were in the minority in other tissues where TgTCEA transcripts were dominant, indicating a tissue preference for the transcription of those isozyme genes.

glucose ester, lactone-forming carboxylesterase, tulipalin, tuliposide, tuliposide-converting enzyme

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