TAILIEUCHUNG - Báo cáo khoa học: Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm pheromone, from the astigmatid mite Carpoglyphus lactis (Acari: Carpoglyphidae)

Geraniol dehydrogenase (GeDH), which plays an important role in the bio-synthesis of neral, an alarm pheromone, was purified from the astigmatid miteCarpoglyphus lactis. The enzyme was obtained in an apparently homo-geneous and active form after 1879-fold purification through seven steps of chromatography. | ỊFEBS Journal Geraniol dehydrogenase the key enzyme in biosynthesis of the alarm pheromone from the astigmatid mite Carpoglyphus lactis Acari Carpoglyphidae Koji Noge1 Makiko Kato1 Naoki Mori1 Michihiko Kataoka1 Chihiro Tanaka2 Yuji Yamasue3 Ritsuo Nishida1 and Yasumasa Kuwahara1 1 Division of Applied Life Sciences Graduate Schoolof Agriculture Kyoto University Japan 2 Division of EnvironmentalScience and Technology Graduate Schoolof Agriculture Kyoto University Japan 3 Division of Agronomy and HorticulturalScience Graduate Schoolof Agriculture Kyoto University Japan Keywords alarm pheromone biosynthesis Carpoglyphus lactis geraniol dehydrogenase monomeric alcohol dehydrogenase Correspondence K. Noge Department of Entomology University of Arizona Tucson AZ 85721 USA Fax 1 520 621 1150 Tel 1 520 621 1328 E-mail noge@ Present address Department of Entomology University of Arizona Tucson AZ USA TDepartment of Bioscience and Biotechnology Faculty of BioenvironmentalScience Kyotogakuen University Kameoka Japan Database Nucleotide sequence data are available in the DDBJ EMBL GenBank databases under the accession numbers AB305641 and AB305642 Received 30 October 2007 revised 20 March 2008 accepted 25 March 2008 doi Geraniol dehydrogenase GeDH which plays an important role in the biosynthesis of neral an alarm pheromone was purified from the astigmatid mite Carpoglyphus lactis. The enzyme was obtained in an apparently homogeneous and active form after 1879-fold purification through seven steps of chromatography. Car. lactis GeDH was determined to be a monomer in its active form with a relative molecular mass of 42 800 which is a unique subunit structure in comparison with already established alcohol dehydrogenases. Car. lactis GeDH oxidized geraniol into geranial in the presence of NAD . NADP was ineffective as a cofactor suggesting that Car. lactis GeDH is an NAD -dependent alcohol dehydrogenase. The optimal pH and .

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