A Novel Cellulase of the Mulberry Longicorn Beetle, Apriona germari, Dependent on N-Glycosylation for Enzymatic Activity

  • Lee, Seong-Jin (College of Natural Resources and Life Science, Dong-A University) ;
  • Kim, Seong-Ryul (College of Natural Resources and Life Science, Dong-A University) ;
  • Yoon, Hyung-Joo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technolog) ;
  • Kim, IK-Soo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technolog) ;
  • Lee, Kwang-Sik (College of Natural Resources and Life Science, Dong-A University) ;
  • Je, Yeon-Ho (School of Agricultural Biotechnology, Seoul National University) ;
  • Lee, Sang-Mong (Department of Sericultural and Entomological Biology, Miryang National University) ;
  • Seo, Sook-Jae (Division of Life Science, Gyeongsang National University) ;
  • Sohn, Hung-Dae (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University)
  • Published : 2003.04.01

Abstract

A novel -1, 4-endoglucanase (EGase, EC 3.2.1.4) cDNA belonging to glycoside hydrolase family (GHF) 45 was cloned from the mulberry longicorn beetle, Apriona germari. The cDNA encoding EGase of A. germari (Ag-EGase) is 711 base pairs long with an open reading frame of 237 amino acid residues. The deduced protein sequence of Ag-EGase showed 54% and 48% identity to phytophagous beetle Phaedon cochleariae and termite Reticulitermes speratus hindgut symbiont, respectively. (omitted)

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