Journal article

Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase.

Y Zhou, X-W Lin, Y-R Zhang, Y-J Huang, C-H Zhang, Q Yang, H-Y Li, J-Q Yuan, J-A Cheng, R Xu, C Mao, Z-R Zhu

Insect Mol Biol | Published : 2013

Abstract

Ceramidases are a group of enzymes that catalyse hydrolysis of ceramides to generate fatty acid and sphingosine. In this study, we report the cloning and characterization of the rice small brown planthopper Laodelphax striatellus neutral ceramidase (nCDase), LsnCer. LsnCer was identified by sequencing the transcriptome of L. striatellus and is a protein of 717 amino acids with a predicted molecular weight of 79.3 kDa. Similarly to other known nCDases, the optimum pH for LsnCer is 8.0 and the optimum temperature is 37 °C for its in vitro activity. LsnCer activity is inhibited by Zn(2+) significantly and Fe(2+) slightly. LsnCer has broad substrate specificity with a preference for ceramides wi..

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University of Melbourne Researchers