N-glycosylation influences the catalytic activity of mosquito α-glucosidases associated with susceptibility or refractoriness to Lysinibacillus sphaericus

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• 作者：Nathaly Alexandre do Nascimento^a ; Lí ; gia Maria Ferreira^a ; Tatiany Patrí ; cia Romã ; o^a ; Darleide Maria da Conceiç ; ã ; o Correia^a ; Crhisllane Rafaele dos Santos Vasconcelos^b ; Antô ; nio Mauro Rezende^b ; Samara Graciane Costa^c ; Fernando Ariel Genta^c ; ^d ; Osvaldo Pompí ; lio de-Melo-Neto^b ; Maria Helena Neves Lobo Silva-Filha^a ; ^{mhneves@cpqam.fiocruz.br}
• 关键词：Cqm1 ; Aam1 ; Culex quinquefasciatus ; Aedes aegypti ; N-glycosylation ; Glucosidases
• 刊名：Insect Biochemistry and Molecular Biology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：81
• 期：Complete
• 页码：62-71
• 全文大小：1473 K
• 卷排序：81

文摘

Mutant proteins in N-glycosylation sites, that were abolished in Aam1 or inserted into Cqm1, were generated. Aam1 has four N-glycosylated sites localized externally on its structure, while N-glycans seemed absent from Cqm1. Aam1 has higher catalytic efficiency than Cqm1, and carbohydrates removal from Aam1 changed the catalytic activity. N-glycosylation can enhance the functional diversity of these related orthologs proteins.