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Title of Journal: Mol Cell Biochem

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Abbravation: Molecular and Cellular Biochemistry

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Springer US

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DOI

10.1007/BF03224223

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1573-4919

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Bioinformatic and biochemical studies point to AAG

Authors: Jakub Sikora Jana Uřinovská Filip Majer Helena Poupětová Jitka Hlavatá Marta Kostrouchová Jana Ledvinová Martin Hřebíček
Publish Date: 2010/03/27
Volume: 341, Issue: 1-2, Pages: 51-63
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Abstract

Human acid αglucosidase GAA EC 32120 is a lysosomal enzyme that belongs to the glycoside hydrolase family 31 GH31 and catalyses the hydrolysis of α14 and α16glucosidic linkages at acid pH Hereditary deficiency of GAA results in lysosomal glycogen storage disease type II GSDII Pompe disease The aim of this study was to assess GH31 proteins in Caenorhabditis elegans C elegans to identify the ortholog of human GAA Bioinformatic searches for GAA ortholog in C elegans genome revealed four acid alphaglucosidaserelated aagr1–4 genes Multiple sequence alignment of AAGRs with other GH31 proteins demonstrated their evolutionary conservation Phylogenetic analyses suggested clustering of AAGR1 and 2 with acidactive and AAGR3 and 4 with neutralactive GH31 enzymes In order to prove the AAGRs’ predicted αglucosidase activity we performed RNA interference of all four aagr genes The impact on the αglucosidase activity was evaluated at pH 40 acid and pH 65 neutral with or without the inhibitor acarbose AAGR1 and 2 expressed acidic αglucosidase activity on the contrary AAGR3 not 4 represented the predominant neutral αglucosidase activity in C elegans Similar results were obtained in each of aagr1 and 4 deletion mutants Moreover based on our structural models of AAGRs and these biochemical experiments we hypothesize that the enzymatic sensitivity of AAGR2 and human maltaseglucoamylase to the inhibitor acarbose is associated with a tyrosine residue in the GH31 active site whereas acarbose resistance of AAGR1 and human GAA is associated with the corresponding tryptophane in the active site Acidactive AAGR1 may thus represent the ortholog of human GAA in C elegansThe authors would like to thank Dr Karel Jelinek Mathematical and Statistical Projects Prague Czech Republic for initial homology modelling of AAGRs on the basis of YicI template We would also like to thank Eliska Machalova for technical assistance This study was funded by the research project 0021620806 from the Ministry of Education Youth and Sports of the Czech Republic and in part by the grant 304/08/0970 from the Czech Science Foundation

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