The novel R347g pathogenic mutation of aromatic amino acid decarboxylase provides additional molecular insights into enzyme catalysis and deficiency
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- 作者：Riccardo Montiolia ; 1 ; Alessandro Paiardinib ; 1 ; Manju A. Kurianc ; d ; Mirco Dindoa ; Giada Rossignolia ; Simon J.R. Healese ; f ; Simon Popef ; Carla Borri Voltattornia ; Mariarita Bertoldia ; mita.bertoldi@univr.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：PLP ; pyridoxal 5&prime ; -phosphate ; AADC ; aromatic amino acid decarboxylase ; HDC ; histidine decarboxylase ; DME ; dopa methyl ester ; ANS ; 1 ; 8-anilinonaphtalene sulfonic acid ; PMP ; pyridoxamine 5&prime ; -phosphate ; KD(PLP) ; equilibrium dissociation constant for PLP ; TNB ; 2 ; 4 ; 6-trinitrobenzene-1-sulfonic acid
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1864
- 期：6
- 页码：676-682
- 全文大小：663 K
文摘
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A novel mutation R347G associated with AADC deficiency is identified.
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Mutation R347G mainly affects the catalytic activity.
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Interactions of Arg347 with both Asp345 and Leu333 are missing in the R347G mutant.
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Mutation R347G alters the correct location of the external aldimine.
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Therapeutic guidelines are suggested for patients bearing mutations of Arg347.