کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
11015546 | 1782694 | 2018 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Multiple mutations in the aglycone binding pocket to convert the substrate specificity of dalcochinase to linamarase
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Multiple mutations in the aglycone binding pocket to convert the substrate specificity of dalcochinase to linamarase Multiple mutations in the aglycone binding pocket to convert the substrate specificity of dalcochinase to linamarase](/preview/png/11015546.png)
چکیده انگلیسی
Dalcochinase from Dalbergia cochinchinensis Pierre and linamarase from Manihot esculenta Crantz are β-glucosidases which share 47% sequence identity, but show distinct substrate specificities in hydrolysis and transglucosylation. Previously, three amino acid residues of dalcochinase, namely I185, N189 and V255, were identified as being important for determining substrate specificity. In this study, kinetic analysis of the ensuing double and triple mutants of dalcochinase showed that only those containing the 185A mutation could appreciably hydrolyze linamarin as well as transfer glucose to 2-methyl-2-propanol. So, the space provided by the I185A mutation appeared to be a prerequisite for accommodation of the aglycone moiety containing three substituents at the carbinol carbon. However, quantitative analysis of the energy parameters revealed mostly antagonistic interactions between these mutations. In addition, the N189F mutant showed a potential for use in enzymatic synthesis of alkyl glucosides via transglucosylation and reverse hydrolysis reactions. Thus, substitution of only 2-3 key residues in the aglycone binding pocket of dalcochinase could convert its specificities to that of linamarase, as well as to be suitable for any chosen hydrolytic or synthetic applications.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 504, Issue 4, 12 October 2018, Pages 647-653
Journal: Biochemical and Biophysical Research Communications - Volume 504, Issue 4, 12 October 2018, Pages 647-653
نویسندگان
Nusra Tongtubtim, Pornpanna Thenchartanan, Khakhanang Ratananikom, Khuanjarat Choengpanya, Jisnuson Svasti, Prachumporn T. Kongsaeree,