التفاصيل البيبلوغرافية
| العنوان: |
A new NAD -dependent glyceraldehyde dehydrogenase obtained by rational design of l -lactaldehyde dehydrogenase from Escherichia coli. |
| المؤلفون: |
Wu, Xing, Xu, Lin, Yan, Ming |
| المصدر: |
Bioscience, Biotechnology & Biochemistry; Dec2016, Vol. 80 Issue 12, p2306-2310, 5p |
| مصطلحات موضوعية: |
L-Lactate dehydrogenase, ESCHERICHIA coli, ALDEHYDE dehydrogenase |
| مستخلص: |
NAD + -dependent glyceraldehyde dehydrogenases usually had lower activity in the nonphosphorylated Entner–Doudoroff (nED) pathway. In the present study, a new NAD + -dependent glyceraldehyde dehydrogenase was engineered froml-lactaldehyde dehydrogenase ofE. coli(EC: 1.2.1.22). Through comparison of the sequence alignment and the active center model, we found that a residue N286 ofl-lactaldehyde dehydrogenase contributed an important structure role to substrate identification. By free energy calculation, three mutations (N286E, N286H, N286T) were chosen to investigate the change of substrate specificity of the enzyme. All mutants were able to oxidate glyceraldehyde. Especially, N286T showed the highest activity of 1.1U/mg, which was 5-fold higher than the reported NAD + -dependent glyceraldehyde dehydrogenases, and 70% activity was retained at 55 °C after an hour. Compared tol-lactaldehyde, N286T had a one-third lowerKmvalue to glyceraldehyde. Molecular structure ofl-lactaldehyde dehydrogenase fromE. coli. [ABSTRACT FROM PUBLISHER] |
|
Copyright of Bioscience, Biotechnology & Biochemistry is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Supplemental Index |
