دورية أكاديمية
Mechanoresponsive Protein Crystals for NADH Recycling in Multicycle Enzyme Reactions.
| العنوان: | Mechanoresponsive Protein Crystals for NADH Recycling in Multicycle Enzyme Reactions. |
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| المؤلفون: | Yekta R; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077., Xiong X; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077., Li J; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077., Heater BS; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077., Lee MM; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077., Chan MK; School of Life Sciences & Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin, Hong Kong S.A.R. 999077. |
| المصدر: | Journal of the American Chemical Society [J Am Chem Soc] 2024 Jul 17; Vol. 146 (28), pp. 18817-18822. Date of Electronic Publication: 2024 Jul 05. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington, DC : American Chemical Society Original Publication: Easton, Pa. [etc.] |
| مواضيع طبية MeSH: | NAD*/metabolism , NAD*/chemistry , Formate Dehydrogenases*/metabolism , Formate Dehydrogenases*/chemistry, Leucine Dehydrogenase/metabolism ; Leucine Dehydrogenase/chemistry ; Crystallization ; Enzymes, Immobilized/chemistry ; Enzymes, Immobilized/metabolism ; Models, Molecular |
| مستخلص: | NAD(H)-dependent enzymes play a crucial role in the biosynthesis of pharmaceuticals and fine chemicals, but the limited recyclability of the NAD(H) cofactor hinders its more general application. Here, we report the generation of mechano-responsive PEI-modified Cry3Aa protein crystals and their use for NADH recycling over multiple reaction cycles. For demonstration of its practical utility, a complementary Cry3Aa protein particle containing genetically encoded and co-immobilized formate dehydrogenase for NADH regeneration and leucine dehydrogenase for catalyzing the NADH-dependent l- tert -leucine (l- tert -Leu) biosynthesis has been produced. When combined with the PEI-modified Cry3Aa crystal, the resultant reaction system could be used for the efficient biosynthesis of l- tert -Leu for up to 21 days with a 10.5-fold improvement in the NADH turnover number. |
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| المشرفين على المادة: | 0U46U6E8UK (NAD) EC 1.17.1.9 (Formate Dehydrogenases) EC 1.4.1.9 (Leucine Dehydrogenase) 0 (Enzymes, Immobilized) |
| تواريخ الأحداث: | Date Created: 20240705 Date Completed: 20240717 Latest Revision: 20240722 |
| رمز التحديث: | 20240722 |
| مُعرف محوري في PubMed: | PMC11258682 |
| DOI: | 10.1021/jacs.4c04725 |
| PMID: | 38968608 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-5126 |
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| DOI: | 10.1021/jacs.4c04725 |