دورية أكاديمية
أعرض في EDS

Coenzyme A Thioester Intermediates as Platform Molecules in Cell-Free Chemical Biomanufacturing.

التفاصيل البيبلوغرافية
العنوان: Coenzyme A Thioester Intermediates as Platform Molecules in Cell-Free Chemical Biomanufacturing.
المؤلفون: Ducrot L; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramón 194, Donostia-San Sebastián, 20014, Spain., López IL; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramón 194, Donostia-San Sebastián, 20014, Spain., Orrego AH; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramón 194, Donostia-San Sebastián, 20014, Spain., López-Gallego F; Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramón 194, Donostia-San Sebastián, 20014, Spain.; Ikerbasque, Basque Foundation for Science, 48009, Bilbao, Spain.
المصدر: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Jan 15; Vol. 25 (2), pp. e202300673. Date of Electronic Publication: 2023 Nov 23.
نوع المنشور: Review; Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Wiley-VCH Verlag Country of Publication: Germany NLM ID: 100937360 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1439-7633 (Electronic) Linking ISSN: 14394227 NLM ISO Abbreviation: Chembiochem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Weinheim, Germany : Wiley-VCH Verlag, c2000-
مواضيع طبية MeSH: Acyl Coenzyme A*/metabolism , NAD*/metabolism, Coenzyme A/metabolism
مستخلص: The in vitro synthesis of Coenzyme A (CoA)-thioester intermediates opens new avenues to transform simple molecules into more complex and multifunctional ones by assembling cell-free biosynthetic cascades. In this review, we have systematically cataloged known CoA-dependent enzyme reactions that have been successfully implemented in vitro. To faciliate their identification, we provide their UniProt ID when available. Based on this catalog, we have organized enzymes into three modules: activation, modification, and removal. i) The activation module includes enzymes capable of fusing CoA with organic molecules. ii) The modification module includes enzymes capable of catalyzing chemical modifications in the structure of acyl-CoA intermediates. And iii) the removal module includes enzymes able to remove the CoA and release an organic molecule different from the one activated in the upstream. Based on these reactions, we constructed a reaction network that summarizes the most relevant CoA-dependent biosynthetic pathways reported until today. From the information available in the articles, we have plotted the total turnover number of CoA as a function of the product titer, observing a positive correlation between both parameters. Therefore, the success of a CoA-dependent in vitro pathway depends on its ability to regenerate CoA, but also to regenerate other cofactors such as NAD(P)H and ATP.
(© 2023 Wiley-VCH GmbH.)
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معلومات مُعتمدة: METACELL-878089 ERC-Co; IKERBASQUE; Maria de Maeztu Units of Excellence Program; MDM-2017-0720 Spanish State Research Agency
فهرسة مساهمة: Keywords: artificial metabolism; biocatalysis; cell-free pathways; cofactor recycling; multienzymatic cascades
المشرفين على المادة: 0 (Acyl Coenzyme A)
0U46U6E8UK (NAD)
SAA04E81UX (Coenzyme A)
تواريخ الأحداث: Date Created: 20231123 Date Completed: 20240117 Latest Revision: 20240326
رمز التحديث: 20240327
DOI: 10.1002/cbic.202300673
PMID: 37994376
قاعدة البيانات: MEDLINE
الوصف
تدمد:1439-7633
DOI:10.1002/cbic.202300673