Formate Dehydrogenase: Recent Developments for NADH and NADPH Recycling in Biocatalysis
Formate dehydrogenases (FDHs) catalyze the oxidation of formate to CO2 while reducing NAD(P)+ to NAD(P)H and are classified into two main classes: metal‐dependent (Mo‐ or W‐containing) and metal‐independent FDHs. The latter are oxygen‐tolerant and relevant as a cofactor regeneration system for vario...
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| description | Formate dehydrogenases (FDHs) catalyze the oxidation of formate to CO2 while reducing NAD(P)+ to NAD(P)H and are classified into two main classes: metal‐dependent (Mo‐ or W‐containing) and metal‐independent FDHs. The latter are oxygen‐tolerant and relevant as a cofactor regeneration system for various bioprocesses and gained more and more attention due to their ability to catalyze the reverse CO2 reduction. This review gives an overview of metal‐independent FDHs, the recent advances made in this field, and their relevance for future applications in biocatalysis. This includes the exploitation of novel FDHs which have altered co‐substrate specificity as well as enzyme engineering approaches to improve process stability and general performance.
Formate dehydrogenases (FDHs) are widely utilized to drive various biocatalysts for the production of valuable compounds. Recent advancements in enzyme engineering have enhanced the functionality of metal‐independent FDHs, increasing their applicability and suitability for specific bioprocesses. This review highlights the latest progress in FDH research, with a particular focus on structural insights, engineering progress, and applications in bioprocesses. |
| doi_str_mv | 10.1002/cctc.202401021 |
| format | Article |
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Formate dehydrogenases (FDHs) are widely utilized to drive various biocatalysts for the production of valuable compounds. Recent advancements in enzyme engineering have enhanced the functionality of metal‐independent FDHs, increasing their applicability and suitability for specific bioprocesses. This review highlights the latest progress in FDH research, with a particular focus on structural insights, engineering progress, and applications in bioprocesses.</description><subject>biocatalysis</subject><subject>biotransformation</subject><subject>Carbon dioxide</subject><subject>enzyme cascade</subject><subject>Formate dehydrogenase</subject><subject>Nicotinamide adenine dinucleotide</subject><subject>Oxidation</subject><subject>oxidoreductase</subject><subject>protein engineering</subject><issn>1867-3880</issn><issn>1867-3899</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNqFkN1LwzAUxYMoOKevPgd87rz5aNP6NqtzwlCRiY8hTZPZ0TUz6ZT-97ZM5qNP93D5nftxELokMCEA9FrrVk8oUA4EKDlCI5ImImJplh0fdAqn6CyENUCSMRGP0PvM-Y1qDb4zH13p3co0Kpgb_Gq0adq--2Vqt930OmDrPH6a3s2xaspBvMwHrNN11axw1eDbymnVqroLVThHJ1bVwVz81jF6m90v83m0eH54zKeLSFNOSWSJMVz1p_A0ZqCTpEj7B6wytkwJKVTJ46SIuRYWhCAxcKV1QVKWaJsB6JiN0dV-7ta7z50JrVy7nW_6lZIRKoBlQmQ9NdlT2rsQvLFy66uN8p0kIIfw5BCePITXG7K94buqTfcPLfN8mf95fwDMZnID</recordid><startdate>20241111</startdate><enddate>20241111</enddate><creator>Maier, Artur</creator><creator>Mguni, Lindelo M.</creator><creator>Ngo, Anna C. R.</creator><creator>Tischler, Dirk</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0003-0132-4085</orcidid><orcidid>https://orcid.org/0000-0002-6288-2403</orcidid><orcidid>https://orcid.org/0000-0003-0718-6787</orcidid><orcidid>https://orcid.org/0000-0001-5684-6978</orcidid></search><sort><creationdate>20241111</creationdate><title>Formate Dehydrogenase: Recent Developments for NADH and NADPH Recycling in Biocatalysis</title><author>Maier, Artur ; Mguni, Lindelo M. ; Ngo, Anna C. R. ; Tischler, Dirk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2421-f1ee4a93748530c66b8024faefd811bad456b54c7f0771504accb1836cf900c53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>biocatalysis</topic><topic>biotransformation</topic><topic>Carbon dioxide</topic><topic>enzyme cascade</topic><topic>Formate dehydrogenase</topic><topic>Nicotinamide adenine dinucleotide</topic><topic>Oxidation</topic><topic>oxidoreductase</topic><topic>protein engineering</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maier, Artur</creatorcontrib><creatorcontrib>Mguni, Lindelo M.</creatorcontrib><creatorcontrib>Ngo, Anna C. R.</creatorcontrib><creatorcontrib>Tischler, Dirk</creatorcontrib><collection>Wiley-Blackwell Open Access Collection</collection><collection>Wiley Free Archive</collection><collection>CrossRef</collection><jtitle>ChemCatChem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maier, Artur</au><au>Mguni, Lindelo M.</au><au>Ngo, Anna C. R.</au><au>Tischler, Dirk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formate Dehydrogenase: Recent Developments for NADH and NADPH Recycling in Biocatalysis</atitle><jtitle>ChemCatChem</jtitle><date>2024-11-11</date><risdate>2024</risdate><volume>16</volume><issue>21</issue><epage>n/a</epage><issn>1867-3880</issn><eissn>1867-3899</eissn><abstract>Formate dehydrogenases (FDHs) catalyze the oxidation of formate to CO2 while reducing NAD(P)+ to NAD(P)H and are classified into two main classes: metal‐dependent (Mo‐ or W‐containing) and metal‐independent FDHs. The latter are oxygen‐tolerant and relevant as a cofactor regeneration system for various bioprocesses and gained more and more attention due to their ability to catalyze the reverse CO2 reduction. This review gives an overview of metal‐independent FDHs, the recent advances made in this field, and their relevance for future applications in biocatalysis. This includes the exploitation of novel FDHs which have altered co‐substrate specificity as well as enzyme engineering approaches to improve process stability and general performance.
Formate dehydrogenases (FDHs) are widely utilized to drive various biocatalysts for the production of valuable compounds. Recent advancements in enzyme engineering have enhanced the functionality of metal‐independent FDHs, increasing their applicability and suitability for specific bioprocesses. This review highlights the latest progress in FDH research, with a particular focus on structural insights, engineering progress, and applications in bioprocesses.</abstract><cop>Weinheim</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1002/cctc.202401021</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0003-0132-4085</orcidid><orcidid>https://orcid.org/0000-0002-6288-2403</orcidid><orcidid>https://orcid.org/0000-0003-0718-6787</orcidid><orcidid>https://orcid.org/0000-0001-5684-6978</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | biocatalysis biotransformation Carbon dioxide enzyme cascade Formate dehydrogenase Nicotinamide adenine dinucleotide Oxidation oxidoreductase protein engineering |
| title | Formate Dehydrogenase: Recent Developments for NADH and NADPH Recycling in Biocatalysis |
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