Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis
The asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable...
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| Veröffentlicht in: | Catalysts 2019-10, Vol.9 (10), p.868 |
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| creator | Shah, Mihir V. Antoney, James Kang, Suk Woo Warden, Andrew C. Hartley, Carol J. Nazem-Bokaee, Hadi Jackson, Colin J. Scott, Colin |
| description | The asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. This review considers the cofactor F420-dependent enzyme families with the greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). The characterized F420-dependent reductions that have the potential for adaptation for biocatalysis are discussed, and the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ are considered. Further discussed are the recent advances in the production of cofactor F420 and its functional analog FO-5′-phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis are discussed. |
| doi_str_mv | 10.3390/catal9100868 |
| format | Article |
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These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. This review considers the cofactor F420-dependent enzyme families with the greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). The characterized F420-dependent reductions that have the potential for adaptation for biocatalysis are discussed, and the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ are considered. Further discussed are the recent advances in the production of cofactor F420 and its functional analog FO-5′-phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis are discussed.</description><identifier>ISSN: 2073-4344</identifier><identifier>EISSN: 2073-4344</identifier><identifier>DOI: 10.3390/catal9100868</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Alcohol ; Asymmetry ; Carbon ; Catalysts ; Chemical reactions ; Chemical reduction ; Dehydrogenases ; Electrochemical analysis ; Enzymes ; Glucose ; Imines ; Ketones ; Nicotinamide ; Oxidation ; Physiology ; Proteins ; Reducing agents ; Tuberculosis</subject><ispartof>Catalysts, 2019-10, Vol.9 (10), p.868</ispartof><rights>2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2168-d21b36175a8831b001a7fc5aa344e617879acda9d6d5be7265ec616b217d25693</citedby><cites>FETCH-LOGICAL-c2168-d21b36175a8831b001a7fc5aa344e617879acda9d6d5be7265ec616b217d25693</cites><orcidid>0000-0003-2683-9798 ; 0000-0002-1927-8040 ; 0000-0001-6110-6982 ; 0000-0003-4033-6898</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Shah, Mihir V.</creatorcontrib><creatorcontrib>Antoney, James</creatorcontrib><creatorcontrib>Kang, Suk Woo</creatorcontrib><creatorcontrib>Warden, Andrew C.</creatorcontrib><creatorcontrib>Hartley, Carol J.</creatorcontrib><creatorcontrib>Nazem-Bokaee, Hadi</creatorcontrib><creatorcontrib>Jackson, Colin J.</creatorcontrib><creatorcontrib>Scott, Colin</creatorcontrib><title>Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis</title><title>Catalysts</title><description>The asymmetric reduction of enoates, imines and ketones are among the most important reactions in biocatalysis. These reactions are routinely conducted using enzymes that use nicotinamide cofactors as reductants. The deazaflavin cofactor F420 also has electrochemical properties that make it suitable as an alternative to nicotinamide cofactors for use in asymmetric reduction reactions. However, cofactor F420-dependent enzymes remain under-explored as a resource for biocatalysis. This review considers the cofactor F420-dependent enzyme families with the greatest potential for the discovery of new biocatalysts: the flavin/deazaflavin-dependent oxidoreductases (FDORs) and the luciferase-like hydride transferases (LLHTs). The characterized F420-dependent reductions that have the potential for adaptation for biocatalysis are discussed, and the enzymes best suited for use in the reduction of oxidized cofactor F420 to allow cofactor recycling in situ are considered. Further discussed are the recent advances in the production of cofactor F420 and its functional analog FO-5′-phosphate, which remains an impediment to the adoption of this family of enzymes for industrial biocatalytic processes. Finally, the prospects for the use of this cofactor and dependent enzymes as a resource for industrial biocatalysis are discussed.</description><subject>Alcohol</subject><subject>Asymmetry</subject><subject>Carbon</subject><subject>Catalysts</subject><subject>Chemical reactions</subject><subject>Chemical reduction</subject><subject>Dehydrogenases</subject><subject>Electrochemical analysis</subject><subject>Enzymes</subject><subject>Glucose</subject><subject>Imines</subject><subject>Ketones</subject><subject>Nicotinamide</subject><subject>Oxidation</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Reducing agents</subject><subject>Tuberculosis</subject><issn>2073-4344</issn><issn>2073-4344</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNpNkE1Lw0AQhhdRsGhv_oAFr0b3I_sRb7W2KhQEsUcJm90JpDTZuJtC4693az10LjO8vDPz8CJ0Q8k95wV5sGYw24ISoqU-QxNGFM9ynufnJ_Mlmsa4IakKyjUVE_Q197Wxgw94mTOSPUMPnYNuwIvuZ2whPuJZh9dJCtli3299AIc_IPpdsIDrtDaLY9vCEBqbdOf3-KnxfyhjbOI1uqjNNsL0v1-h9XLxOX_NVu8vb_PZKrOMSp05RisuqRJGa04rQqhRtRXGJGRIulaFsc4UTjpRgWJSgJVUVowqx4Qs-BW6Pd7tg__eQRzKTSLs0suSiVwJKok-uO6OLht8jAHqsg9Na8JYUlIeMixPM-S_RM9jnQ</recordid><startdate>20191020</startdate><enddate>20191020</enddate><creator>Shah, Mihir V.</creator><creator>Antoney, James</creator><creator>Kang, Suk Woo</creator><creator>Warden, Andrew C.</creator><creator>Hartley, Carol J.</creator><creator>Nazem-Bokaee, Hadi</creator><creator>Jackson, Colin J.</creator><creator>Scott, Colin</creator><general>MDPI AG</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>KB.</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><orcidid>https://orcid.org/0000-0003-2683-9798</orcidid><orcidid>https://orcid.org/0000-0002-1927-8040</orcidid><orcidid>https://orcid.org/0000-0001-6110-6982</orcidid><orcidid>https://orcid.org/0000-0003-4033-6898</orcidid></search><sort><creationdate>20191020</creationdate><title>Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis</title><author>Shah, Mihir V. ; 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| subjects | Alcohol Asymmetry Carbon Catalysts Chemical reactions Chemical reduction Dehydrogenases Electrochemical analysis Enzymes Glucose Imines Ketones Nicotinamide Oxidation Physiology Proteins Reducing agents Tuberculosis |
| title | Cofactor F420-Dependent Enzymes: An Under-Explored Resource for Asymmetric Redox Biocatalysis |
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