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CC Hydrolases for Biocatalysis
Although CC bond hydrolases are distributed widely in Nature, they has as yet have received only limited attention in the area of biocatalysis compared to their counterpart the C‐heteroatom hydrolases, such as lipases and proteases. However, the substrate range of CC hydrolases, and their non‐depe...
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Published in: | Advanced synthesis & catalysis 2013-06, Vol.355 (9), p.1677-1691 |
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description | Although CC bond hydrolases are distributed widely in Nature, they has as yet have received only limited attention in the area of biocatalysis compared to their counterpart the C‐heteroatom hydrolases, such as lipases and proteases. However, the substrate range of CC hydrolases, and their non‐dependence on cofactors, suggest that these enzymes may have considerable potential for applications in synthesis. In addition, hydrolases such as the β‐diketone hydrolase from Rhodococcus (OCH) are known, that catalyse the formation of interesting chiral intermediates. Further enzymes, such as kynureninase and a meta‐cleavage product hydrolase (MhpC), are able to catalyse carbon‐carbon bond formation, suggesting wider applications in biocatalysis than previously envisaged. In this review, the distribution, catalytic characteristics and applications of CC hydrolases are described, with a view to assessing their potentialfor use in biocatalytic processes in the future. |
doi_str_mv | 10.1002/adsc.201300232 |
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However, the substrate range of CC hydrolases, and their non‐dependence on cofactors, suggest that these enzymes may have considerable potential for applications in synthesis. In addition, hydrolases such as the β‐diketone hydrolase from Rhodococcus (OCH) are known, that catalyse the formation of interesting chiral intermediates. Further enzymes, such as kynureninase and a meta‐cleavage product hydrolase (MhpC), are able to catalyse carbon‐carbon bond formation, suggesting wider applications in biocatalysis than previously envisaged. In this review, the distribution, catalytic characteristics and applications of CC hydrolases are described, with a view to assessing their potentialfor use in biocatalytic processes in the future.</description><identifier>ISSN: 1615-4150</identifier><identifier>EISSN: 1615-4169</identifier><identifier>DOI: 10.1002/adsc.201300232</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Anabaena ; Aspergillus ; asymmetric catalysis ; biotransformations ; Bonding ; Carbon-carbon composites ; Catalysis ; CC hydrolysis ; Enzymes ; hydrolases ; Rhodococcus ; Synthesis</subject><ispartof>Advanced synthesis & catalysis, 2013-06, Vol.355 (9), p.1677-1691</ispartof><rights>Copyright © 2013 WILEY‐VCH Verlag GmbH & Co. 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In this review, the distribution, catalytic characteristics and applications of CC hydrolases are described, with a view to assessing their potentialfor use in biocatalytic processes in the future.</description><subject>Anabaena</subject><subject>Aspergillus</subject><subject>asymmetric catalysis</subject><subject>biotransformations</subject><subject>Bonding</subject><subject>Carbon-carbon composites</subject><subject>Catalysis</subject><subject>CC hydrolysis</subject><subject>Enzymes</subject><subject>hydrolases</subject><subject>Rhodococcus</subject><subject>Synthesis</subject><issn>1615-4150</issn><issn>1615-4169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqFkLFOwzAQQC0EEqWwMpeNJeVsx7E9tgFaUAUDINgsx7GlQEqKrxXke_gQPolfoFVQxcZ0d9J7NzxCjikMKQA7syW6IQPK1wdnO6RHMyqSlGZ6d7sL2CcHiM8AVCope-Qk__78ygfTtoxNbdHjIDRxMK4aZ5e2brHCQ7IXbI3-6Hf2ycPlxX0-TWa3k6t8NEsc15IlqqBSaJup0paUWygKroUvFAPNAwuSK7DeSe-hkEoHKpwTzEqmy6BBFJL3yWn3dxGbt5XHpZlX6Hxd21ffrNDQlGklVJaqNTrsUBcbxOiDWcRqbmNrKJhNC7NpYbYt1oLuhPeq9u0_tBmd3-V_3aRzK1z6j61r44vJJJfCPN5MzPQpzceT68xo_gNGOnFJ</recordid><startdate>20130617</startdate><enddate>20130617</enddate><creator>Siirola, Elina</creator><creator>Frank, Annika</creator><creator>Grogan, Gideon</creator><creator>Kroutil, Wolfgang</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope></search><sort><creationdate>20130617</creationdate><title>CC Hydrolases for Biocatalysis</title><author>Siirola, Elina ; Frank, Annika ; Grogan, Gideon ; Kroutil, Wolfgang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3972-8b1759a68dad13a0bb395eb82093f2f7380aec7ee0b789f15cc52a729df905b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Anabaena</topic><topic>Aspergillus</topic><topic>asymmetric catalysis</topic><topic>biotransformations</topic><topic>Bonding</topic><topic>Carbon-carbon composites</topic><topic>Catalysis</topic><topic>CC hydrolysis</topic><topic>Enzymes</topic><topic>hydrolases</topic><topic>Rhodococcus</topic><topic>Synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siirola, Elina</creatorcontrib><creatorcontrib>Frank, Annika</creatorcontrib><creatorcontrib>Grogan, Gideon</creatorcontrib><creatorcontrib>Kroutil, Wolfgang</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Advanced synthesis & catalysis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siirola, Elina</au><au>Frank, Annika</au><au>Grogan, Gideon</au><au>Kroutil, Wolfgang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CC Hydrolases for Biocatalysis</atitle><jtitle>Advanced synthesis & catalysis</jtitle><addtitle>Adv. Synth. Catal</addtitle><date>2013-06-17</date><risdate>2013</risdate><volume>355</volume><issue>9</issue><spage>1677</spage><epage>1691</epage><pages>1677-1691</pages><issn>1615-4150</issn><eissn>1615-4169</eissn><abstract>Although CC bond hydrolases are distributed widely in Nature, they has as yet have received only limited attention in the area of biocatalysis compared to their counterpart the C‐heteroatom hydrolases, such as lipases and proteases. However, the substrate range of CC hydrolases, and their non‐dependence on cofactors, suggest that these enzymes may have considerable potential for applications in synthesis. In addition, hydrolases such as the β‐diketone hydrolase from Rhodococcus (OCH) are known, that catalyse the formation of interesting chiral intermediates. Further enzymes, such as kynureninase and a meta‐cleavage product hydrolase (MhpC), are able to catalyse carbon‐carbon bond formation, suggesting wider applications in biocatalysis than previously envisaged. In this review, the distribution, catalytic characteristics and applications of CC hydrolases are described, with a view to assessing their potentialfor use in biocatalytic processes in the future.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/adsc.201300232</doi><tpages>15</tpages></addata></record> |
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subjects | Anabaena Aspergillus asymmetric catalysis biotransformations Bonding Carbon-carbon composites Catalysis CC hydrolysis Enzymes hydrolases Rhodococcus Synthesis |
title | CC Hydrolases for Biocatalysis |
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