Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity.
Structural and mechanistic studies on the crotonase superfamily (CS) are reviewed with the aim of illustrating how a conserved structural platform can enable catalysis of a very wide range of reactions. Many CS reactions have precedent in the 'carbonyl' chemistry of organic synthesis; they...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2008
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| _version_ | 1826260313886949376 |
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| author | Hamed, R Batchelar, E Clifton, I Schofield, C |
| author_facet | Hamed, R Batchelar, E Clifton, I Schofield, C |
| author_sort | Hamed, R |
| collection | OXFORD |
| description | Structural and mechanistic studies on the crotonase superfamily (CS) are reviewed with the aim of illustrating how a conserved structural platform can enable catalysis of a very wide range of reactions. Many CS reactions have precedent in the 'carbonyl' chemistry of organic synthesis; they include alkene hydration/isomerization, aryl-halide dehalogenation, (de)carboxylation, CoA ester and peptide hydrolysis, fragmentation of beta-diketones and C-C bond formation, cleavage and oxidation. CS enzymes possess a canonical fold formed from repeated betabetaalpha units that assemble into two approximately perpendicular beta-sheets surrounded by alpha-helices. CS enzymes often, although not exclusively, oligomerize as trimers or dimers of trimers. Two conserved backbone NH groups in CS active sites form an oxyanion 'hole' that can stabilize enolate/oxyanion intermediates. The range and efficiency of known CS-catalyzed reactions coupled to their common structural platforms suggest that CS variants may have widespread utility in biocatalysis. |
| first_indexed | 2024-03-06T19:03:39Z |
| format | Journal article |
| id | oxford-uuid:1465369f-76bf-442a-9783-dfdb8642e520 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:03:39Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:1465369f-76bf-442a-9783-dfdb8642e5202022-03-26T10:19:35ZMechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1465369f-76bf-442a-9783-dfdb8642e520EnglishSymplectic Elements at Oxford2008Hamed, RBatchelar, EClifton, ISchofield, CStructural and mechanistic studies on the crotonase superfamily (CS) are reviewed with the aim of illustrating how a conserved structural platform can enable catalysis of a very wide range of reactions. Many CS reactions have precedent in the 'carbonyl' chemistry of organic synthesis; they include alkene hydration/isomerization, aryl-halide dehalogenation, (de)carboxylation, CoA ester and peptide hydrolysis, fragmentation of beta-diketones and C-C bond formation, cleavage and oxidation. CS enzymes possess a canonical fold formed from repeated betabetaalpha units that assemble into two approximately perpendicular beta-sheets surrounded by alpha-helices. CS enzymes often, although not exclusively, oligomerize as trimers or dimers of trimers. Two conserved backbone NH groups in CS active sites form an oxyanion 'hole' that can stabilize enolate/oxyanion intermediates. The range and efficiency of known CS-catalyzed reactions coupled to their common structural platforms suggest that CS variants may have widespread utility in biocatalysis. |
| spellingShingle | Hamed, R Batchelar, E Clifton, I Schofield, C Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title_full | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title_fullStr | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title_full_unstemmed | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title_short | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
| title_sort | mechanisms and structures of crotonase superfamily enzymes how nature controls enolate and oxyanion reactivity |
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