Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors.
(Figure Presented) Structural "valid"-ation: The mechanism of enzyme-catalyzed glycosyl transfer with retention of anomeric configuration continues to baffle, a situation compounded by the lack of insightful 3-D structures of ternary enzyme complexes. Synthesis and multi-dimensional kineti...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2010
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| _version_ | 1797104385799487488 |
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| author | Errey, J Lee, S Gibson, R Martinez Fleites, C Barry, C Jung, P O'Sullivan, A Davis, B Davies, G |
| author_facet | Errey, J Lee, S Gibson, R Martinez Fleites, C Barry, C Jung, P O'Sullivan, A Davis, B Davies, G |
| author_sort | Errey, J |
| collection | OXFORD |
| description | (Figure Presented) Structural "valid"-ation: The mechanism of enzyme-catalyzed glycosyl transfer with retention of anomeric configuration continues to baffle, a situation compounded by the lack of insightful 3-D structures of ternary enzyme complexes. Synthesis and multi-dimensional kinetic analysis of validoxylamine derivatives are used to access the 3-D structure of a ternary complex (see picture; U = uridyl) providing insight into the geometry and donor-acceptor interplay at the glycosyltransfer site. © 2010 Wiley-VCH Verlag GmbH and. Co. KGaA. |
| first_indexed | 2024-03-07T06:33:06Z |
| format | Journal article |
| id | oxford-uuid:f6b39966-7a05-4758-a33e-9081d8a3c29e |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:33:06Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:f6b39966-7a05-4758-a33e-9081d8a3c29e2022-03-27T12:37:00ZMechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f6b39966-7a05-4758-a33e-9081d8a3c29eEnglishSymplectic Elements at Oxford2010Errey, JLee, SGibson, RMartinez Fleites, CBarry, CJung, PO'Sullivan, ADavis, BDavies, G(Figure Presented) Structural "valid"-ation: The mechanism of enzyme-catalyzed glycosyl transfer with retention of anomeric configuration continues to baffle, a situation compounded by the lack of insightful 3-D structures of ternary enzyme complexes. Synthesis and multi-dimensional kinetic analysis of validoxylamine derivatives are used to access the 3-D structure of a ternary complex (see picture; U = uridyl) providing insight into the geometry and donor-acceptor interplay at the glycosyltransfer site. © 2010 Wiley-VCH Verlag GmbH and. Co. KGaA. |
| spellingShingle | Errey, J Lee, S Gibson, R Martinez Fleites, C Barry, C Jung, P O'Sullivan, A Davis, B Davies, G Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title | Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title_full | Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title_fullStr | Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title_full_unstemmed | Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title_short | Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. |
| title_sort | mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors |
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