Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites.
Biomimicry valuably allows the understanding of the essential chemical components required to recapitulate biological function, yet direct strategies for evaluating the roles of amino acids in proteins can be limited by access to suitable, subtly-altered unnatural variants. Here we describe a strate...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
ACS Publications
2017
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| _version_ | 1826292627880804352 |
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| author | Dadová, J Wu, K Isenegger, P Errey, J Bernardes, G Chalker, J Raich, L Rovira, C Davis, B |
| author_facet | Dadová, J Wu, K Isenegger, P Errey, J Bernardes, G Chalker, J Raich, L Rovira, C Davis, B |
| author_sort | Dadová, J |
| collection | OXFORD |
| description | Biomimicry valuably allows the understanding of the essential chemical components required to recapitulate biological function, yet direct strategies for evaluating the roles of amino acids in proteins can be limited by access to suitable, subtly-altered unnatural variants. Here we describe a strategy for dissecting the role of histidine residues in enzyme active sites using unprecedented, chemical, post-translational side-chain-β,γ C-N bond formation. Installation of dehydroalanine (as a "tag") allowed the testing of nitrogen conjugate nucleophiles in "aza-Michael"-1,4-additions (to "modify"). This allowed the creation of a regioisomer of His (iso-His, His |
| first_indexed | 2024-03-07T03:17:37Z |
| format | Journal article |
| id | oxford-uuid:b654e241-1255-4019-8004-205a2c195072 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:17:37Z |
| publishDate | 2017 |
| publisher | ACS Publications |
| record_format | dspace |
| spelling | oxford-uuid:b654e241-1255-4019-8004-205a2c1950722022-03-27T04:40:15ZPrecise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b654e241-1255-4019-8004-205a2c195072EnglishSymplectic Elements at OxfordACS Publications2017Dadová, JWu, KIsenegger, PErrey, JBernardes, GChalker, JRaich, LRovira, CDavis, BBiomimicry valuably allows the understanding of the essential chemical components required to recapitulate biological function, yet direct strategies for evaluating the roles of amino acids in proteins can be limited by access to suitable, subtly-altered unnatural variants. Here we describe a strategy for dissecting the role of histidine residues in enzyme active sites using unprecedented, chemical, post-translational side-chain-β,γ C-N bond formation. Installation of dehydroalanine (as a "tag") allowed the testing of nitrogen conjugate nucleophiles in "aza-Michael"-1,4-additions (to "modify"). This allowed the creation of a regioisomer of His (iso-His, His |
| spellingShingle | Dadová, J Wu, K Isenegger, P Errey, J Bernardes, G Chalker, J Raich, L Rovira, C Davis, B Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title | Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title_full | Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title_fullStr | Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title_full_unstemmed | Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title_short | Precise probing of residue roles by post-translational β,γ-C,N aza-Michael mutagenesis in enzyme active sites. |
| title_sort | precise probing of residue roles by post translational β γ c n aza michael mutagenesis in enzyme active sites |
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