Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Claire L. Windle"'
Autor:
Arwen R. Pearson, Katie J. Simmons, Adam Nelson, Chi H. Trinh, James R. Ault, Alan Berry, Claire L. Windle
Natural enzymes are constructed from the twenty proteogenic amino acids, which may then require post-translational modification or the recruitment of coenzymes or metal ions to achieve catalytic function. Here, we demonstrate that expansion of the al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93032c2717ba309eb7fae3aa9f791c0a
https://europepmc.org/articles/PMC5347630/
https://europepmc.org/articles/PMC5347630/
Publikováno v:
Current opinion in chemical biology. 37
The introduction of fluorine has been widely exploited to tune the biological functions of small molecules. Indeed, around 20% of leading drugs contain at least one fluorine atom. Yet, despite profound effects of fluorination on conformation, there i
Autor:
Arwen R. Pearson, Thomas Harman, Thomas Woodhall, Adam D. Daniels, Adam Nelson, Jennifer Stockwell, Alan Berry, Tomas Lebl, Claire L. Windle, Keith R. Mulholland, Chi H. Trinh
The catalysis of reactions involving fluoropyruvate as donor by N-acetyl neuraminic acid lyase (NAL) variants was investigated. Under kinetic control, the wild-type enzyme catalysed the reaction between fluoropyruvate and N-acetyl mannosamine to give
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85b4e7305d5331e56a3201123957266d
https://eprints.whiterose.ac.uk/91457/8/c5ob02037a.pdf
https://eprints.whiterose.ac.uk/91457/8/c5ob02037a.pdf
Publikováno v:
The FASEB Journal. 29
Autor:
Arwen R. Pearson, James R. Ault, Adam Nelson, Claire L. Windle, N. Timms, Chi H. Trinh, Alan Berry, Anna Polyakova
Publikováno v:
Chembiochem
Chemical modification has been used to introduce the unnatural amino acid γ-thialysine in place of the catalytically important Lys165 in the enzyme N-acetylneuraminic acid lyase (NAL). The Staphylococcus aureus nanA gene, encoding NAL, was cloned an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5edfde1776b666d4b80c7ad34d335fae
Autor:
Arwen R. Pearson, Anna Polyakova, James R. Ault, Chi H. Trinh, N. Timms, Adam Nelson, Alan Berry, Claire L. Windle
Publikováno v:
ChemBioChem. 14:401-401
Publikováno v:
Current Opinion in Chemical Biology
Highlights • Aldolase enzymes are attractive candidates as biocatalysts. • Stability, stereoselectivity and substrate specificity of aldolases have been altered. • Aldolases with desirable activities have been produced using a variety of method