Zobrazeno 1 - 6 of 6 pro vyhledávání: '"Matthew R, Bauerle"'
1
Analysis of RNA Methylation by Phylogenetically Diverse Cfr Radical S-Adenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme
Autor: Squire J. Booker, Ryan J. Martinie, Carsten Krebs, Matthew R. Bauerle, Mohamed Almarei, James D. Gumkowski, Patrick S. Corrigan, Alexey Silakov, Juan Pan, Amie K. Boal
Publikováno v: Biochemistry. 58:3169-3184
Cfr is a radical S-adenosylmethionine (SAM) RNA methylase linked to multidrug antibiotic resistance in bacterial pathogens. It catalyzes a chemically challenging C-C bond-forming reaction to methylate C8 of A2503 (Escherichia coli numbering) of 23S r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f7c9590ed60eae307acd7841e8f2ed44
https://doi.org/10.1021/acs.biochem.9b00197
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2
Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein Cfr
Autor: Squire J. Booker, Matthew R. Bauerle, Tyler L. Grove
Publikováno v: Biochemistry. 57:4431-4439
Cfr is a radical S-adenosylmethionine (RS) methylase that appends methyl groups to C8 and C2 of adenosine 2503 in 23S ribosomal RNA. Methylation of C8 confers resistance to several classes of antibiotics that bind in or near the peptidyl transferase
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a07bde5e11423e2f840bb1583866ed0
https://doi.org/10.1021/acs.biochem.8b00347
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3
Analysis of RNA Methylation by Phylogenetically Diverse Cfr Radical
Autor: James D, Gumkowski, Ryan J, Martinie, Patrick S, Corrigan, Juan, Pan, Matthew R, Bauerle, Mohamed, Almarei, Squire J, Booker, Alexey, Silakov, Carsten, Krebs, Amie K, Boal
Publikováno v: Biochemistry
Cfr is a radical S-adenosylmethionine (SAM) RNA methylase linked to multi-drug antibiotic resistance in bacterial pathogens. It catalyzes a chemically challenging C-C-bond forming reaction to methylate C8 of A2503 [Escherichia coli (Ec) numbering) of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::79c386cf30fbc6dcbffbd07ca389d436
https://pubmed.ncbi.nlm.nih.gov/31246421
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4
Characterization of a Cross-Linked Protein–Nucleic Acid Substrate Radical in the Reaction Catalyzed by RlmN
Autor: Matthew I. Radle, Tyler L. Grove, Amie K. Boal, Alexey Silakov, Matthew R. Bauerle, Michael Green, Amy C. Rosenzweig, Squire J. Booker
Publikováno v: Journal of the American Chemical Society
RlmN and Cfr are methyltransferases/methylsynthases that belong to the radical S-adenosylmethionine superfamily of enzymes. RlmN catalyzes C2 methylation of adenosine 2503 (A2503) of 23S rRNA, while Cfr catalyzes C8 methylation of the exact same nucl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15105d2bee02115c4903db82cd2b1cac
http://europepmc.org/articles/PMC4227720
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5
Mechanistic diversity of radical S-adenosylmethionine (SAM)-dependent methylation
Autor: Matthew R. Bauerle, Squire J. Booker, Erica L. Schwalm
Publikováno v: The Journal of biological chemistry. 290(7)
Radical S-adenosylmethionine (SAM) enzymes use the oxidizing power of a 5'-deoxyadenosyl 5'-radical to initiate an amazing array of transformations, usually through the abstraction of a target substrate hydrogen atom. A common reaction of radical SAM
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2b2a0cf277de4dcd75c1b19b13264e2
https://pubmed.ncbi.nlm.nih.gov/25477520
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