Protein Residues That Control the Reaction Trajectory in S-Adenosylmethionine Radical Enzymes: Mutagenesis of Asparagine 153 and Aspartate 155 in Escherichia coli Biotin Synthase
Author:
Affiliation:
1. Department of Chemistry, University of Hawaii at Manoa, Honolulu, Hawaii 96822
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi8022569
Reference33 articles.
1. The novel structure and chemistry of iron–sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase
2. Biosynthesis of biotin and lipoic acid
3. Biotin Synthase Mechanism: Evidence for Hydrogen Transfer from the Substrate into Deoxyadenosine
4. Spectroscopic Changes during a Single Turnover of Biotin Synthase: Destruction of a [2Fe-2S] Cluster Accompanies Sulfur Insertion
5. 9-Mercaptodethiobiotin Is Formed as a Competent Catalytic Intermediate byEscherichia coliBiotin Synthase†
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1. Investigation of (S)-(−)-Acidomycin: A Selective Antimycobacterial Natural Product That Inhibits Biotin Synthase;ACS Infectious Diseases;2019-01-17
2. Purification, Characterization, and Biochemical Assays of Biotin Synthase From Escherichia coli;Methods in Enzymology;2018
3. Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme;Journal of the American Chemical Society;2017-08-22
4. Tryptophan Lyase (NosL): A Cornucopia of 5′-Deoxyadenosyl Radical Mediated Transformations;Journal of the American Chemical Society;2016-12-08
5. SPASM and Twitch Domains in S-Adenosylmethionine (SAM) Radical Enzymes;Journal of Biological Chemistry;2015-02
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