New standards for collecting and fitting steady state kinetic data

Scholarly Works

• Patra, S. K.; Douglas, J.; Wills, P. R.; Betts, L.; Qing, T. G.; Carter, C. W. A genomic database furnishes minimal functional glycyl-tRNA synthetases homologous to other, designed class II urzymes. Nucleic acids research 2024. doi:10.1093/nar/gkae992
• Lau, E. S.; Majerova, M.; Hensley, N. M.; Mukherjee, A.; Vasina, M.; Pluskal, D.; Damborsky, J.; Prokop, Z.; Delroisse, J.; Bayaert, W.-S.; Parey, E.; Oliveri, P.; Marletaz, F.; Marek, M.; Oakley, T. H. Functional characterization of luciferase in a brittle star indicates parallel evolution influenced by genomic availability of haloalkane dehalogenase. 2024. doi:10.1101/2024.10.14.618359
• Slanska, M.; Stackova, L.; Marques, S. M.; Stacko, P.; Martínek, M.; Jílek, L.; Toul, M.; Damborsky, J.; Bednar, D.; Klán, P.; Prokop, Z. Azobenzene-Based Photoswitchable Substrates for Advanced Mechanistic Studies of Model Haloalkane Dehalogenase Enzyme Family. ACS catalysis 2024, 14, 11635–11645. doi:10.1021/acscatal.4c03503
• Miller, J. R.; Schnorrenberg, E. C.; Aschenbrener, C.; Fox, B. G.; Brunold, T. C. Kinetic and Spectroscopic Investigation of the Y157F and C93G/Y157F Variants of Cysteine Dioxygenase: Dissecting the Roles of the Second-Sphere Residues C93 and Y157. Biochemistry 2024, 63, 1684–1696. doi:10.1021/acs.biochem.4c00177
• Tang, G. Q.; Hu, H.; Douglas, J.; Carter, C. W. Primordial aminoacyl-tRNA synthetases preferred minihelices to full-length tRNA. Nucleic acids research 2024, 52, 7096–7111. doi:10.1093/nar/gkae417
• Kenward, C.; Vuckovic, M.; Paetzel, M.; Strynadka, N. C. J. Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 main protease using a linked protein FRET platform. The Journal of biological chemistry 2024, 300, 107367. doi:10.1016/j.jbc.2024.107367
• Long, A. R.; Mortara, E. L.; Mendoza, B. N.; Fink, E. C.; Sacco, F. X.; Ciesla, M. J.; Stack, T. M. M. Sequence similarity network analysis of drug- and dye-modifying azoreductase enzymes found in the human gut microbiome. Archives of biochemistry and biophysics 2024, 757, 110025. doi:10.1016/j.abb.2024.110025
• Marshall, L. R.; Korendovych, I. V. Avoiding common pitfalls in designing kinetic protocols for catalytic amyloid studies. Methods in enzymology 2024, 697, 1–13. doi:10.1016/bs.mie.2024.03.029
• Ringenbach, S.; Yoza, R.; Jones, P. A.; Du, M.; Klugh, K. L.; Peterson, L. W.; Colabroy, K. L. Discovery and characterization of l-DOPA 2,3-dioxygenase from Streptomyces hygroscopicus jingganensis. Archives of biochemistry and biophysics 2024, 755, 109967. doi:10.1016/j.abb.2024.109967
• Marshall, L. R.; Makhlynets, O. V. Stopped-flow measurement of CO2 hydration activity by catalytic amyloids. Methods in enzymology 2024, 697, 35–49. doi:10.1016/bs.mie.2024.01.016
• Nalefski, E. A.; Kooistra, R. M.; Parikh, I.; Hedley, S.; Rajaraman, K.; Madan, D. Determinants of CRISPR Cas12a nuclease activation by DNA and RNA targets. Nucleic acids research 2024, 52, 4502–4522. doi:10.1093/nar/gkae152
• Carter, C. W. Base Pairing Promoted the Self-Organization of Genetic Coding, Catalysis, and Free-Energy Transduction. Life (Basel, Switzerland) 2024, 14, 199. doi:10.3390/life14020199
• McCarty, K. D.; Liu, L.; Tateishi, Y.; Wapshott-Stehli, H. L.; Guengerich, F. P. The multistep oxidation of cholesterol to pregnenolone by human cytochrome P450 11A1 is highly processive. The Journal of biological chemistry 2023, 300, 105495. doi:10.1016/j.jbc.2023.105495
• Simpson, M. C.; Harding, C. J.; Czekster, R. M.; Remmel, L.; Bode, B. E.; Czekster, C. M. Unveiling the Catalytic Mechanism of a Processive Metalloaminopeptidase. Biochemistry 2023, 62, 3188–3205. doi:10.1021/acs.biochem.3c00420
• Chaillou, L. L.; Boeris, V.; Spelzini, D.; Nazareno, M. A. Enzymes in Biocatalysis: Characteristics, Kinetic Approach, Production, and Uses. Advanced Pharmacy; BENTHAM SCIENCE PUBLISHERS, 2023; pp 83–107. doi:10.2174/9789815049428123010007
• Körner, A.; Bazzone, A.; Wichert, M.; Barthmes, M.; Dondapati, S. K.; Fertig, N.; Kubick, S. Unraveling the kinetics and pharmacology of human PepT1 using solid supported membrane-based electrophysiology. Bioelectrochemistry (Amsterdam, Netherlands) 2023, 155, 108573. doi:10.1016/j.bioelechem.2023.108573
• Johnson, K. A. You get what you screen for: Standards for experimental design and data fitting in drug discovery. Methods in enzymology 2023, 690, 131–157. doi:10.1016/bs.mie.2023.08.003
• Johnson, K. A. History of advances in enzyme kinetic methods: From minutes to milliseconds. The Enzymes 2023, 54, 107–134. doi:10.1016/bs.enz.2023.07.005
• Bursch, K. L.; Olp, M. D.; Smith, B. C. Analysis of continuous enzyme kinetic data using ICEKAT. Methods in enzymology 2023, 690, 109–129. doi:10.1016/bs.mie.2023.06.019
• Lee, D. F.; Atencio, N.; Bouchey, S.; Shoemaker, M. R.; Dodd, J. S.; Satre, M.; Miller, K. A.; McFarlane, J. S. Kinetic and structural characterization of carboxyspermidine dehydrogenase of polyamine biosynthesis. The Journal of biological chemistry 2023, 299, 105033. doi:10.1016/j.jbc.2023.105033

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