New standards for collecting and fitting steady state kinetic data

Scholarly Works

• Barnsley, E. The Steady State Approximation in Enzyme Kinetics: Reflections in Its Centennial Year. Qeios 2025, 7. doi:10.32388/1c11nk.2
• Greene, E.; Muniz, R.; Yamamura, H.; Hoff, S. E.; Bajaj, P.; Lee, D. J.; Thompson, E. M.; Arada, A.; Lee, G. M.; Bonomi, M.; Kollman, J. M.; Fraser, J. S. Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity. eLife Sciences Publications, Ltd 2025. doi:10.7554/elife.108336.1
• Greene, E.; Muniz, R.; Yamamura, H.; Hoff, S. E.; Bajaj, P.; Lee, D. J.; Thompson, E. M.; Arada, A.; Lee, G. M.; Bonomi, M.; Kollman, J. M.; Fraser, J. S. Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity. eLife Sciences Publications, Ltd 2025. doi:10.7554/elife.108336
• Stack, T. M. M. From Classroom to Publication: Improving Enzyme Kinetic Constant Estimation and Graphical Visualization. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology 2025. doi:10.1002/bmb.70014
• Niu, C.; Zhang, D.; Zou, D.; Zhao, W.; Liu, D.; Huang, K.; Wei, X.; Li, D.; Ye, C.; Xiong, H. Novel Insights for α-amylase Improvement: Leveraging Amylopectin into Accurate Molecular Docking and Mutant Selection. Journal of agricultural and food chemistry 2025, 73, 24251–24261. doi:10.1021/acs.jafc.5c05133
• Atampugbire, G. A.; Quaye, J. A.; Gadda, G. How Mechanistic Enzymology Helps Industrial Biocatalysis: The Case for Kinetic Solvent Viscosity Effects. Catalysts 2025, 15, 736. doi:10.3390/catal15080736
• Nalefski, E. A.; Hedley, S.; Rajaraman, K.; Kooistra, R. M.; Parikh, I.; Sinan, S.; Finklestein, I. J.; Madan, D. Unleashing high trans-substrate cleavage kinetics of Cas12a for nucleic acid diagnostics. Nucleic acids research 2025, 53. doi:10.1093/nar/gkaf712
• Demisew, A. T.; Cohen, J. R.; Gruss, E. G.; Bui, J. D.; Steiner, J. L.; Xhafkollari, G.; Marasco, R. N.; Betonio, M.; Strzeminski, D.; Leyes Porello, S.; Colabroy, K. L.; Peterson, L. W. Probing the Mechanism of l‑DOPA 2,3-Dioxygenase Using Synthetic Derivatives of 3,4-Dihydroxyhydrocinnamic Acid. ACS omega 2025, 10, 32053–32069. doi:10.1021/acsomega.5c03691
• Barnsley, E. The Steady State Approximation in Enzyme Kinetics: Reflections in Its Centennial Year. Qeios Ltd 2025. doi:10.32388/1c11nk
• Greene, E.; Muniz, R.; Yamamura, H.; Hoff, S. E.; Bajaj, P.; Lee, D. J.; Thompson, E. M.; Arada, A.; Lee, G. M.; Bonomi, M.; Kollman, J. M.; Fraser, J. S. Product-stabilized filamentation by human glutamine synthetase allosterically tunes metabolic activity. 2025. doi:10.1101/2025.07.04.663231
• Wieland, M.; Luizaga, J.; Duran, C.; Germscheid, B.; Rein, J.; Bruckmann, A.; Hiefinger, C.; Osuna, S.; Hupfeld, A. Reversible Substrate-Specific Photocontrol of the Chemotherapeutic Asparaginase(-Glutaminase) from Escherichia coli. ACS catalysis 2025, 15, 8462–8478. doi:10.1021/acscatal.5c01608
• Akagawa, M.; Sugasawa, K.; Ura, K.; Sassa, A. Impact of an oxidative RNA lesion on in vitro replication catalyzed by SARS-CoV-2 RNA-dependent RNA polymerase. The Journal of biological chemistry 2025, 301, 108512. doi:10.1016/j.jbc.2025.108512
• Tang, G. Q.; Carter, C. W. Escherichia coli deletes in vivo the same domains from a double-mutant leucyl-tRNA synthetase gene that were deleted in vitro to make the LeuAC urzyme. Cold Spring Harbor Laboratory 2025. doi:10.1101/2025.04.05.647346
• 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.; Marlétaz, F.; Marek, M.; Oakley, T. H. Functional Characterization of Luciferase in a Brittle Star Indicates Parallel Evolution Influenced by Genomic Availability of Haloalkane Dehalogenase. Molecular biology and evolution 2025, 42. doi:10.1093/molbev/msaf081
• Waluga, T.; von Ziegner, F.; Skiborowski, M. Analytical and numerical approaches to the analysis of progress curves: A methodological comparison. Process Biochemistry 2025, 151, 1–13. doi:10.1016/j.procbio.2025.01.029
• Juretić, D. Exploring the Evolution-Coupling Hypothesis: Do Enzymes' Performance Gains Correlate with Increased Dissipation?. Entropy (Basel, Switzerland) 2025, 27, 365. doi:10.3390/e27040365
• Patra, S. K.; Randolph, N.; Kuhlman, B.; Dieckhaus, H.; Betts, L.; Douglas, J.; Wills, P. R.; Carter, C. W. Aminoacyl-tRNA synthetase urzymes optimized by deep learning behave as a quasispecies. Structural dynamics (Melville, N.Y.) 2025, 12, 024701. doi:10.1063/4.0000294
• Punekar, N. S. Enzyme Kinetic Data: Collection and Analysis. ENZYMES: Catalysis, Kinetics and Mechanisms; Springer Nature Singapore, 2025; pp 189–206. doi:10.1007/978-981-97-8179-9_16
• Creon, A.; Scheer, T. E. S.; Reinke, P.; Mashhour, A. R.; Günther, S.; Niebling, S.; Schamoni-Kast, K.; Uetrecht, C.; Meents, A.; Chapman, H. N.; Sprenger, J.; Lane, T. J. Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro. Cold Spring Harbor Laboratory 2025. doi:10.1101/2025.01.28.635305
• McCarty, K. D.; Guengerich, F. P. Liver fatty acid binding protein FABP1 transfers substrates to cytochrome P450 4A11 for catalysis. The Journal of biological chemistry 2025, 301, 108168. doi:10.1016/j.jbc.2025.108168

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