Michaelis-menten Specificity
Michaelis-Menten Specificity is a theoretical construct in enzyme kinetics that characterizes the intrinsic selectivity of an enzyme for a particular substrate by quantifying the relationship between substrate concentration and reaction rate according to the Michaelis-Menten model, distinguishing it from other forms of enzymatic specificity by its reliance on the kinetic parameters \( K_m \) and \( V_{\text{max}} \) derived from saturation kinetics.
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2017–2026
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Enzymatic catalysis in nonaqueous solvents.
A. S. Zaks, Alexander M. Klibanov · Journal of Biological Chemistry · 1988 · 993 citations · Full text
Laccases: A Useful Group of Oxidoreductive Enzymes
Liliana Gianfreda, Feng Xu, Jean‐Marc Bollag · Bioremediation Journal · 1999 · 818 citations
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Massachusetts Institute of Technology, United States
3 publications · 1.6K citations
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Centre National de la Recherche Scientifique
Paris, France
7 h-index
30 publications
944 citations

Augusta University
Augusta, United States
6 h-index
23 publications
1.5K citations

University of Helsinki
Helsinki, Finland
4 h-index
13 publications
455 citations
National Institutes of Health
Bethesda, United States
4 h-index
9 publications
1.4K citations
Purdue University West Lafayette
West Lafayette, United States
3 h-index
6 publications
272 citations
Louisiana State University
Baton Rouge, United States
3 h-index
5 publications
95 citations

Virginia Commonwealth University Medical Center
Richmond, United States
3 h-index
8 publications
405 citations
University of California, Davis
Davis, United States
3 h-index
3 publications
91 citations
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JBC · 23 publications · 3.2K citations
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17 publications · 534 citations
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BJ · 11 publications · 628 citations
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JB · 11 publications · 846 citations
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EJB · 9 publications · 574 citations
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