Article ID Journal Published Year Pages File Type
9602680 Enzyme and Microbial Technology 2005 13 Pages PDF
Abstract
Within the framework of classical Michaelis-Menten kinetics and in accordance with the customary use of KM for a comparison of enzyme-substrate affinity, the MCR parameter may be interpreted as a relative substrate affinity. This proportion remains nearly the same for different mould (or yeast) β-galactosidases, though the affinity to a particular substrate may vary essentially from enzyme to enzyme. The constancy of MCR may be a manifestation of structural similarity of binding sites for these enzymes.
Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
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