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- W1467055635 abstract "This chapter gives an introduction to enzymes, which work as catalysts. Metabolism is impossibly slow without enzymes. Enzymes are virtual on/off switches, with efficient conversion to products in an enzyme's presence and extremely low or no substrate reactivity in an enzyme's absence. When an uncatalyzed reaction is reasonably fast, an enzyme is required to assure that the reaction's pace is compatible with efficient metabolism under the full range of conditions experienced by that enzyme. Most enzymes also exhibit rate-saturation kinetics, meaning that velocity ramps linearly when the substrate concentration is below the Michaelis constant, and reaches maximal activity when the substrate is present at a concentration that is 10–20 times the value of the Michaelis constant. Biochemists recognize that substrate specificity is another fundamental biotic strategy for effectively organizing biochemical reactions into metabolic pathways. By controlling the relative concentrations of such enzymes, cells also avoid undesirable kinetic bottlenecks or the undue accumulation of pathway intermediates. Enzyme active sites can also harbor metal ions that attain unusually reactive oxidation states that rarely form in aqueous medium and even less often in the absence of side-reactions. The resilience of living organisms stems in large measure from the capacity of enzymes to specifically or selectively bind other ligands (e.g., coenzymes, cofactors, activators, inhibitors, protons, and metal ions). Enzymes are often altered conformationally via biospecific binding interactions with substrates and/or regulatory molecules to achieve optimal metabolic control. An additional feature is the capacity of multisubunit enzymes to exhibit cooperativity." @default.
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- W1467055635 date "2010-01-01" @default.
- W1467055635 modified "2023-09-23" @default.
- W1467055635 title "An Introduction to Enzyme Science" @default.
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- W1467055635 doi "https://doi.org/10.1016/b978-0-12-380924-7.10001-8" @default.
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