- Oct 2024
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www.ncbi.nlm.nih.gov www.ncbi.nlm.nih.gov
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not constant but instead can be modulated
Makes for enzymes to be more multifunctional?
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NAD
I am familiar with NAD+ yet never knew it was a coenzyme
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The
In general this document is an educational description of the process of enzymes being used as biological catalysts and the different mechanisms that are utlized in the process as a whole
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ction.
Lots of more dense scientific description of substrate binding
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induced fit
Term
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lock-and-key model
Term
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Although the simple example discussed in the previous section involved only a single substrate molecule, most biochemical reactions involve interactions between two or more different substrates
Does a process like this occur when enzymes are used by bacteria to counter antibiotics?
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Substrates initially bind to the active site by noncovalent interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Once a substrate is bound to the active site of an enzyme, multiple mechanisms can accelerate its conversion to the product of the reaction.
How substrates bond and what happens once they do
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called the active site
Another key term, includes link with extra information(read later)
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energy state, called the transition state.
Key terminology
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A fundamental task of proteins is to act as enzymes—catalysts that increase the rate of virtually all the chemical reactions within cells.
The first statement appears to be a general statement of the material to be discuessed further in the document based off the title
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Like all other catalysts, enzymes are characterized by two fundamental properties. First, they increase the rate of chemical reactions without themselves being consumed or permanently altered by the reaction. Second, they increase reaction rates without altering the chemical equilibrium between reactants and products.
General introduction to the purpose of the following subsection of this article
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