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- Overview
- Introduction
- Enzymes and activation energy
- Active sites and substrate specificity
- Environmental effects on enzyme function
- Induced fit
- Explore outside of Khan Academy
Enzymes as biological catalysts, activation energy, the active site, and environmental effects on enzyme activity.
As a kid, I wore glasses and desperately wanted a pair of contact lenses. When I was finally allowed to get contacts, part of the deal was that I had to take very, very good care of them, which meant washing them with cleaner every day, storing them in a sterile solution, and, once a week, adding a few drops of something called “enzymatic cleaner.” I didn’t know exactly what “enzymatic cleaner” meant, but I did learn that if you forgot you’d added it and accidentally put your contacts in your eyes without washing them, you were going to have burning eyes for a good fifteen minutes.
As I would later learn, all that “enzymatic” meant was that the cleaner contained one or more enzymes, proteins that catalyzed particular chemical reactions – in this case, reactions that broke down the film of eye goo that accumulated on my contacts after a week of use. (Presumably, the reason it stung when I got it in my eyes was that the enzymes would also happily break down eye goo in an intact eye.) In this article, we’ll look in greater depth at what an enzyme is and how it catalyzes a particular chemical reaction.
A substance that speeds up a chemical reaction—without being a reactant—is called a catalyst. The catalysts for biochemical reactions that happen in living organisms are called enzymes. Enzymes are usually proteins, though some ribonucleic acid (RNA) molecules act as enzymes too.
Enzymes perform the critical task of lowering a reaction's activation energy—that is, the amount of energy that must be put in for the reaction to begin. Enzymes work by binding to reactant molecules and holding them in such a way that the chemical bond-breaking and bond-forming processes take place more readily.
To clarify one important point, enzymes don’t change a reaction’s ∆G value. That is, they don’t change whether a reaction is energy-releasing or energy-absorbing overall. That's because enzymes don’t affect the free energy of the reactants or products.
Instead, enzymes lower the energy of the transition state, an unstable state that products must pass through in order to become reactants. The transition state is at the top of the energy "hill" in the diagram above.
To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. These molecules are the enzyme's substrates.
In some reactions, one substrate is broken down into multiple products. In others, two substrates come together to create one larger molecule or to swap pieces. In fact, whatever type of biological reaction you can think of, there is probably an enzyme to speed it up!
The part of the enzyme where the substrate binds is called the active site (since that’s where the catalytic “action” happens).
Proteins are made of units called amino acids, and in enzymes that are proteins, the active site gets its properties from the amino acids it's built out of. These amino acids may have side chains that are large or small, acidic or basic, hydrophilic or hydrophobic.
The set of amino acids found in the active site, along with their positions in 3D space, give the active site a very specific size, shape, and chemical behavior. Thanks to these amino acids, an enzyme's active site is uniquely suited to bind to a particular target—the enzyme's substrate or substrates—and help them undergo a chemical reaction.
[How specific is the matching between enzyme and substrate?]
Because active sites are finely tuned to help a chemical reaction happen, they can be very sensitive to changes in the enzyme’s environment. Factors that may affect the active site and enzyme function include:
•Temperature. A higher temperature generally makes for higher rates of reaction, enzyme-catalyzed or otherwise. However, either increasing or decreasing the temperature outside of a tolerable range can affect chemical bonds in the active site, making them less well-suited to bind substrates. Very high temperatures (for animal enzymes, above 40 ∘C or 104 ∘F ) may cause an enzyme to denature, losing its shape and activity.2
The matching between an enzyme's active site and the substrate isn’t just like two puzzle pieces fitting together (though scientists once thought it was, in an old model called the “lock-and-key” model).
Instead, an enzyme changes shape slightly when it binds its substrate, resulting in an even tighter fit. This adjustment of the enzyme to snugly fit the substrate is called induced fit.
When an enzyme binds to its substrate, we know it lowers the activation energy of the reaction, allowing it to happen more quickly. But, you may wonder, what does the enzyme actually do to the substrate to make the activation energy lower?
The answer depends on the enzyme. Some enzymes speed up chemical reactions by bringing two substrates together in the right orientation. Others create an environment inside the active site that's favorable to the reaction (for instance, one that's slightly acidic or non-polar). The enzyme-substrate complex can also lower activation energy by bending substrate molecules in a way that facilitates bond-breaking, helping to reach the transition state.
Finally, some enzymes lower activation energies by taking part in the chemical reaction themselves. That is, active site residues may form temporary covalent bonds with substrate molecules as part of the reaction process.
An important word here is "temporary." In all cases, the enzyme will return to its original state at the end of the reaction—it won't stay bound to the reacting molecules. In fact, a hallmark property of enzymes is that they aren't altered by the reactions they catalyze. When an enzyme is done catalyzing a reaction, it just releases the product (or products) and is ready for the next cycle of catalysis.
Do you want to learn more about the effect of temperature on enzyme function? Check out this interactive image from LabXchange.
Do you want to learn more about the effect of pH on enzyme function? Check out this interactive image from LabXchange.
LabXchange is a free online science education platform created at Harvard’s Faculty of Arts and Sciences and supported by the Amgen Foundation.
[Attribution and references]
Nov 22, 2020 · The ribosomes then build a protein is created from individual amino acids. Three bases make a codon. One codon correlates to one amino acid. Amino acids forms chains called proteins. There are three slides on this activity, the first two show images of the process and the last slide asks students to answer text questions that describe various ...
As tRNA bring amino acids, the amino acids bond together forming polypeptide chains, which will form proteins. Rewrite your mRNA sequence from part A. Using the amino acids table, determine the sequence of amino acids based on your mRNA strand. Use hyphens (dashes) to separate amino acids. Label the following diagram of Protein Synthesis.
The cell cycle is a cycle, rather than a linear pathway, because at the end of each go-round, the two daughter cells can start the exact same process over again from the beginning. In eukaryotic cells, or cells with a nucleus, the stages of the cell cycle are divided into two major phases: interphase and the mitotic (M) phase.
