People want to be able to do things, but they don’t know what they want, so we have to help them figure that out. We do that by studying the enzymes in their body and figuring out how they work. We then create one or more products designed to fill that niche. Creating a product is called “designing” or “developing”; this is where the real work happens.
2. What are enzymes?
In this post, I look at enzymes as a classic example of the power and potential of everyday objects. The enzyme is something that can be found in, or on, every single one of us: it’s in the air that we breathe and the water we drink; it’s in food that we eat; it’s in our hair and skin; it’s in our bodies that carry out chemical reactions.
So what exactly is an enzyme? In this post, I lay out what enzymes are, how they work (and how they aren’t), and why they count as a critical part of every single one of us — because, without them, everything else would be impossible.
3. The characteristics of enzymes
This is a relatively simple question with a fairly straightforward answer. The characteristics of enzymes (among many other things) are that they catalyze chemical reactions and that only certain enzymes can catalyze chemical reactions.
A second related question is:
• What is the best approach for choosing an enzyme?
In this post, I’ll cover an approach to this question.
Choosing the correct enzyme for a given reaction is a very careful trade-off. The two answers are:
1) One enzyme may be better than another at catalyzing the reaction, but it may require too much power or not sufficiently energy and thus be overused, or 2) There is only one enzyme that can do it, and you can’t tell which one will be most effective at doing so (so you need to experiment).
This leads us to an essential distinction between enzymes and other chemicals: enzymes have specific physical properties, while chemicals generally have no such properties (e.g., carbon monoxide has none). The third part of this distinction is quite subtle: if you think you know what the characteristics of an enzyme look like, you probably don’t.
Without actually trying out reactions with different enzymes (like the ones in our experiments), there might be no way of knowing. If we think we know which enzyme will do what, though, all we need to do is find one that fits the conditions of the problem. It turns out that it’s a bit more complicated, though there are at least two different ways to find an enzyme for a given reaction.
One approach is less demanding than the first, while another requires more work but has certain advantages — so this post will introduce both methods using some examples from our lab. We hope it clarifies the issue somewhat and will give examples of each strategy in action in our ongoing microbial polymerase assays series.
4. The role of enzymes in the body
What is an enzyme? Enzymes are some of the most critical biological tools in the body. They work entirely differently from other body parts and do important jobs that we don’t understand very well. Here are just a few examples:
1. Enzymes help us regulate how our bodies digest food and how much we eat — they are crucial to keeping us alive and healthy.
2. Enzymes create vitamin D in the body, which is essential for bone health.
3. Enzymes help our bodies break down carbohydrates into energy for us to use every day – better known as digesting carbs — so it’s excellent for blood sugar control, cholesterol management, and a whole bunch of other things.
4. Enzymes work with proteins to build up and repair tissue like all living tissues do (and all tissues can be repaired).
5. Enzymes recycle waste products like carbon dioxide and water from cells, making them essential to all animals (including humans).
5. The benefits of enzymes
In this post, I’m going to talk about enzymes. Enzymes are catalytic proteins that catalyze chemical reactions, allowing chemical compounds to move from one place to another. Most of us know enzymes as the active ingredients in artificial and natural food products; it’s hard to think of them without thinking of bread, cheese, or beer. However, most people don’t know what an enzyme is — that is, they know only that it is a protein.
Enzymes can be found in every living system on Earth: all animals have enzymes, plants, fungi, and even some microorganisms such as yeasts. And every cell uses them: every cell has an enzyme called ADP ribosylpyrimidine decarboxylase (ARPD), which is used by the cell to convert the product of its DNA replication into RNA (RNA synthesis) and then into DNA (DNA replication).
But there are also enzymes in our bodies that we don’t use very often: they are produced by our immune system when we get sick. Our immune system produces antibodies against viral infections and bacteria when we get ill or injured.
Enzymes like ARPD help produce these antibodies: they convert incoming viral or bacterial antigens into sugars that can be transferred across the membrane barriers between different body parts to the cells where the infection originated from by an antibody-producing T-cell (the “antibody factory”).
The enzyme also helps create a signal for a T-cell to recognize foreign antigens (the “antibody response”) on its way in from outside the body — for example, if a virus invades your blood, it will typically enter your “proximal lymph nodes” and incubate there for at least 24 hours before it invades your “distal lymph nodes” – so you will not usually feel anything until well after days have passed.
but because you have been infected with bacteria you will develop symptoms within hours of exposure — those first few hours become known as your “coeliac illness” because they indicate how fast you became ill after infection rather than how long it went on. ARPD mediates the first part of this process — this particular enzyme was made by ferret kidney cells which understand molecules called peptides which act as peptidoglycan (which is what peptidoglycans ).
6. The side effects of enzymes
If you consider going into the world of enzymes, you should learn how they work.
Enzymes are a fascinating class of molecules; they change their shape and properties in response to various stimuli, from light to heat to pH. They can be precise in their work and perform hundreds or thousands of specific chemical reactions in a concise amount of time.
They can even affect other molecules in myriad ways; for example, one enzyme will break down another enzyme’s protein, creating an enzyme inhibitor that is immediately degraded.
For most people, it is straightforward to understand how enzymes perform and how they can facilitate specific chemical reactions, but many fundamental aspects need a more profound understanding:
• The way enzymes change their shape (both under heat and light) (the process is called denaturation).
• How enzymes perform hundreds or thousands of chemical reactions each second (called catalysis).
• The role that enzymes play in the body — for example, transforming glucose into ATP (adenosine triphosphate), which is then released into the bloodstream for use by cells as energy.
Enzymes are remarkable molecules. They catalyze chemical reactions, breaking down products of the reactions they catalyze into smaller components that can be reused. They do this in a particular way: they work by breaking down an enzyme’s substrate(s) into smaller particles that can be catalyzed using other enzymes or directly by the substrate itself (the substrate is often one of their substrates). Other enzymes then use these to re-acquire the products of the previous reaction and so on.
This ability for enzymes to be active in a specific way is what makes them so unique (and why we refer to them as “enzymes” rather than “molecules”).
But this is not all there is to it: enzymes also perform a wide range of other roles (in addition to catalyzing chemical reactions), such as protecting cells from various kinds of damage, regulating certain types of cell function, and even performing simple metabolic processes like photosynthesis. And these range from very complex pathways of reactions involving over 1000 different molecules to simpler ones that use just two molecules at a time (such as sugars and amino acids).
The first step in understanding how these different kinds of activities occur is understanding when each type begins and ceases. There are three types:
• Catalytic activity occurs when the enzyme breaks down the substrate into its parts so that they can then be used by other enzymes or directly by their substrates (as opposed to being consumed or broken down).
• Antibody formation occurs when an antibody binds with an enzyme and blocks it from reacting with its substrate, which prevents it from working usually. Antibodies may act alone or in groups – most ‘active’ antibodies only bind once; this means that some unbound antibody molecules will always be available for use at any given time.
• Noncatalytic activity occurs when an enzyme needs its substrate but doesn’t require a particular product, meaning it can potentially break down all sorts of stuff if antibodies don’t block some part. This includes energy metabolism, detoxification, cell signaling, and many others (such as heat generation).
This category consists of a variety of much more subtle interactions between enzyme subunits and substrates than those shown above, so you never quite know which kind you will see described here.