Enzymes & Life
During every moment of every living things life an enzyme is at work keeping it alive. At any given moment there are several million enzymes going to work on your body allowing you to perform such simple tasks as breathe, read, taste and hear. Over 3,000 types of enzymes have been identified within the human body with millions of them renewing, maintaining, and protecting us. Needless to say, without enzymes you would be very dead.
Enzymes are protein based substances found in every cell of every plant and animal. Without them beer would not ferment, leaves would not change color in the fall, and fruit would not ripen. They are the powerhouse of every cell (sorry mitochondria) and start chemical reactions or make chemical reactions run faster while remaining unchanged themselves. Every civilization has used enzymes, whether knowingly or not, in making every bottle of wine, block of cheese, and loaf of bread. Enzymes have long helped people prepare and preserve food.
Ancients believed that the transformation of one food into another, such as milk into cheese, was a magical process that involved an inherent secret of all living things; a type of Vitality. Alchemists tried to harness this Vitality in an effort to turn iron into gold. Today we use the â€œmagicâ€? of fermentation by harnessing the chemical changes induced by bacteria, microscopic yeasts, and molds. These changes make the production of many types of antibiotics possible, allow materials to be altered in a more economically efficient way, and allow for advanced food processing techniques.
Enzymes regulate that series of complex chemical reactions known as metabolism which is the combined action of anabolism and catabolism. Anabolism is the process of building up (such as new tissue growth) by means of combining simpler substances to form more complex ones. Catabolism is the very opposite and includes any process that breaks down a substance into a simpler substance, such as digestion. Enzymes catalyze the chemical processes that make metabolism possible. As well as making our metabolism get underway, enzymes also act as food potentiators, that is, they unlock the potential nutritive content of food.
Our production of enzymes can decrease in the midst aging, illness, injury, or stress and if the body canâ€™t produce enough then they must be gotten from an outside source. Itâ€™s like a fish tank with a malfunctioning water filter; something that was once self sufficient now needs an outside source of fresh water. If we start to lack one enzyme then it will affect the whole bunch and eventually we will have to introduce enzyme rich foods or supplements. The millions of enzymes that exist in every system or our bodies are what keep us alive and well.
Types Of Enzymes & Their Actions
Enzymes are classified into six main groups based on what they do, what their substrate is, and what reaction they start or accelerate. Following is a list of enzyme groups:
Hydrolases: This group breaks down proteins, carbohydrates and fats such as during digestion by adding a water molecule.
Isomerases: This group acts as a catalyst for the rearrangement of chemical groups with the same molecule.
Ligases: Through the use of an energy source, this group acts to catalyze the formation of a bond between two substrate molecules.
Lyases: By adding or subtracting chemical groups, these enzymes catalyze the formation of double bonds between atoms.
Oxidoreductases: This group makes oxidation reduction possible.
Transferases: This group of enzymes transfers chemical groups from one molecule to another.
The majority of enzymes (about 95%) are catabolic and help your body take things apart. In other words, they break down complex substances into usable, simple substances. For example, digestive enzymes help breakdown a meal into its smallest components such as amino acids, mono- and disaccharides, esters, et cetera by clipping the bonds that hold all the various parts together.
All enzymes are substrate specific meaning that it takes one enzyme to break apart (lyse) the protein in meat and many others to get to work on that potato, broccoli, cheese, ketchup, etc. ad nauseum.
Why This Works...
The Lock and Key Theory: Suggests that the right substrate for an enzyme acts as a key and fits into a specific activating shape for that particular enzyme.
The Induced Fit Theory: In this theory the enzyme becomes a blanket that changes its shape in order to fit around a substrate or bind with it.
The place where an enzyme connects with a substrate is referred to as the active site which requires that a substrate come into contact with an enzymes active site in order for the enzyme to do its work. This process is precautionary and makes sure that an enzyme recognizes only a specific molecule as being a proper substrate.
All enzymes work under their own unique conditions at their own unique speed. To get an idea of how fast enzymes work (and they work very fast), consider the slowest known enzyme, lysozyme. Lysozyme goes to work destroying bacteria possessing about thirty substrate molecules per minute or one substrate every two seconds. But compared to carboanhydrase which can process 36 million substrate molecules in one minute, lysozyme really isnâ€™t fast at all. Naturally, an enzymeâ€™s working speed is influenced by its environment, in other words, the health of the individual.
Enzymes can only do their work when in association with small molecules called coenzymes and cofactors. In order for an enzyme to function, cofactors such as the minerals zinc, magnesium, copper and calcium must be present. An inactive enzyme (an apoenzyme) can become an active enzyme (a holoenzyme) when combined with organic substances known as coenzymes which includes the C and B vitamins. A coenzyme may sometimes be a cofactor.
Just as there are substances that can make enzymes work better, there are those that inhibit their activity. Some enzyme inhibitors are known as competitive because they prevent the substrate from getting to the active site and bonding with the enzyme. Other inhibitors are noncompetitive and simply impede the conversion of a substrate by an enzyme. The majority of medicines (including the â€œinnocuousâ€? Aspirin) inhibit the functionality of our enzymes. Organic solvents such as methanol, ethanol, formic acid, ethylene glycol and others are also known to inhibit a large variety of enzymes.
Every enzyme eventually wears out and dies. As an enzyme begins to show signs of wear, another enzyme comes along and breaks it down to be transported away. Some enzyme live for only about twenty minutes while others can last for weeks. After an enzyme dies it is replaced by a newly created enzyme of the same type. Enzymes actually work and communicate with one another to form cooperatives when necessary and maintain equilibrium within all the bodiesâ€™ systems.
Enzymes Complete Part Two.