EOB-Tutorial 4 Harsh Pittroda: Lock and Key Theory

EOB-Tutorial 4
Harsh Pittroda
1. What are enzymes? Explain Lock & Key Mechanism of Enzymes.
Enzymes are a special kind of protein that are found in the cells of living organisms.
Enzymes are made up of long chains of amino acids that are held together by
peptide bonds.
Enzymes help with processes like digestion, blood clotting, and hormone
production. They basically either catalyze (cause) or speed up chemical reactions
that take place in the bodies of living things. Typically, enzymes are only responsible
for one kind of chemical reaction. So, an enzyme that helps with digestion won’t
also help with blood clotting.
We need enzymes because they help us initiate chemical reactions. For every
chemical reaction, a specific amount of energy needs to be applied to the reactants
before the reaction can happen. Enzymes help make reactions happen. It’s kind of
like they are the final push over the hill before you can get a ball to roll down it.
Lock and Key Theory:

The specific action of an enzyme with a single substrate can be explained using
a Lock and Key analogy first postulated in 1894 by Emil Fischer. In this analogy, the
lock is the enzyme and the key are the substrate. Only the correctly sized key
(substrate) fits into the keyhole (active site) of the lock (enzyme).
Smaller keys, larger keys, or incorrectly positioned teeth on keys (incorrectly
shaped or sized substrate molecules) do not fit into the lock (enzyme). Only the
correctly shaped key opens a lock. This is illustrated in graphic on the left.
QUES: Using a diagram and in your own words, describe the various lock and key
theory of enzyme action in relation to a correct and incorrect substrate.
2. Explain the working of any two enzymes in detail.
Lipase is an enzyme that breaks down triglycerides into free fatty acids and
glycerol. Lipases are present in pancreatic secretions and are responsible for fat
digestion. There are many different types of lipases; for example, hepatic lipases
are in the liver, hormone-sensitive lipases are in adipocytes, lipoprotein lipase is in
the vascular endothelial surface, and pancreatic lipase in the small intestine.
Understanding lipase is crucial for understanding the pathophysiology of fat
necrosis and is clinically significant in the understanding of acute and chronic
pancreatitis. The role of lipase is also crucial in the mechanism of some medications
indicated for lowering cholesterol.
Lipase is an enzyme that breaks down triglycerides into free fatty acids and glycerol.
Lipases are present in pancreatic secretions and are responsible for fat digestion.
Lipases are enzymes that play a crucial role in lipid transport. There are many
different types of lipases; hepatic lipases are in the liver, hormone-sensitive lipases
are in adipocytes, lipoprotein lipase is in the vascular endothelial surface, and
pancreatic lipase is in the small Hormone-sensitive lipase is found within fat tissue
and is responsible for degrading the triglycerides that are stored within
adipocytes. Lipoprotein lipase is found on the vascular endothelial surface and is
responsible for degrading triglycerides that circulating from chylomicrons and
VLDLs. Pancreatic lipase is found within the small intestine and is responsible for
degrading dietary triglycerides.
Amylase: An enzyme produced in the pancreas and salivary glands that helps in
the digestion of starches. Elevation of blood amylase is common in pancreatitis.
Amylase, any member of a class of enzymes that catalyze the hydrolysis (splitting
of a compound by addition of a water molecule) of starch into smaller
carbohydrate molecules such as maltose (a molecule composed of
two glucose molecules). Two categories of amylases, denoted alpha and beta,
differ in the way they attack the bonds of the starch molecules.
Alpha-amylase is widespread among living organisms. In the digestive systems of
humans and many other mammals, an alpha-amylase called ptyalin is produced by
the salivary glands, whereas pancreatic amylase is secreted by the pancreas into
the small intestine.
Ptyalin is mixed with food in the mouth, where it acts upon starches. Although the
food remains in the mouth for only a short time, the action of ptyalin continues for
up to several hours in the stomach—until the food is mixed with the stomach
secretions, the high acidity of which inactivates ptyalin. Ptyalin’s digestive action
depends upon how much acid is in the stomach, how rapidly the stomach contents
empty, and how thoroughly the food has mixed with the acid. Under optimal
conditions as much as 30 to 40 percent of ingested starches can be broken down
to maltose by ptyalin during digestion in the stomach.
When food passes to the small intestine, the remainder of the starch molecules are
catalyzed mainly to maltose by pancreatic amylase. This step-in starch digestion
occurs in the first section of the small intestine (the duodenum), the region into
which the pancreatic juices empty. The by-products of amylase hydrolysis are
ultimately broken down by other enzymes into molecules of glucose, which are
rapidly absorbed through the intestinal wall.

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