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Essay on Enzymes: Definition, Properties and Factors

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In this essay we will discuss about:- 1. Definition of Enzymes 2. Classification of Enzymes 3. Properties 4. Specificity 5. Preparation and Isolation 6. Recognition 7. Factors Influencing the Action 8. Catalytic Site 9. General Acid or Base Catalysts 10. Mechanism 11. Diagnostic Value.

• Essay on the Diagnostic Value of Serum Enzymes

Essay # 1. Definition of Enzymes :

Enzymes are soluble, colloidal organic cata­lysts formed by living cells, specific in action, pro­tein in nature, inactive at 0°C and destroyed by moist heat at 100°C.

Intracellular Enzymes:

Enzymes which are used in the cells which make them are said to be intracellular enzymes. These enzymes correspond to the old “organised ferments”.

Extracellular Enzymes:

Enzymes which are produced by other cells and are secreted to other parts of the body (e.g., digestive juice) are called extracellular enzymes. These enzymes correspond to the old “unorganised ferments”.

Zymase secretion:

An extracellular enzyme which is secreted ready for action is called a zymase secretion.

Amylase of saliva.

Zymogen secretion:

An enzyme which is se­creted in inactive form and ultimately activated by an agent secreted by other cell is said to be zy­mogen secretion.

Trypsinogen (in pan­creatic juice) activated by enterokinase (in intesti­nal mucosa) to give active trypsin, prothrombin (in blood) activated by thromboplastin (in tissues) to give active thrombin.

Zymogen secretion is probably a protective mechanism to prevent digestion of cell walls and ducts, since it is most frequently found with pro­tein-splitting enzymes.

The substance on which an en­zyme acts is called the substrate.

Maltose is the substrate on which the enzyme maltase acts to form glucose.

Except the enzymes ptyalin, pepsin, trypsin and erepsin, enzymes are usually named by adding the suffixase to the main part of the name of the substrate on which they act.

Maltase acts on maltose.

Lactase acts on lactose.

Lipases act on lipids.

Carbohydrases act on carbohydrates.

Proteases act on proteins.

Amylases act on starch (Amylum).

But there are many substances which are acted on by some enzymes in different ways. A dipeptide can be attacked by three enzymes. These enzymes are named by their function.

A dipeptide can be hydrolysed by di-peptidase into amino acids. The free amino group of the amino acid is removed by another enzyme and the free carboxyl group is also removed by another enzyme. So the names of these three enzymes act­ing on a dipeptide are a di-peptidase, a deaminase and a decarboxylase. Other enzymes are named by their functions only.

Transferases, dehydrogenases, hydrolases, oxidases and reductases.

Many enzymes with the same function act on one substance; it is, therefore, better to specify the enzyme by its source.

Pancreatic amy­lase, bone phosphatase, liver esterase.

Some enzymes acting on the substrates are freely described by the adjectives.

Amylolytic, lipolytic, proteolytic.

Catalytic RNAs :

a. Certain ribonucleic acids (RNAs) show highly substrate-specific catalytic activity.

b. These RNAs satisfy the classic criteria for definition as enzymes and are termed ribozymes.

c. Ribozymes catalyse trans-esterification and finally hydrolysis of phosphodiester bonds in RNA molecules. These reactions are enhanced by free OH groups.

d. Ribozymes are involved in the main roles in the intron splicing events essential for the conversion of Pre-mRNA in mature mRNAs.

Essay # 2. Classification of Enzymes :

The 6 major classes of enzymes with some examples are:

a. Oxidoreductases:

Enzymes catalyzing oxidoreductions between two substrates A and B:

A reduced + B oxidized = A oxidized + B reduced

These enzymes can be grouped in many different ways.

Three main groups can be explained in order to get the simpler ex­pression:

The enzymes which use oxy­gen as hydrogen acceptor.

Ty­rosinase, cytochrome oxidase, uricase.

Anaerobic dehydrogenases:

The enzymes which use some other substance as hydro­gen acceptor.

Malate dehydro­genase, succinate dehydrogenase, lactate dehydrogenase.

Hydro-peroxidases:

The enzymes which use hydrogen peroxide as substrate.

Ex­amples:

Peroxidase, catalase.

Aerobic dehydrogenases:

The enzymes which use either oxygen or another sub­stance as hydrogen acceptor.

D- and L-amino acid oxidases, xanthine oxidase, aldehyde oxidase.

Two other groups are:

Oxygenases:

The enzymes which act on single hydrogen donors with incorpora­tion of oxygen.

Tryptophan oxygenase.

Hydroxylases:

The enzymes which act on paired donors with incorporation of oxy­gen into one donor.

Steroid hydroxylases, phenylalanine 4-hydroxy- lase.

b. Transferases (Transferring enzymes):

They catalyse the transfer of some group or radi­cal, R, from one molecule A, to another molecule, B:

The kinetic equation can be expressed mathematically by Michaelismenten equation:

e. Oxidation :

(i) The sulfhydryl (SH) groups of many en­zymes are essential for enzyme activity.

(ii) Oxidation of these (SH) groups by many oxidizing agents including the oxygen of air forms the disulfide (S-S) linkages and results in loss of enzyme activity.

Examples of allosteric modulation :

Both the allosteric site and active site are lo­cated on different subunits of oligomeric enzymes. Alternation in the enzyme substrate interaction owing to the allosteric effects of regulatory mol­ecules other than the substrate are said to be heterotopic allosteric modulations.

The positive and negative arrangements with the substrate are exhibited by allosteric activators and inhibitors, respectively. Binding of substrate to one promoter accelerates the binding of the same to another promoter on the same enzyme molecule.

Homo-tropic allosteric effect results in the binding of a substrate enhancing the interaction between the allosteric enzyme and more molecules of the same substrate.

(i) Reversal of inhibition can be brought about by increasing the amount of substrate relative to inhibitor.

(ii) Inhibition may also be reversed by re­moval of the inhibitor by treatment with hydrogen sulphide (H 2 S):

Flexible Model of the Catalytic Site :

In the Fischer model, the catalytic is presumed to be pre-shaped to fit the substrate. In the induced fit model, the substrate induces a conformational change in the enzyme.

This aligns amino acid residues or other groups on the enzyme in the cor­rect spatial orientation for substrate binding, ca­talysis, or both.

At the same time, other amino acid residues may be buried in the interior of the mol­ecule. Hydrophobic groups (hatched portion) and charged groups (dots) both are involved in substrate binding.

A phosphoserine (-P) and the -SH of a cysteine are involved in catalysis. Other residues involved in neither process are represented by the side chains of lysine and methionine.

In the absence of substrate, the catalytic and the substrate-binding groups are several bond dis­tances removed from one another. Approach of the substrate induces a conformational change in the enzyme. At the same time, the spatial orientations of other regions are also altered, the lysine and methionine are now closer together.

In the representation of a catalytic site shown in Fig. 10.20, several regions of a polypeptide chain contribute amino acid residues to the site.

Three types of amino acid residues are distinguished in enzymes:

a. Contact residue:

An amino acid residue with one bond distance (0.2 nm) of the substrate.

b. Specificity residue:

An amino residue is involved in substrate binding as well as in catalytic process.

c. Catalytic residue:

An amino acid residue is directly involved in covalent bond changes during enzyme action.

Substrate analogs may cause some of the con­formational changes (Fig. 10.21). On attachment of the true substrate (A), all groups (shown as closed circles) are brought into correct alignment. Attach­ment of a substrate analog that is too “bulky” (Fig. 10.21B) or too “slim” (Fig. 10.21C) induces incor­rect alignment.

The exact sequence of events in a substrate induced conformational change remains to be es­tablished. Several possibilities stand (Fig. 10.22).

It is still difficult to decide exactly which residues constitute the catalytic site even after knowing the complete primary structure of an en­zyme.

Modifiers of Enzyme Activity :

Like all mammalian proteins, enzymes are degraded to amino acids. Although this mechanism reduces enzyme concentration and, hence, catalytic activity, still they are slow, wasteful of carbon and energy and, rather, they are like turning out a light by smashing the bulb, then inserting a new one when light is needed.

The catalytic activity of certain key enzymes can be reversibly decreased or increased by small molecules. Small molecule modifiers which de­crease catalytic activity are termed negative modi­fiers and those which increase or stimulate activity are called positive modifiers.

Essay # 9. Enzymes as General Acid or Base Catalysts :

Reactions whose rates vary as regards to changes in H + or H 3 O + concentration but are independent of the concentrations of other acids or bases present in the solution are said to be specific acid or spe­cific base catalysis.

Reactions whose rates are responsive to all acids or bases present in solution are said to be general acid or general base catalysis. Mutarotation of glucose is one reaction subject to general acid-base catalysis.

Role of Metal Ions :

More than 25 per cent of the enzymes contain tightly-bound metal ions for their activity. The func­tions of these metal ions may be studied by X-ray crystallography, nuclear magnetic resonance (NMR) and electron spin resonance (ESR).

Metal loenzymes and metal-activated en­zymes:

A definite quantity of functional metal ion is present in metallo-enzymes and that metal ion is also retained throughout purification. Metal-acti­vated enzymes bind metals less tightly but require added metals. The mechanism of action in both cases appears to be similar.

Essay # 11. Diagnostic Value of Serum Enzymes :

Very small amounts of enzymes which are involved in the reactions in the tissues are present in blood under normal conditions. The concentrations of these enzymes are significantly increased due to their more liberation by the affected tissues to the blood stream under certain clinical conditions.

Increase in the enzyme activities in cerebros­pinal fluid is not reflected in the blood. Changes may occur in the cerebrospinal fluid enzymes in certain diseases of the central nervous system.Lactate dehydrogenase activity in cerebro­spinal fluid is increased frequently in meningitis, cerebral thrombosis and hemorrhage.

Glucose phos­phate isomerase concentration in the cerebrospi­nal fluid is also elevated in malignant tumors of the brain and frequently in meningitis and cerebral thrombosis. The determination of the activity of the fol­lowing enzymes shown in the list can give valu­able confirmatory or suggestive diagnostic evi­dence to the physicians.

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• Activity of Enzymes in Plants: 7 Factors
• Allosteric Enzymes: Properties and Mechanism | Microbiology

Essay , Chemistry , Biochemistry , Living Cells , Catalyst , Essay on Enzymes

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Chemical nature

Nomenclature, mechanism of enzyme action.

• Factors affecting enzyme activity

What is an enzyme?

What are enzymes composed of, what are examples of enzymes, what factors affect enzyme activity.

Our editors will review what you’ve submitted and determine whether to revise the article.

• National Library of Medicine - Enzymes: principles and biotechnological applications
• Open Oregon Educational Resources - Enzymes
• Khan Academy - Enzyme structure and function
• Royal Society of Biology - Enzymes
• Cleveland Clinic - Enzymes
• Chemistry LibreTexts - Enzymes
• The University of Hawaiʻi Pressbooks - Biology - Enzymes
• enzyme - Children's Encyclopedia (Ages 8-11)
• enzyme - Student Encyclopedia (Ages 11 and up)
• Table Of Contents

• An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process.
• The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes.
• Without enzymes, many of these reactions would not take place at a perceptible rate.
• Enzymes catalyze all aspects of cell metabolism. This includes the digestion of food, in which large nutrient molecules (such as proteins, carbohydrates, and fats) are broken down into smaller molecules; the conservation and transformation of chemical energy; and the construction of cellular macromolecules from smaller precursors.
• Many inherited human diseases, such as albinism and phenylketonuria , result from a deficiency of a particular enzyme.
• A large protein enzyme molecule is composed of one or more amino acid chains called polypeptide chains. The amino acid sequence determines the characteristic folding patterns of the protein’s structure, which is essential to enzyme specificity.
• If the enzyme is subjected to changes, such as fluctuations in temperature or pH, the protein structure may lose its integrity (denature) and its enzymatic ability.
• Bound to some enzymes is an additional chemical component called a cofactor , which is a direct participant in the catalytic event and thus is required for enzymatic activity. A cofactor may be either a coenzyme —an organic molecule, such as a vitamin—or an inorganic metal ion. Some enzymes require both.
• All enzymes were once thought to be proteins, but since the 1980s the catalytic ability of certain nucleic acids, called ribozymes (or catalytic RNAs), has been demonstrated, refuting this axiom.
• Practically all of the numerous and complex biochemical reactions that take place in animals, plants, and microorganisms are regulated by enzymes, and so there are many examples. Among some of the better-known enzymes are the digestive enzymes of animals. The enzyme pepsin , for example, is a critical component of gastric juices, helping to break down food particles in the stomach. Likewise, the enzyme amylase , which is present in saliva, converts starch into sugar, helping to initiate digestion.
• In medicine, the enzyme thrombin is used to promote wound healing. Other enzymes are used to diagnose certain diseases. The enzyme lysozyme , which destroys cell walls, is used to kill bacteria.
• The enzyme catalase brings about the reaction by which hydrogen peroxide is decomposed to water and oxygen. Catalase protects cellular organelles and tissues from damage by peroxide, which is continuously produced by metabolic reactions.
• Enzyme activity is affected by various factors, including substrate concentration and the presence of inhibiting molecules.
• The rate of an enzymatic reaction increases with increased substrate concentration, reaching maximum velocity when all active sites of the enzyme molecules are engaged. Thus, enzymatic reaction rate is determined by the speed at which the active sites convert substrate to product.
• Inhibition of enzyme activity occurs in different ways. Competitive inhibition occurs when molecules similar to the substrate molecules bind to the active site and prevent binding of the actual substrate.
• Noncompetitive inhibition occurs when an inhibitor binds to the enzyme at a location other than the active site.
• Another factor affecting enzyme activity is allosteric control , which can involve stimulation of enzyme action as well as inhibition. Allosteric stimulation and inhibition allow production of energy and materials by the cell when they are needed and inhibit production when the supply is adequate.

enzyme , a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process.

A brief treatment of enzymes follows. For full treatment, see protein: Enzymes .

The biological processes that occur within all living organisms are chemical reactions , and most are regulated by enzymes. Without enzymes, many of these reactions would not take place at a perceptible rate. Enzymes catalyze all aspects of cell metabolism . This includes the digestion of food, in which large nutrient molecules (such as proteins , carbohydrates , and fats ) are broken down into smaller molecules; the conservation and transformation of chemical energy ; and the construction of cellular macromolecules from smaller precursors . Many inherited human diseases, such as albinism and phenylketonuria , result from a deficiency of a particular enzyme.

Enzymes also have valuable industrial and medical applications. The fermenting of wine, leavening of bread, curdling of cheese , and brewing of beer have been practiced from earliest times, but not until the 19th century were these reactions understood to be the result of the catalytic activity of enzymes. Since then, enzymes have assumed an increasing importance in industrial processes that involve organic chemical reactions. The uses of enzymes in medicine include killing disease-causing microorganisms, promoting wound healing, and diagnosing certain diseases.

All enzymes were once thought to be proteins, but since the 1980s the catalytic ability of certain nucleic acids, called ribozymes (or catalytic RNAs), has been demonstrated, refuting this axiom. Because so little is yet known about the enzymatic functioning of RNA , this discussion will focus primarily on protein enzymes.

A large protein enzyme molecule is composed of one or more amino acid chains called polypeptide chains. The amino acid sequence determines the characteristic folding patterns of the protein’s structure, which is essential to enzyme specificity. If the enzyme is subjected to changes, such as fluctuations in temperature or pH, the protein structure may lose its integrity (denature) and its enzymatic ability. Denaturation is sometimes, but not always, reversible.

Bound to some enzymes is an additional chemical component called a cofactor , which is a direct participant in the catalytic event and thus is required for enzymatic activity. A cofactor may be either a coenzyme —an organic molecule, such as a vitamin —or an inorganic metal ion ; some enzymes require both. A cofactor may be either tightly or loosely bound to the enzyme. If tightly connected, the cofactor is referred to as a prosthetic group.

An enzyme will interact with only one type of substance or group of substances, called the substrate , to catalyze a certain kind of reaction. Because of this specificity, enzymes often have been named by adding the suffix “-ase” to the substrate’s name (as in urease , which catalyzes the breakdown of urea ). Not all enzymes have been named in this manner, however, and to ease the confusion surrounding enzyme nomenclature , a classification system has been developed based on the type of reaction the enzyme catalyzes. There are six principal categories and their reactions: (1) oxidoreductases , which are involved in electron transfer; (2) transferases , which transfer a chemical group from one substance to another; (3) hydrolases , which cleave the substrate by uptake of a water molecule (hydrolysis); (4) lyases , which form double bonds by adding or removing a chemical group; (5) isomerases , which transfer a group within a molecule to form an isomer; and (6) ligases , or synthetases, which couple the formation of various chemical bonds to the breakdown of a pyrophosphate bond in adenosine triphosphate or a similar nucleotide .

In most chemical reactions, an energy barrier exists that must be overcome for the reaction to occur. This barrier prevents complex molecules such as proteins and nucleic acids from spontaneously degrading, and so is necessary for the preservation of life. When metabolic changes are required in a cell, however, certain of these complex molecules must be broken down, and this energy barrier must be surmounted. Heat could provide the additional needed energy (called activation energy ), but the rise in temperature would kill the cell. The alternative is to lower the activation energy level through the use of a catalyst . This is the role that enzymes play. They react with the substrate to form an intermediate complex—a “transition state”—that requires less energy for the reaction to proceed. The unstable intermediate compound quickly breaks down to form reaction products, and the unchanged enzyme is free to react with other substrate molecules.

Only a certain region of the enzyme, called the active site , binds to the substrate. The active site is a groove or pocket formed by the folding pattern of the protein. This three-dimensional structure, together with the chemical and electrical properties of the amino acids and cofactors within the active site, permits only a particular substrate to bind to the site, thus determining the enzyme’s specificity.

Enzyme synthesis and activity also are influenced by genetic control and distribution in a cell. Some enzymes are not produced by certain cells, and others are formed only when required. Enzymes are not always found uniformly within a cell; often they are compartmentalized in the nucleus , on the cell membrane , or in subcellular structures. The rates of enzyme synthesis and activity are further influenced by hormones , neurosecretions, and other chemicals that affect the cell’s internal environment .

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AP®︎/College Biology

Course: ap®︎/college biology   >   unit 3, enzymes review.

• Enzyme reaction velocity and pH
• Competitive inhibition
• Noncompetitive inhibition
• Enzyme regulation
• Basics of enzyme kinetics graphs
• Environmental impacts on enzyme function

Enzyme structure and function

Factors affecting enzyme activity.

• Temperature: Raising temperature generally speeds up a reaction, and lowering temperature slows down a reaction. However, extreme high temperatures can cause an enzyme to lose its shape (denature) and stop working.
• pH: Each enzyme has an optimum pH range. Changing the pH outside of this range will slow enzyme activity. Extreme pH values can cause enzymes to denature.
• Enzyme concentration : Increasing enzyme concentration will speed up the reaction, as long as there is substrate available to bind to. Once all of the substrate is bound, the reaction will no longer speed up, since there will be nothing for additional enzymes to bind to.
• Substrate concentration: Increasing substrate concentration also increases the rate of reaction to a certain point. Once all of the enzymes have bound, any substrate increase will have no effect on the rate of reaction, as the available enzymes will be saturated and working at their maximum rate.

Common mistakes and misconceptions

• Enzymes are "specific." Each type of enzyme typically only reacts with one, or a couple, of substrates. Some enzymes are more specific than others and will only accept one particular substrate. Other enzymes can act on a range of molecules, as long as they contain the type of bond or chemical group that the enzyme targets.
• Enzymes are reusable. Enzymes are not reactants and are not used up during the reaction. Once an enzyme binds to a substrate and catalyzes the reaction, the enzyme is released, unchanged, and can be used for another reaction. This means that for each reaction, there does not need to be a 1:1 ratio between enzyme and substrate molecules.

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Home — Essay Samples — Science — Enzyme — Enzyme Dynamics and Metabolic Pathways

Enzyme Dynamics and Metabolic Pathways

• Categories: Enzyme

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Words: 360 |

Published: Nov 15, 2018

Words: 360 | Page: 1 | 2 min read

• Competitive inhibitors. The inhibitors molecules bind to the active site to block the substrate molecules from binding to the active site. The molecular structure of competitive inhibitors is similar to that of the substrate so it can fit in the active site and block the substrate.
• Non-competitive inhibitors. The inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate. The inhibitor may bind to the enzyme whether or not the substrate has already been bound, but if it has a higher affinity for binding the enzyme in one state or the other, it is called a mixed inhibitor.

Works Cited

• Berg, J. M., Tymoczko, J. L., & Gatto, G. J. (2020). Biochemistry (9th ed.). W. H. Freeman and Company.
• Nelson, D. L., Cox, M. M. (2020). Lehninger Principles of Biochemistry (8th ed.). W. H. Freeman and Company.
• Lodish, H., Berk, A., Zipursky, S. L., et al. (2022). Molecular Cell Biology (9th ed.). W. H. Freeman and Company.
• Garrett, R. H., & Grisham, C. M. (2019). Biochemistry (6th ed.). Cengage Learning.
• Alberts, B., Johnson, A., Lewis, J., et al. (2019). Molecular Biology of the Cell (6th ed.). Garland Science.
• Cox, M. M., Nelson, D. L. (2021). Lehninger Principles of Biochemistry: Study Guide and Solutions Manual (7th ed.). W. H. Freeman and Company.
• Nelson, D. L., Cox, M. M. (2021). Lehninger Principles of Biochemistry: Lecture Notebook (7th ed.). W. H. Freeman and Company.
• Price, N. C., Stevens, L. (2020). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins. Oxford University Press.
• Cornish-Bowden, A. (2012). Fundamentals of Enzyme Kinetics (4th ed.). Wiley.
• Segel, I. H. (1993). Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. Wiley.

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