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Enzymes: Catalysts for Biological Reactions, Lecture notes of Biochemistry

A comprehensive overview of enzymes, their structure, function, and classification. It explains how enzymes work as catalysts to accelerate biological reactions, lowering the activation energy required. The key factors that affect enzyme activity, including environmental conditions, cofactors and coenzymes, and enzyme inhibitors. It also delves into the different types of enzymes based on their catalytic functions, such as oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The enzyme-substrate binding process, the role of the active site, and the concept of the enzyme-substrate complex. Additionally, it discusses the importance of enzymes in various biological processes, including signal transduction, cell regulation, muscle contraction, active transport, and metabolic pathways. This document would be a valuable resource for students and researchers interested in understanding the fundamental principles of enzymes and their crucial role in sustaining life.

Typology: Lecture notes

2022/2023

Available from 08/26/2024

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1 | E n z y m e s
ENZYMES
Usually protein, but some are RNA. Work by lowering the activation energy of a reaction
Most enzymes are Proteins (tertiary and quaternary structures)
Act as Catalyst to accelerates a reaction
Not permanently changed in the process
Are specific for what they will catalyze
Are Reusable
End in ase
-Sucrase
-Lactase
-Maltase
HOW DO ENZYMES WORK?
- Enzymes work by weakening bonds which lowers activation energy
ENZYME-SUBSTRATE COMPLEX
- The substance (reactant) an enzyme acts on is the substrate
ACTIVE SITE
- A restricted region of an enzyme molecule which binds to the substrate.
INDUCED FIT
- A change in the shape of an enzyme’s active site
- Induced by the substrate
- A change in the configuration of an enzyme’s active site (H+ and ionic bonds are involved).
WHAT AFFECTS ENZYME ACTIVITY?
3 FACTORS
1. Environmental Conditions
- Extreme Temperature are the most dangerous
- - high temps may denature (unfold) the enzyme.
- pH (most like 6 - 8 pH near neutral)
- Ionic concentration (salt ions)
2. Cofactors and Coenzymes
- Inorganic substances (zinc, iron) and vitamins (respectively) are sometimes need for proper
enzymatic activity.
- EX: Iron must be present in the quaternary structure - hemoglobin in order for it to pick
up oxygen.
3. Enzyme Inhibitors
- EX: Competitive inhibitors: are chemicals that resemble an enzyme’s normal substrate and compete
with it for the active site.
- EX: Noncompetitive inhibitors:
Inhibitors that do not enter the active site, but bind to another part of the enzyme causing the
enzyme to change its shape, which in turn alters the active site.
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ENZYMES

Usually protein, but some are RNA. Work by lowering the activation energy of a reaction  Most enzymes are Proteins (tertiary and quaternary structures)Act as Catalyst to accelerates a reactionNot permanently changed in the processAre specific for what they will catalyzeAre ReusableEnd in – ase

**_- Sucrase

  • Lactase
  • Maltase_**  HOW DO ENZYMES WORK?
  • Enzymes work by weakening bonds which lowers activation energy  ENZYME-SUBSTRATE COMPLEX
  • The substance (reactant) an enzyme acts on is the substrate  ACTIVE SITE
  • A restricted region of an enzyme molecule which binds to the substrate.  INDUCED FIT
  • A change in the shape of an enzyme’s active site
  • Induced by the substrate
  • A change in the configuration of an enzyme’s active site (H+ and ionic bonds are involved).  WHAT AFFECTS ENZYME ACTIVITY?  3 FACTORS
  1. Environmental Conditions
  • Extreme Temperature are the most dangerous
  • - high temps may denature (unfold) the enzyme.
  • pH (most like 6 - 8 pH near neutral)
  • Ionic concentration (salt ions)
  1. Cofactors and Coenzymes
  • Inorganic substances (zinc, iron) and vitamins (respectively) are sometimes need for proper enzymatic activity.
  • EX: Iron must be present in the quaternary structure - hemoglobin in order for it to pick up oxygen.
  1. Enzyme Inhibitors
  • EX: Competitive inhibitors: are chemicals that resemble an enzyme’s normal substrate and compete with it for the active site.
  • EX: Noncompetitive inhibitors: Inhibitors that do not enter the active site, but bind to another part of the enzyme causing the enzyme to change its shape, which in turn alters the active site.

 General Characteristic  Catalyst for biological reactions  Cause cellular reactions to occur faster  Most are globular proteins, some are simple proteins  Are large biomolecules that are responsible for many chemical reactions that are necessary to sustain life  A protein molecule and are biological catalysts  They function with only one reactant to produce specific products  Have three-dimensional structure and they utilize organic molecules like biotin and inorganic molecules like metal ions (magnesium ions) for assistance in catalysis

  • SUBSTRATE is the reactant in an enzyme catalyzed reaction. The portion of the molecule that is responsible for catalytic action of enzyme is the active site.  Enzymes show varying degree of specificities  Absolute specificity where enzymes react only with one substrate.  Apoenzyme – The protein part of the enzyme.  Cofactor – Non protein part of the enzyme.  The apoenzyme and the cofactor together is called the HoloenzymeCofactors may be of three types: Prosthetic Groups (organic groups that are permanently bound to enzymes), Activators (are cations – positively charged metal ions), Coenzymes (organic molecules usually vitamins or made from vitamins, they are not bound permanently to enzymes but they combine with enzymes)  Functions  Major components in signal transduction and cell regulation, kinases, and phosphatases help in this function.  Take part in the movement with the help of the protein myosin which aids in muscle contraction.  Acts as ion pumps in active transport mechanism.  Present in the virus are for infecting cell.  Plays an important role in the digestive activity of the enzymes.  Amylases and proteases are enzyme that breakdown large molecules into absorbable molecules.  Forming metabolic pathways. Example: Glycolisis  Factors affecting enzymes (Read further page 72)  Enzymes Concentration  Temperature  Effect of PH  Other Substances  Radiation  Classification  Oxidoreductases
  • Catalyze redox reactions, adds or removes 𝑂 2 or 𝐻 2
    • are the enzymes that catalyze oxidation-reduction reactions Responsible for the production of heat and energy  Transferases
  • Transfers functional groups
    • catalyze reactions where transfer of functional group between two substrates takes place

**3. Effect of PH

  1. Other substances
  2. Radiation**