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Questions and Answers
What is an example of a condition that can cause disruption of cardiac enzymes in the blood?
What is an example of a condition that can cause disruption of cardiac enzymes in the blood?
What is the impact of liver damage on enzymatic levels?
What is the impact of liver damage on enzymatic levels?
Which of the following statements about muscle enzymes is true?
Which of the following statements about muscle enzymes is true?
What does the nomenclature 'enzymes + substrate = ES complex' represent?
What does the nomenclature 'enzymes + substrate = ES complex' represent?
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Which factor likely influences the rate of enzymatic reactions?
Which factor likely influences the rate of enzymatic reactions?
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What is the primary function of enzymes in biological systems?
What is the primary function of enzymes in biological systems?
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Which type of enzyme specificity allows an enzyme to catalyze a reaction with only one specific substrate?
Which type of enzyme specificity allows an enzyme to catalyze a reaction with only one specific substrate?
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What role do competitive inhibitors play in enzymatic reactions?
What role do competitive inhibitors play in enzymatic reactions?
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How does substrate concentration affect the rate of enzymatic reactions?
How does substrate concentration affect the rate of enzymatic reactions?
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Which statement is true regarding enzymes in the body?
Which statement is true regarding enzymes in the body?
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Study Notes
Enzymology Overview
- Enzymology is the study of enzymes and their roles in biological processes.
- Clinically significant enzymes help diagnose diseases based on their levels in the blood.
- Enzymes are proteins that catalyze biochemical reactions, enhancing reaction rates.
Enzyme Characteristics
- Enzymes bind substrates at an active site, forming an enzyme-substrate (ES) complex.
- The allosteric site is another area on the enzyme that can influence activity without binding the substrate.
- Enzymes can only catalyze specific reactions based on their structure and the nature of their substrates.
Types of Specificity
- Absolute specificity: Enzyme interacts with only one specific substrate.
- Group specificity: Enzyme interacts with all substrates that have a particular chemical group.
- Bond specificity: Enzyme acts on substrates with a specific type of chemical bond.
- Stereoisomeric specificity: Enzyme interacts with substrates that are specific optical isomers.
Factors Influencing Enzymatic Reactions
- Substrate and enzyme concentration: Michaelis-Menten kinetics; reaction rates depend on the concentration of substrates and enzymes.
- Saturation kinetics: Maximum reaction rate is reached when the enzyme is fully saturated with substrates.
- pH levels: Enzymes have an optimal pH (7.0-8.0); extreme pH can deactivate enzymes.
- Temperature: Increased temperatures generally increase reaction rates up to a point (optimum around 37°C), beyond which enzymes denature.
Inhibitors
- Inhibitors interfere with enzymatic activity.
- Competitive inhibition: Inhibitors compete with the substrate for the active site.
- Non-competitive inhibition: Inhibitors bind to an allosteric site, altering enzyme activity.
- Uncompetitive inhibition: Inhibitors bind the ES complex, preventing a reaction.
Temperature and Storage
- Enzymes are preserved at various temperatures:
- Long-term storage at -20°C.
- Short-term storage in the refrigerator (2-8°C).
- Room temperature (15-30°C) for labile enzymes.
- Avoid repeated freezing and thawing to prevent enzyme inactivation.
Enzyme Structure
- Enzymes consist of amino acids, forming complex structures:
- Primary structure: Specific sequence of amino acids.
- Secondary structure: Twisting of polypeptide chains.
- Tertiary structure: Three-dimensional folding of secondary structures.
- Quaternary structure: Combination of multiple tertiary structures.
Isoenzymes
- Isoenzymes are variants of enzymes that catalyze the same reaction but differ in physical properties.
- Examples include creatine kinase isoenzymes:
- CK1 (CKBB) - Brain
- CK2 - Heart
- CK3 (CKMM) - Muscle
Nomenclature and Classification
- Enzymes are classified based on their activity and reaction types established by the Enzyme Commission (E.C.):
- Oxidoreductases: Oxidation-reduction reactions.
- Transferases: Transfer of groups other than hydrogen.
- Hydrolases: Hydrolysis reactions.
- Lyases: Removal of groups without hydrolysis.
- Isomerases: Isomerization reactions.
- Ligases: Joining of substrates with energy expenditure.
Important Notes
-
Enzymatic elevation in blood indicates cell damage or disease presence.
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Understanding enzyme characteristics and factors influencing their activity is essential for clinical diagnostics.### Enzymes and Their Classifications
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Lactate Dehydrogenase (LDH)
- Systematic Name: L-Lactate: NAD+
- Abbreviation: LDH
- Enzyme Classification: 1.1.1.27, oxidoreductase
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Glucose-6-phosphate Dehydrogenase (G-6-PDH)
- Systematic Name: D-Glucose-6-phosphate: NADP
- Abbreviation: G-6-PD
- Enzyme Classification: 1.1.1.49, oxidoreductase
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Glutamate Dehydrogenase (GLD)
- Systematic Name: L-Glutamate: NAD(P)
- Abbreviation: GLD
- Enzyme Classification: 1.4.1.3, oxidoreductase and deaminase
Aminotransferases
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Aspartate Aminotransferase (AST)
- Systematic Name: L-Aspartate: 2-oxoglutarate aminotransferase
- Abbreviation: GOT (glutamate oxaloacetate transaminase)
- Enzyme Classification: 2.6.1.1
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Alanine Aminotransferase (ALT)
- Systematic Name: L-Alanine: 2-oxoglutarate aminotransferase
- Abbreviation: GPT (glutamate transaminase)
- Enzyme Classification: 2.6.1.2
Kinases and Transferases
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Creatine Kinase (CK)
- Systematic Name: Creatine phosphokinase
- Abbreviation: CPK
- Enzyme Classification: 2.7.3.2
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Gamma-Glutamyl Transferase (GGT)
- Systematic Name: (5-Glutamyl) peptide: amino acid-5-glutamyltransferase
- Abbreviation: GGPT
- Enzyme Classification: 2.3.2.2
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Glutathione-S-Transferase (GST)
- Systematic Name: Glutathione transferase
- Abbreviation: a-GST
- Enzyme Classification: 2.4.1.18
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Glycogen Phosphorylase (GP)
- Systematic Name: Orthophosphate-a-D-glucosyltransferase
- Abbreviation: GP
- Enzyme Classification: 2.4.1.1
Other Enzyme Classes
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Pyruvate Kinase (PK)
- Systematic Name: Pyruvate kinase
- Abbreviation: PK
- Enzyme Classification: 2.7.1.40
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Alkaline Phosphatase (ALP)
- Systematic Name: Orthophosphoric monoester phosphohydrolase (alkaline optimum)
- Abbreviation: ALP
- Enzyme Classification: 3.1.3.1
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Acid Phosphatase (ACP)
- Systematic Name: Orthophosphoric monoester phosphohydrolase (acid optimum)
- Abbreviation: ACP
- Enzyme Classification: 3.1.3.2
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Alpha-Amylase (AMY)
- Systematic Name: 1,2-D-Glucan gluconohydrolase
- Abbreviation: AMS
- Enzyme Classification: 3.2.1.1
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Chymotrypsin
- Systematic Name: Chymotrypsin
- Abbreviation: CHY
- Enzyme Classification: 3.1.21.1
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Trypsin
- Systematic Name: Trypsin
- Abbreviation: TRY
- Enzyme Classification: 3.4.21.4
Isomerases and Lyases
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Aldolase
- Systematic Name: D-D-Fructose-1,6-bisdiphosphate D-glyceraldehyde-3-phosphate-lyase
- Abbreviation: ALD
- Enzyme Classification: 4.1.2.13
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Triosephosphate Isomerase (TPI)
- Systematic Name: Triose-phosphate isomerase
- Abbreviation: TPI
- Enzyme Classification: 5.3.1.1
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Glutathione Synthase
- Systematic Name: Glutathione synthase
- Abbreviation: GSH-S
- Enzyme Classification: 6.3.2.3
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Description
Test your knowledge in Enzymology with this preliminary quiz from CCHM 322. Covering key concepts, including cardiac enzymes and their functions, this quiz is designed to enhance your understanding of the subject matter in the first week. Prepare to challenge yourself and solidify your learning!
