Clinical Enzymology Quiz

<p>They differ in their spatial arrangement, affecting enzyme specificity (D)</p> Signup and view all the answers

<p>The systematic name can include details about the molecular structure (D)</p> Signup and view all the answers

<p>They transfer phosphate groups during phosphorylation. (C)</p> Signup and view all the answers

<p>Splitting or destroying chemical bonds through hydrolysis. (D)</p> Signup and view all the answers

<p>Class of reaction and subclass of reaction. (C)</p> Signup and view all the answers

<p>Lysis reactions generating double bonds. (C)</p> Signup and view all the answers

<p>They speed up chemical reactions in minute amounts. (C)</p> Signup and view all the answers

<p>Alanine aminotransferase. (C)</p> Signup and view all the answers

<p>They represent the enzyme's trivial name. (C)</p> Signup and view all the answers

<p>They are classified under lyases in nomenclature. (C)</p> Signup and view all the answers

<p>The enzyme undergoes denaturation. (A)</p> Signup and view all the answers

<p>The temperature where the enzyme catalyzes the most reactions per second. (B)</p> Signup and view all the answers

<p>Thermophilic bacteria have enzymes with high optimum temperatures. (A)</p> Signup and view all the answers

<p>It forms a holoenzyme when tightly bound to the enzyme. (A)</p> Signup and view all the answers

<p>It increases the vibrations of the enzyme's atoms. (B)</p> Signup and view all the answers

<p>It is undetectable due to its size. (C)</p> Signup and view all the answers

<p>Lipase levels peak at 24 hours. (D)</p> Signup and view all the answers

<p>Lung Cancer (D)</p> Signup and view all the answers

<p>It facilitates the conversion of lactate to pyruvate. (D)</p> Signup and view all the answers

<p>NAD/NADH (D)</p> Signup and view all the answers

<p>Conversion of aspartate and alpha-ketoglutarate into oxaloacetic acid and glutamic acid (A)</p> Signup and view all the answers

<p>AST and ALT (D)</p> Signup and view all the answers

<p>Liver, heart, skeletal muscle, kidney, pancreas, and RBCs (C)</p> Signup and view all the answers

<p>Competes with the substrate for the active site of the enzyme (B)</p> Signup and view all the answers

<p>5-35 IU/L (B)</p> Signup and view all the answers

<p>Inhibitor binds to the ES complex after the substrate binds (C)</p> Signup and view all the answers

<p>Liver function tests (B)</p> Signup and view all the answers

<p>Oxaloacetic acid and glutamic acid (D)</p> Signup and view all the answers

<p>Stable angina pain resolves with rest, while unstable does not. (C)</p> Signup and view all the answers

<p>Sharp, stabbing pain (B)</p> Signup and view all the answers

<p>Can occur at rest or with minimal exertion (C)</p> Signup and view all the answers

<p>8.3 - 8.9 (A)</p> Signup and view all the answers

<p>It alters their enzymatic properties. (C)</p> Signup and view all the answers

<p>Transient pain after strenuous activity (B)</p> Signup and view all the answers

<p>Colorimetric method (C)</p> Signup and view all the answers

<p>It can occur without any triggers. (B)</p> Signup and view all the answers

Enzymes that catalyze the joining of two molecules, often through the hydrolysis of a diphosphate bond (e.g., in ATP).

Enzymes that move a functional group from one molecule to another.

A systematic name for enzymes that explains the reaction it catalyzes (e.g., L-Lactate: NAD+ oxidoreductase).

Using a systematic system developed by the International Union of Biochemistry, with systematic and trivial names.

Enzymes that catalyze electron transfer.

The specific temperature at which an enzyme functions at its highest rate, catalyzing the most reactions per second.

The process where an enzyme loses its 3D structure and active site due to excessive heat, rendering it inactive.

Enzyme activity decreases as the temperature surpasses the optimum temperature.

Enzymes can catalyze reactions in both forward and reverse directions until equilibrium is reached.

A complete enzyme consisting of an apoenzyme (protein part) and a coenzyme (non-protein part).

Chest pain caused by reduced blood flow to the heart muscle, often a symptom of coronary heart disease.

Lactate Dehydrogenase, an enzyme that converts lactate to pyruvate.

Nicotinamide adenine dinucleotide (NAD) and its reduced form (NADH).

A disease characterized by hardening and narrowing of the arteries supplying blood to the heart, leading to reduced blood flow and potential chest pain (angina) or heart attack.

A heart attack, where the heart muscle is damaged due to lack of blood flow.

Enzymes used to evaluate the extent of liver damage.

Aspartate aminotransferase, also known as serum glutamic oxaloacetic transaminase. It's an enzyme found in various tissues, especially the liver, heart, and muscles.

AST catalyzes the conversion of aspartate and alpha-ketoglutarate into oxaloacetic acid and glutamic acid.

The normal range for AST in blood is typically 5-35 IU/L.

Liver enzymes can be divided into two categories: those that assess liver injury and those that assess biliary obstruction.

A blockage in the bile duct, preventing bile from flowing to the gallbladder.

An inhibitor molecule competes with the substrate for binding to the enzyme's active site.

An inhibitor binds to a different site on the enzyme, altering its shape and preventing proper substrate binding.

There are two main types of chest pain: Stable Angina and Unstable Angina.

Chest pain that occurs during strenuous activity and resolves with rest. It is usually predictable and triggered by exertion.

Chest pain that is unpredictable and can occur at rest or with minimal exertion. It is a warning sign of a possible heart attack.

Classic angina typically presents with chest pain that feels like squeezing, burning, or pressure, and can be accompanied by difficulty breathing.

A-Hydroxyurea is a chemical inhibitor used in a specific enzyme analysis method.

The Wacker method is the gold standard for measuring the activity of a specific enzyme used in heart attack diagnosis.

The Wacker method is preferred for measuring LD-1, an enzyme that is specifically elevated in heart attacks.

Enzyme activity can be measured through kinetic or colorimetric methods in the Wacker method.

A unique numerical code assigned to each enzyme, based on its function and the specific reaction it catalyzes.

Enzymes are categorized into six classes based on their primary reaction type: Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, and Ligases.

Hydrolases catalyze hydrolysis reactions, which involve the breaking of bonds through the addition of water.

Hydrolases include enzymes like lipases (break down fats), proteases (break down proteins), nucleases (break down nucleic acids), amylases (break down carbohydrates), and phosphatases (remove phosphate groups).

Lyases catalyze lysis reactions that generate a double bond, without the involvement of water.

Lyases include enzymes like decarboxylases (remove carbon dioxide) and aldolases (break down sugars).

Enzymes are biological catalysts, meaning they speed up chemical reactions without being consumed. They are also required in minute amounts.

Enzyme nomenclature provides a standardized system for naming enzymes based on their function and the specific reactions they catalyze. This helps to ensure clarity and consistency in scientific communication.