MODULE 1 BIOCHEM REVIEW PACKET #2

<p>A reaction with a negative Gibbs free energy change. (A)</p> Signup and view all the answers

<p>Unsaturated hydrocarbons increase membrane fluidity, while saturated hydrocarbons decrease membrane fluidity. (C)</p> Signup and view all the answers

<p>Transferring amino groups between molecules. (D)</p> Signup and view all the answers

<p>Glyceraldehyde (B)</p> Signup and view all the answers

<p>Breaking down molecules by removing a group without hydrolysis. (C)</p> Signup and view all the answers

<p>Acid-Base Catalysis (B)</p> Signup and view all the answers

<p>Competitive Inhibition (B)</p> Signup and view all the answers

<p>The effector molecule is ONLY the substrate. (B)</p> Signup and view all the answers

<p>Increasing the concentration of the substrate. (D)</p> Signup and view all the answers

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

<p>Hydroxyl group (C)</p> Signup and view all the answers

<p>A low Km indicates a high affinity of the enzyme for its substrate, leading to a more efficient reaction. (A)</p> Signup and view all the answers

<p>The reaction's free energy change is negative, indicating it is endergonic and releases energy. (C)</p> Signup and view all the answers

<p>Glutamic acid (C)</p> Signup and view all the answers

<p>A bond between two monosaccharides where the hemiacetal carbon of one sugar has different stereochemistry as the second sugar. (B)</p> Signup and view all the answers

<p>O-linked glycosidic bond (A)</p> Signup and view all the answers

<p>Enzyme function may be adversely altered or suppressed due to the denaturation of proteins. (C)</p> Signup and view all the answers

<p>The step with the highest activation energy. (B)</p> Signup and view all the answers

<p>Km is the substrate concentration at which the reaction rate is half of its maximum. (A)</p> Signup and view all the answers

<p>A high concentration of substrate and a low Km for the corresponding enzyme. (D)</p> Signup and view all the answers

<p>The corresponding enzyme has a low Km. (C)</p> Signup and view all the answers

<p>Cause: Dietary intake of too much bicarbonate (antacids)/too much acid from plasma; Resulting Change: Increased plasma bicarbonate; Compensation: Increased pCO2 (hypoventilation/decreased breathing rate) (B)</p> Signup and view all the answers

<p>4 (C)</p> Signup and view all the answers

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

<p>Regulation of breathing (A)</p> Signup and view all the answers

<p>Acids and Bases (B)</p> Signup and view all the answers

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

Accumulation of hydrogen ions in plasma, lowering pH.

Decrease of hydrogen ions in plasma, raising pH.

Change in pCO2 in response to acid-base imbalances.

Specific groups of atoms in organic molecules that determine behavior.

Classification system using a 4-digit number for enzymes.

Inability to remove acid from plasma, such as kidney dysfunction.

Enzymes that catalyze the transfer of functional groups between molecules.

Process where ATP hydrolysis drives unfavorable reactions by coupling with them.

Presence of saturated hydrocarbons in membrane lipids decreases fluidity.

A triglyceride consists of three fatty acids bound to a glycerol molecule.

Esterification of fatty acids with glycerol produces water.

Enzymes with low Km have high affinity, ensuring reaction progress even at low substrate levels.

Low substrate 1 allows high substrate 2 to bind more favorably in competitive binding.

Indicates substrate concentration at which reaction rate is half of its maximum.

The slowest step in a reaction pathway that determines overall reaction rate.

A measure of how efficiently an enzyme converts a substrate into a product.

The maximum rate of an enzymatic reaction when the enzyme is saturated with substrate.

A type of covalent bond between monosaccharides with specific stereochemistry, differing at the hemiacetal carbon.

A bond between monosaccharides where both have the same stereochemistry at the hemiacetal carbon.

Attachment of a sugar molecule to a nitrogen atom in another molecule, often in proteins.

Attachment of a sugar molecule to an oxygen atom in another molecule, such as a protein.

High temperatures can adversely affect enzyme activity or protein folding.

Enzyme performance may improve with slight increases in temperature, enhancing metabolism.

Fever may impair carbohydrates' structure and function, affecting metabolism.

Catalysis that uses a partner to orient a substrate by donating or accepting protons.

Catalysis involving partners like metal ions that form temporary bonds with substrates.

Inhibition where an effector competes with the substrate for the active site.

Inhibition where an effector binds outside the active site, reducing enzyme activity regardless of substrate presence.

Regulation where binding at a site other than the active site alters enzyme activity.

Sugars with D configuration are more likely incorporated in human structures.