Cofactors in Enzymatic Activity

<p>The synthesis of enzymes requires the transcription and translation of DNA. (D)</p> Signup and view all the answers

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

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

<p>To assist the enzyme in binding to the substrate and/or stabilizing the transition state. (B)</p> Signup and view all the answers

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

<p>Iron in Hemoglobin (A)</p> Signup and view all the answers

<p>They can help the enzyme perform chemical reactions that it wouldn't be able to do on its own. (C)</p> Signup and view all the answers

<p>Flavin adenine dinucleotide (FADH) (D)</p> Signup and view all the answers

<p>Some cofactors can be permanently attached to the enzyme. (B)</p> Signup and view all the answers

<p>Coenzymes can be used by multiple enzymes, whereas prosthetic groups are enzyme-specific. (D)</p> Signup and view all the answers

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

<p>Activation of caspases (C)</p> Signup and view all the answers

<p>Apoptosis involves cell fragmentation while necrosis does not (B)</p> Signup and view all the answers

<p>To serve as inactive enzyme precursors (C)</p> Signup and view all the answers

<p>Intrinsic and extrinsic pathways (B)</p> Signup and view all the answers

<p>To prevent enzymes from digesting the cells they are synthesized in (A)</p> Signup and view all the answers

<p>Pepsinogen (A)</p> Signup and view all the answers

<p>It activates the enzyme by converting it to its active form (B)</p> Signup and view all the answers

<p>Acute pancreatitis (A)</p> Signup and view all the answers

<p>The acini are separated by thin fibrous barriers (A)</p> Signup and view all the answers

<p>To assist in the catalytic function of enzymes (B)</p> Signup and view all the answers

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

<p>A tightly bound cofactor that forms covalent bonds (A)</p> Signup and view all the answers

<p>They must be obtained from the diet (B)</p> Signup and view all the answers

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

<p>It is converted to a holoenzyme (B)</p> Signup and view all the answers

<p>They can be either tightly or loosely bound to enzymes (B)</p> Signup and view all the answers

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

<p>Autocatalyzes the conversion of pepsinogen to pepsin (B)</p> Signup and view all the answers

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

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

<p>Small peptides and free amino acids (D)</p> Signup and view all the answers

<p>Gastric acid (HCl) (A)</p> Signup and view all the answers

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

<p>Proteins -&gt; small peptides -&gt; amino acids (A)</p> Signup and view all the answers

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

<p>To cleave amino acids from the N-terminus of peptides (B)</p> Signup and view all the answers

<p>Proteolytic activation of enzymes (A)</p> Signup and view all the answers

An inactive precursor of an enzyme, activated by cleavage.

An inactive zymogen that converts to pepsin in the stomach for digestion.

Inactive precursor of trypsin, activated in the pancreas.

Process that activates zymogens by cleaving peptide bonds.

Exocrine pancreatic cells that secrete zymogens in granules.

A coenzyme that synthesizes blood coagulation factors II, VII, IX, and X.

A drug that reduces blood clot formation by depleting active Vitamin K.

Programmed cell death mediated by caspases, resulting in no inflammation.

Proteolytic enzymes that execute apoptosis by degrading proteins.

Small molecules that assist enzyme activity.

Organic cofactors that are vital for enzyme function.

Tightly bound cofactors that remain attached to enzymes.

Mechanisms that control enzyme activity and function.

Metal ions that assist enzymes, like Zn and Mg.

Coenzymes that are organic molecules aiding enzymes.

Effectors that are different from the enzyme's substrate and influence enzyme activity.

Reversible addition or removal of chemical groups, primarily phosphate, that alters enzyme activity.

Regulation of enzyme activity through the binding of effectors at sites other than the active site.

Regulation of enzyme synthesis that controls enzyme levels based on developmental or physiological needs.

A mechanism where the end product of a metabolic pathway inhibits an earlier step in the pathway.

The inactive form of an enzyme that requires a cofactor to become active.

The active form of an enzyme, consisting of an apoenzyme and its cofactor.

Vitamins are essential nutrients that must be obtained from diet.

A coenzyme associated with gene regulation and histone modification.

Active enzyme that digests proteins in the stomach.

Zymogen that is converted to chymotrypsin by trypsin.

Zymogen activated to carboxypeptidase for protein digestion.

Inactive enzyme that converts to elastase in the digestive process.

Enzyme that activates trypsinogen to trypsin in the small intestine.

Series of enzyme activations in blood clotting or protein digestion.

Series of proteolytic activations in blood clotting.