Introduction to Enzymes and Their History

<p>Various bonds by adding water (D)</p> Signup and view all the answers

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

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

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

<p>They catalyze reactions by adding water across a bond. (C)</p> Signup and view all the answers

<p>They are consumed during the reaction they catalyze. (C)</p> Signup and view all the answers

<p>Enzymes were considered inseparable from living cells for activity. (D)</p> Signup and view all the answers

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

<p>It creates a favorable chemical environment for a specific reaction to occur. (B)</p> Signup and view all the answers

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

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

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

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

<p>Carbonic anhydrase enhances the hydration of $CO_2$ by a factor of $10^7$. (D)</p> Signup and view all the answers

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

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

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

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

<p>37 ℃, physiological pH, and ambient atmospheric pressure (D)</p> Signup and view all the answers

<p>$10^{3}$ to $10^{17}$ (B)</p> Signup and view all the answers

<p>Requirement for extreme reaction conditions (D)</p> Signup and view all the answers

An enzyme that converts glucose and ATP into glucose-6-phosphate and ADP.

A molecule that provides energy for cellular processes.

The phosphorylated form of glucose, important for metabolism.

Enzymes that catalyze oxidation-reduction reactions.

Enzymes that transfer functional groups between molecules.

Enzymes that catalyze the hydrolysis of bonds using water.

A type of transferase that transfers phosphate groups.

Enzymes that remove amine groups from molecules.

The measure of how fast an enzyme catalyzes a reaction, typically much faster than uncatalyzed reactions.

The ability of an enzyme to interact with only one or a few specific substrates, catalyzing a unique reaction.

Enzymes operate best at physiological temperatures, pH, and pressure, unlike many chemical reactions.

A type of specificity where an enzyme catalyzes only one reaction and one substrate.

A general term for enzymes that can act on multiple substrates having certain common features.

An enzyme type that will act on substrates with specific functional groups, like amino or phosphate groups.

Enzymes that act on certain types of chemical bonds irrespective of the rest of the molecule.

Enzymes that act on a specific steric or optical isomer of a molecule.

Proteins that act as biological catalysts to accelerate chemical reactions.

The specific region on an enzyme where substrate molecules bind and undergo a chemical reaction.

Building blocks of proteins, each with unique side chains that determine their properties.

Amino acids with non-polar side chains that repel water, impacting protein structure.

Amino acids with positively charged side chains at physiological pH, such as lysine and arginine.

Amino acids with negatively charged side chains at physiological pH, like aspartic acid.

Proteins that have a spherical shape, which is crucial for their function as enzymes.

Historical term for enzymes, especially those studied in fermentation processes.