Enzyme Classes Flashcards

Study Notes

Enzyme Classes Overview

Oxidoreductases: Catalyze oxidation-reduction reactions; involve the transfer of electrons where at least one substrate gets oxidized and one reduced.
Transferases: Enzymes that facilitate the transfer of functional groups from one molecule to another, playing a critical role in various metabolic reactions.
Hydrolases: Catalyze the cleavage of bonds through the addition of water; break C-O, C-N, and C-S bonds in hydrolysis reactions by adding OH and H+ ions.
Lyases: Enzymes that cleave substrates without adding water and do not transfer electrons; they are often involved in the reverse reaction which is more biologically significant.
Isomerases: Enzymes that catalyze the interconversion of isomers—both constitutional and stereoisomers; they rearrange atoms within molecules to produce isomers.
Ligases: Responsible for joining large biomolecules, typically through the synthesis of various bonds (C-C, C-S, C-O, C-N) by utilizing the energy derived from ATP cleavage.

Isomer Types

Constitutional Isomers: Molecules that share the same molecular formula but differ in the bonding order of atoms, resulting in distinct compounds.
Stereoisomers: Molecules with the same molecular formula and connectivity as their constitutional isomers but vary in the spatial orientation of their bonds, leading to different properties.

Quick Reference for Enzyme Classes

LIL HOT: An acronym for remembering the classes of enzymes:
- L - Ligases
- I - Isomerases
- L - Lyases
- H - Hydrolases
- O - Oxidoreductases
- T - Transferases

Description

Test your knowledge on different classes of enzymes with these flashcards. Each card provides a term and a concise definition to help you understand the role of oxidoreductases, transferases, and hydrolases in biochemical reactions. Ideal for students and enthusiasts of biochemistry.