Enzymes

mostly proteins that function as biological catalysts

What are enzymes and its role

accelerates chemical processes that reduces the activation energy required for the reaction

function of catalysts

T

t or f

catalysts remain unchanged after a reaction, they are not consumed

exothermic

a reaction where the reactant has lower energy used than the formation of a product

heat/energy

what is used up during exothermic reactions that lowers the Ea of a product

simple enzymes - only has one amino acid chain

conjugated enzymes - has a nonprotein part in addition to a protein part

difference between simple and conjugate enzymes

apoenzyme - inactive protein part

cofactor - nonprotein organic/inorganic moiety

parts of an enzyme

combination of the apoenzyme and the cofactor

what are haloenzymes

catalyzed rate/uncatalyzed rate

catalytic power formula

due to the several amino acids in the active sites that must line up with substrates

why are enzymes considered highly specific

active site

a crevice like location where catalysis happens

substrates

compounds that are being catalyzed

H-bonds

salt links

van der Waals

hydrophobic effect

the interactions that comprises the bonds of the active sites to the substrates

contact - binds reversibly while positioning it in correct orientation; directly involved in a reaction

auxiliary - metal coordination; indirect; only for the stabilization of a molecule

the binding residues of amino acids and their difference

-ase to the name of their substrate

suffix of most enzymes

oxidoreductases

transferases

hydrolases

lyases

isomerases

ligases

six classification of enzymes

redox reactions; oxidases, dehydrogenases

reaction type of oxidoreductases and common nomenclature

transfers a functional group from one molecule to another; kinases, transaminases

reaction type of transferases and common nomenclature

cleaves bonds via the addition of water (hydrolysis); proteases, lipases, amylases

reaction type of hydrolases and common nomenclature

bond cleavage without hydrolysis or oxidation; decarboxylase, aldolases

reaction type of lyases and common nomenclature

intramolecular group transfer to form an isomer, only changes orientation; mutases, isomerases

reaction type of isomerases and common nomenclature

synthesis of covalent bonds between substrates via ATP hydrolysis; idk

reaction type of ligases and common nomenclature

lock and key model

enzyme model with a fixed geometrical conformation; only a specific enzyme can be used to a particular substrate

induced fit

enzyme model where the active site adapts to conformation changes based on the substrate

scissile bonds

type of bond that is susceptible to cleavage or breaking by an enzyme

oxidation - loss of proton

reduction - gain of proton

how do you determine the oxidation or reduction reaction

oxidizing agent - reactant of reduction reaction

reducing agent - reactant of oxidizing reaction

how do you determine the oxidizing/reducing agent in a reaction

1. General Acid-Base Catalysis

2. Metal Ion Catalysis

3. Covalent Catalysis

Enzyme Mechanisms of Action

general acid catalysis

specific base catalysis

Two types of acid-base catalysis

general acid catalysis

a partial proton transfer mechanism from bronsted acid that lowers the free energy of the reaction’s transition state

specific base catalysis

a partial proton abstraction process by a bronsted base that lowers the free energy of a reaction’s transition state

adduct

the product of a direct addition reaction between two or more distinct molecules, where all atoms from the original components are retained in the resulting single molecule

involves the formation of a covalent bond between the enzyme and at least one of the substrates involved in the reaction