I.

OVERVIEW  Contains amino acid chains that participate in substrate

binding and catalysis
 ENZYMES  Held together by HYDROGEN BONDS
 Protein catalysts that increases rate of reaction  Highly specific
without being consumed or changed within the
process
 Direct all metabolic events

II. NOMENCLATURE

A. Recommended Name

 Most commonly used enzyme names have the suffix “-ase”

attached to the substrate of the reaction (e.g. Glucosidase,
Urease)
 Description of the actin performed (e.g. Lactate
dehydrogenase, Adenylyl cyclase)
 Some enzymes retain trivial names – no hint on the reaction  LOCK AND KEY
(e.g. Pepsin, Trypsin)  Enzyme is the lock; Substrate is the key
 No changes were made
B. Systematic Name
 Perfect fit
 7 major classes
 For a given enzyme, “-ase” is attached to a fairly complete  INDUCED FIT
description of the chemical reaction catalyzed (e.g.  Conformational change and adjustments were
lactate:NAD+ oxidoreductase) made (Ipinilit cutie haha)

B. Catalytic efficiency

III. FUNCTIONS
 biologic polymers that CATALYZE the chemical reactions
by factors of at least 106.
 essential for the BREAKDOWN OF NUTRIENTS to
supply energy and chemical building blocks.
 Important in the assembly of:
 proteins, DNA, membranes, cells, and tissues;
 Harness energy to power cell motility, neural function,
and muscle contraction.
 Protein catalysts
 Isozymes are physically distinct versions of a given
enzyme, each of which catalyzes the same reaction (e.g.
Hexokinase and Glucokinase)
IV. PROPERTIES
A. Active sites
 Highly efficient
 Proceeds from 10^3 to 10^8 times faster than uncatalyzed
reactioons
 TURNOVER NUMBET (kcat) – number of molecules of
substrate converted to product per enzyme molecule per
second (10^2 to 10^4s^-1)
C. Specificity
 Highly specific
 Interacts with one or a few substrates
 Catalyzes only one type of chemical reaction
D. Holoenzyme
 Enzyme + Nonprotein component
 APOENZYME – Enzyme without nonprotein
component
 NONPROTEIN COMPONENT – can either be a
COENZYME OR COFACTOR
o COENZYME – serve as recyclable shuttles or
group transfer agents that transport many
substrates from the point of generation to point of
utilization (e.g. small organic molecules)
 COFACTOR – bind in a transient, dissociable
o
manner either to the enzyme or to a substrate
(e.g. vitamins or metals)
 COENZYME – can either be COSUBSTRATE or
PROSTHETIC GROUP
o COSUBSTRATE – dissociate from the enzyme
in the altered state (e.g. NAD+)
o PROSTHETIC GROUP – distinguished by
their tight, stable incorporation into a protein's
structure by covalent or noncovalent forces;
permanently associates with the enzyme (e.g.
FAD+)

V. HOW ENZYMES WORK?

 Ezymes lower free energy of activation
 Can be regulated or inhibited
 Enzymes don’t change the energy of the reactants and
products, and the equilibrium of the reaction.

COFACTOR vs. EFFECTORS

NOTE:

 Cofactors are essential for function.

 Effectors are optional.
 Most vitamins, especially the water-soluble ones, serve as
cofactors for chemical reactions, which is why they are
important.
 In the absence of these vitamins, the enzymes will not
work.

E. Regulation

 Can be regulated
 INCREASED or DECREASED

F. Location within the cell

 Localized in specific organelles within the cell

 Compartmentalized to isolate the reaction substrate or
product from other competing reactions