BIOCHEMISTRY: ENZYMES

ENZYMES  COENZYMES – type of cofactor,

 Protein with catalytic properties due to its specifically organic molecules
power of specific activation
 Catalyze nearly all chemical reactions in the
cells ENZYME SPECIFICITY
 Reacting substance ends with “-ase”  Enzymes have varying degrees of specificity
for substrates
CHARACTERISTICS OF ENZYMES  Enzymes may recognize and catalyze:
 High degree of specificity for their substrate - Single substrate
 Regulatory - Group of similar substrates
 can only alter the rate of reaction - Particular type of bond
 Work under very mild condition of temperature
and pH
 NOT consumed in the reactions they catalyze

ENZYME STRUCTURE
 Enzymes are proteins
 Globular shape
 Complex 3D structure THE “LOCK AND KEY” MODEL
 Active site has a rigid shape
How do enzymes work?  Only substrates with matching shapes can fit
 Enzymes catalyze reactions by weakening  The substrate is a key that fits the lock of the
chemical bonds, which lowers activation active site
energy
 Each enzyme has a unique 3D shape, INDUCED FIT MODEL
including a surface groove called an
 Active site is flexible
ACTIVE SITE
 “maximumize” the fit
 Binds a specific chemical reactant
SUBSTRATE to its active site, causing the  Greater range of substrate specificity
substrate to become unstable and react  More consistent with a wider range of
 The resulting product is released from the enzymes
active site
FACTORS THAT INFLUENCE ENZYME
ACTIVITY
 Enzyme concentration and reaction rate
 Substrate concentration and reaction rate
 Temperature
 pH
!!! When an enzyme is reacting with its  Cofactor and coenzymes
substrate, during the chemical reaction, they are
 Inhibitors
referred as ENZYME SUBSTRATE COMPLEX
ENZYME CONCENTRATION AND
ACTIVE SITE
REACTION RATE
 A region within an enzyme that fits the
 Reaction increases as enzyme concentration
shape of the substrate molecules
increases
 Products are released when reaction is
 Higher enzyme concentrations = more
complete
enzymes catalyze the reaction
 Shape and chemical environment of the
 There is a linear relationship between
active site permits chemical reaction to
reaction rate and enzyme concentration
proceed more easily
SUBSTRATE CONCENTRATION AND
SUBSTRATE
REACTION RATE
 The reactants that are activated by the
 Reaction increases as substrate
enzyme
concentration increases
 Enzymes are specific to their substrates
 Maximum activity occurs when the enzyme
 Determines the specificity
is saturated (when all enzymes are binding
substrate)
COFACTORS AND COENZYMES
 The relationship between reaction rate and
 Non-protein substances (zinc, iron, copper,
substrate is exponential and asymptotes
vitamins) are sometimes needed for proper (level off) when the enzyme is saturated
enzyme activity
 COFACTORS – general term, includes
inorganic and organic molecules
 BIOCHEMISTRY: ENZYMES

TEMPERATURE AND PH - Do not enter active site, but bind to

 Temperatures far above the normal range another part of the enzyme causing it to
DENATURE enzymes change shape
 Most enzymes work best near NEUTRAL - Usually REVERSIBLE
pH (6 to 8)
Example: heavy metals like lead, copper, mercury,
silver

!!! Blocking an enzyme’s activity can kill a

pathogen or correct a metabolic imbalance

Many medications are enzyme inhibitors

CLASSIFICATION OF ENZYMES

Oxidoreductases Oxidation reduction

Transferases Transfer groups of
atoms
Hydrolases hydrolysis
lyases Add or remove atoms
Isomerases Rearrange atoms
The effect of temperature:
Ligases Use ATP to combine
 30C is the optimum temp. molecules
 Some bacterias can withstand 100C
 Most enzymes are denatured at 70C

EFFECT OF pH
 Extreme pH levels will produce denaturation
 Structure of enzyme is changed
 The active site is distorted and the substrate
molecules will no longer fit
 At pH, values are slightly different from the
enzyme’s optimum values, small changes in
the charges of the enzyme and it’s substrate
molecules will occur

COENZYMES: VITAMIN B12

 Vitamins – coenyzmes essential in helping
move atoms between molecules in the
formation of carbohydrates, fats, and
proteins
 Exclusively synthesized by BACTERIA
 Dietary sources – meat, eggs, dairy
products, and supplements

INHIBITORS
 Enzymes that reduce the rate of enzymic
reactions
 Specific and work at LOW concentrations CATECHOLASE
 Block the enzyme but doesn’t destroy it  Present in most fruits and vegetables
 Can be REVERSIBLE and  Facilitates the browning of cut or bruised
IRREVERSIBLE fruits

2 TYPES OF ENZYME INHIBITORS BROMELAIN

1. Competitive inhibitors  Present in pineapples
– resemble an enzyme’s normal substrate  Protease enzyme that facilitates hydrolysis
and compete with it for the active site of protein
- REVERSIBLE depending on  Used as meat tenderizer, breaks down
concentration of inhibitor and substrate collagen in meat
Example : Antabuse – used to help alcoholics quit
drinking, inhibits aldehyde oxidase

2. Non-competitive inhibitor