What are enzymes?

highly specialized proteins

they are also denatured by the same reagents
main activity is to accelerate or increase biochemical reaction
reaction catalyst there is no reaction/very slow reaction with/out? the
presence of enzymes
they are organic
there are two remarkable traits of enzymes
o 1 They are extremely effective because they increase/accelerate
chemical reactions from 100X to 1000X and more.
Example: Headache, umiinom tayo ng gamut, after 30 mins,
nawawala na yung sakit. Sometimes, nagkaag sanang diit na
lenement, nawala na.
o 2 They are extremely specific.
4 specificities
1 Absolute specificity enzyme catalyzes a single
reaction of a single substrate
2 Group specificity enzyme acts only on certain
functional group in similar chemical environment
3 Linkage specificity enzyme catalyzes the reaction
of a particular functional group regardless of the
surrounding structural environment
4 Stereochemical specificity enzyme will catalyze
only one enantiomeric form of a substrate
present in many processes
2 characteristics
1 enzyme is not changed as a result of catalysis (analogy:
referee)
2 enzyme does not change the equilibrium constant of the
reaction but it simply increases the rate at which the reaction
approaches equilibrium
2 examples:
o LDH lactate dehydrogenase
LDH 1 enzyme found in the heart and red blood cells (normal:
18-27% of the normal total serum)
LDH 2 also found in the heart and red blood cells (27-37% of
the normal total serum)
LDH 3 found in the variety of organs (18-25% of the total
normal serum)
LDH 4 found in the variety of organs (3-8% of the total normal
serum)
LDH 5 found in liver and skeletal muscle (0-5% of the normal
total serum)
o CTK creatin phosphokinase more on the muscle
CTK 1 isoenzyme found in the brain, smooth muscle (0%)

CTK 2 cardiac muscle (35%); skeletal muscle (0%)

CTK 3 all types of muscle (100% of the dominant serum)

Name

Normal activity

Body fluid

Disease/Diagnose

Alanine
aminotransferase

3-17 UL
(international unit
per liter)

Blood serum

Hepatitis

Acid phosphatase

2.5-12 UL

Blood serum

Prostate cancer

Alkaline
phosphatase

13-38 UL

Blood serum

Liver-bone
disease
Cerosis
Bone cancer

Creatin kinase

7-60 UL

Blood serum

Heart attack

19-80 UL

Blood serum

Pancreatic
disease & mumps

Lactic
dehydrogenase
Phospho hexose
isomerase
Amylase

Terminologies:

Apoenzyme an inactive enzyme the protein part of the enzyme has no

cofactor or prosthetic group; it requires cofactor and prosthetic group to
make this enzyme functional
o Cofactor inorganic elements (minerals) pag intense ang kulay
maraming minerals (SO MARAMING MINERALS ANG EYE NI MADAM
the orange eyeshadow)
Holoenzyme an active enzyme has cofactor and prosthetic group
Cofactor small organic or inorganic molecules that is needed by
apoenzymes for its activity
Prosthetic group similar to cofactor, but this prosthetic is tightly bound
Oxyhemoglobin cofactor (blood)
Substrate the ones acted upon by the enzyme; can be an organ, tissue,
cell, functional group, etc.
Substrate binding site a site/location/ place in a substrate where you
find the active site; a particular arrangement in the substrate where you can
find the so called active site
Active site a region in a certain substrate where the enzyme binds;
binding site of the enzyme; arrangement of amino acids; a place in amino
acids where the substrate binds
Isozyme oxidoreductases

Allosteric sites near the active site during the binding of the substrate of
an enzyme
Specificity the ability or property of an enzyme to discriminate between
two competing substrate (analogy: may dalawang tao na friends mo, kung
ikaw BFF ka ng dalawa, alam mong idiscriminate ang bawat isa, wag mong
pagsabayin, isa isa lang! WAG KANG MASYADO!!! Anng galing niya din kasi
mayroon siyang specificity)
Catalyst speeds up or slows down reaction; accelerates chemical reaction
Michaelis-Menten equation (by Leonor Michaelis and Maude Menten)
rate reaction of a substance (how it is accelerated or decelerated); velocity
Activation energy the energy input required to initiate the reaction
Transition state activated form of a molecule
ANG SOBRANG SAKIT, NAKAKAMATAY
Standard free energy change the free energy change for a reaction,
may I repeat, the free energy change for a reaction occurring under a set of
standard condition
Inhibitors substances, they interfere with the reaction and slows down the
rate of reaction; are actually enzymes (example: gas pain)
Coenzyme has the cofactors and prosthetic group; supporter
Allosteric effector substances that modifies the quaternary structure (nagiba na yung shape, parang siya, nag-iba na )
Concerted allosteric effector inactive;
Sequential allosteric effector active;
Zymogen an inactive molecule; (may mga ties that the medicine that was
prescribed, minsan magbibigay ang doctor ng 21 tablets for 21 days,
nakainom ka na ng 7 days, wala ka pang nafifeel na effect, (MANHID KANG
KASMAG KA) dun mo malalaman kung naactivate ito or dai)

HOW DO ENZYME ACTS AS CATALYST?

1. Lock-and-Key Theory of enzyme enzyme-substrate interactions involve
a spatial fit between the enzyme and substrate (-fit together because of
complementary shapes, just as a key fits a lock)
- Proposed by the German Biochemist, Emil Fisher, in the year, 1894
with the concept:
What fits the enzymes active sites best is a substrate molecule
induced to take up the activation chuvaiating the transition state
a. 2 reactions:
1 bukas ang padlock or mga doorlock etc. basta lock. (Parang
puso niya, nakalock na para kay ano)
2 gusto buksan yung lock, another reaction, another padlock)
Parang puso, dating sarado, ngayon bukas na. May pag-asa!!!
Love is blind!!!

2. Induced-Fit theory of Enzyme Action an initial contact of a substrate with

enzyme induces the enzyme to undergo a change in shape so that effective
binding can occur
a. States that the enzyme induces a bound substrate molecule to adapt a
conformation resembling the transition state
b. Explains why similar but not identical substrates can be acted upon by
one enzyme
c. Replacement lang (Parang ako, replacement lang nung nangungulila
siya.)
Proposed by Danielle Koshland, in 1958

Classification of Enzymes
Classified according to nomenclature committee appointed by the
International Union of Biochemistry in 1984. EC (Enzyme Commission divided the
enzyme by six main groups according to the reaction they are reacting)
Names composed of four parts (Number, Main class, Subclass and the Serial
number)
Naming has also a systematic way
1. Recommended Name the convenient form used in regular discourse
(example: lactate dehydrogenase has substrate and has the enzyme
already)
2. Systematic Name more specific, less ambiguous, correspond to one-is-toone with the EC number (example: L-lactate has substrate; L means
levorotatory)
3. Enzyme Commission Numeric Designation example: 1.1,1.27 that
numeric expression represents an enzyme
Six Classification (Divided by EC, name is recommended name)
1. Oxidoreductases enzymes that catalyze the oxidation-reduction between
two substrates (example: Dehydrogenase, Oxidase, Catalase)
2. Transferases enzymes that catalyze the transfer of a functional group
between two substrates (example: Acylalkylglycocyl); transfer the phosphate
group from ATP to another compound (Hexokinase, Transaminases,
Transmethylases)
3. Hydrolases enzymes that catalyze the hydrolysis of esters, carbohydrates
and proteins (polypeptides); involves in hydrolytic reaction and their
reversal; the enzymes that removes phosphate (phosphatases) [esterase,
lipases, proteases, amylase, lactase]
4. Lyases enzymes that catalyze the removal of groups from substrates by
mechanisms other that hydrolysis; involves in elimination reaction in which a

group of atom is removed from a substrate (Aldolase, Decarboxylases,

Dehydratases)
5. Isomerases enzymes that catalyze the interconversion of stereoisomers
and structural isomers; catalyzes molecular isomerization reaction
(Epimerases, racemases, cis & trans-isomerase, UDPta)
6. Ligases enzymes that catalyze the linking of two compounds by breaking a
phosphate anhydride bonds in ATP; also called Synthetase; it forms small
group of enzymes formation of covalent bond joining two molecules together
(Examples: Carboxylases, DNA ligase)

Enzyme

Where bound

Substrate

Product

Hydrolytic Carbohydrases
Thialine

Saliva

Starch and
glycogen or
carbohydrates

Maltose

Sucrase

Intestinal juice

Sucrose

Glucose and
Fructose

Sterases or Lipase
Gastric lipase
Strepsine

Gastric juice/
Stomach
Pancreatic
juice/ pancreas

Fats
Fats

Fatty acids
and glycerol
Fatty acids
and glycerol
Amino acids
sp.
Peptones
Polypeptide
s

Pepsin

Gastric juice

protein

Trepsin

Pancreatic
juice

Peptones and
protein

Peroxidase

Plant and
animal tissues

peroxide

Pxidases

Plants and
animal tissue

Carbs and
protein

Cymase

Yeast

monosaccharide

alcohol

Lactic acidase

Lactic acid
bacteria

Lactose

Lactic acid/
Lactacid

Water and
oxygen
Carbon
dioxide and
water

Coagulating
Rennin

Gastric juice

Milk

Casein