What are Enzymes?
o carboxypeptidase – only catalyze the
Hundreds of chemical reactions take place in our
cells every second of our life. Karamihan sa mga
chemical reactions na ito are catalyzed by enzymes,
which are large biological molecules that increase
the rates of chemical reactions in our body.
Pinapabilis ng enzyme yung mga chemical reaction
na kailangan ng katawan natin by lowering the
activation energy of the reaction. Kung walang
enzymes na nagsisilbing biological catalyst, siguro
sobrang gulo ng system natin. Enzymes are very
vital just for example when breaking down food
molecules. Pinapabilis ng digestive enzyme yung
pagdigest so that the food that we ate can quickly
provide the energy and nutrients na kailangan natin
to survive. Without enzymes, siguro kahit kumain
tayo ng kumain, hindi agad tayo mabubusog dahil
nga walang enzyme na nagaact as a catalyst.
Every organism has many enzymes—more
than 3000 in a single cell.
What are ribozymes?
Protein enzymes are known to be a biological
catalyst. Pero not only proteins but also Ribozymes,
which are enzymes made of ribonucleic acids or the
RNA. Ribozymes catalyze or should I say mas
pinapabilis nila yung self-cleaving factor of some
portions ng sarili nilang molecules. Self-cleaving is
yung voluntary splitting of chemical bonds.
Ribozymes are also involved sa mga reactions na
naggegenerate ng peptide bonds. In the field of
biochemistry, maraming mga naniniwala na mas
nauuna na lumabas yung mga RNA catalyst during
evolution of cells, followed by the protein enzymes
later on.
2 Distinct Feature of Enzymes
 They are extremely effective, increasing reaction
rates by anywhere from 10 9 to 1020 times.
(digesting food w enzymes: 10 – 20 mins,
without enzymes: 24 hrs)
 Most of them are extremely specific. So may
mga enzyme na pinapabilis lang nila ang isang
reaction or isang klase ng reaction. So parang
that specific enzyme is only made for that
specific reaction.
o Example is the enzyme urease which only
catalyzes the hydrolysis (adding water) of
urea.
o trypsin, enzyme na nagca-catalyzes sa
hydrolysis ng peptide bonds of protein
molecules—pero hindi lahat ng peptide
bond, yun lang mga nasa carboxyl side of
lysine and arginine residues
hydrolysis ng huling amino acid sa protein
chain—yung nasa C-terminal end.
o Lipases naman are less specific:
pinapabilis nila yung hydrolysis ng kahit
anong triglyceride, but do not affect
carbohydrates or proteins.
Hydrolysis
So literal meaning nya is to spilt water. Hydrolysis
is a chemical process kung saan nagrereact ang
organic chemical with water para makabuo ng 2 o
higit pang new substances and break the chemical
bond in the compound. Yung molecule ay nahahati
into two parts by adding molecule of water. For
example, yung ions ng salt was dissolved sa certain
solution, let’s say water, that will create 2 new
substances which are hydroxide and hydronium. Sa
reaction na yan, one fragment of the target
molecule or yung parent molecule gains a hydrogen
ion.
o Pati strong acid ay naguundergo din sa
hydrolysis. For example, dissolving sulfuric
acid (H2SO4) in water is accompanied by
hydrolysis to produce hydronium and
bisulfate, the sulfuric acid's conjugate base.
Location of Enzymes
Yung mga enzymes natin sa katawan ay kalatkalat
depende kung saang part ng body natin need
magcatalyze ng specific reaction
o Proteases are in the blood, needed to
promote clotting.
o digestive enzymes are located in the
secretions of the stomach and pancreas.
o enzymes that catalyze the oxidation of
compounds that are part of the citric acid
cycle are located in the mitochondria
o lysozyme that catalyzes the dissolution of
bacterial cell walls are found in lysosome
How Are Enzymes Named and Classified?
Madalas yung mga pangalan ng enzymes ay based
sa reaction or compound na kina-catalyze nila.
o For example, pinapabilis ng lactate
dehydrogenase yung removal ng
hydrogen from lactate, so yung name nya is
dehydrogenase.
o Yung acid phosphatase naman
pinapabilis nya yung hydrolysis of
phosphate ester bonds under acidic
conditions.
Karamihan sa mga enzymes ay may suffix na “-ase.”
Yung iba naman, may mga assigned names na
sakanila dati pa bago pa natin maintindihan yung
functions nila. Example of these are pepsin, trypsin,
and chymotrypsin na lahat ay enzymes ng digestive
tract.
6 Groups of Enzymes
Enzymes can be classified into six major groups based sa
type ng reaction that they catalyze
 Oxidoreductases catalyze oxidations and reductions.
 Transferases catalyze the transfer of a group of
atoms, such as from one molecule to another.
 Hydrolases catalyze hydrolysis reactions.
 Lyases catalyze the addition of two groups to a
double bond or the removal of two groups from
adjacent atoms to create a double bond.
 Isomerases catalyze isomerization reactions.
 Ligases, or synthetases, catalyze the joining of two
molecules.
1. OXIDOREDUCTASES
- which move electrons between molecules
- includes two different types of reactions. And these
reactions involve transferring electrons from either
molecule B to molecule A or from molecule A to molecule
B. Oxidase ay involved sa oxidizing or pagtanggal ng
electrons sa molecule, while a reductase is involved in
reducing or pagbibigay ng electrons sa molecule kaya ito
tinawag na oxidoreductases dahil pwede silang ma-
catalayzed both the forward and reverse reactions.
EXAMPLE:
LACTIC ACID FERMENTATION
where in electrons are either magpa-passed sa NADH
(nicotinamide adenine dinucleotide (NAD) + hydrogen
(H)." at ito ay nago-occurs naturally sa ating body at
plays a role in the chemical process that generates
energy.) to pyruvate or from lactic acid to NAD. Dahil
doon naka-catalyzed ito ng kind of an enzyme called
lactate dehydrogenase. At dahil ito ay dehydrogenase
which refers to the removal of a hydride functional
group, ire-remove natin ang electrons . Since hydrides
are basically just hydrogen atoms na mayroong dalawang
electrons on them instead of just one. Kaya ito tinawag
na Lactic Acid Fermentation ay dahil kaya nitong
tanggalin ang hydride, or remove electrons, from a
molecule of lactic acid.
2. TRANSFERASE
- transfer functional groups from one molecule to
another
- catalyze by moving some functional group, X, from
molecule B to molecule A.
EXAMPLE:
PROTEIN TRANSLATION
where amino acids na nagbound sa tRNA molecules are
transferred patungo sa growing polypeptide chain. So in
this case, A refers to our amino acid chain, B refers to
our tRNA, and X refers to this lysine residue, which is
being transferred from B to A. At itong reaction na ito ay
particular na kina-catalyzed by an enzyme called
peptidyl transferase, which is an appropriate name since
ang enzyme na transferase involved sa pag-gawa ng
peptides.
3. HYDROLASES
- which break bonds using water
- use water to cleave a molecule, like molecule A, into
two other molecules, B and C.
EXAMPLE:
HYDROLYSIS REACTION
Yung reaction na iyon ay nago-occur to peptide bonds. At
kapag mayroong lysine-alanine dipeptide naman ay
maaring mag-react ito sa tubig para mag-form ng two
individual amino acids that are no longer bound. At dahil
doon ang hydrolysis reaction ay maaring ma-catalyzed
ng isang klase ng enzymes na tinatawag na serine
hydrolases or serine proteases. And they are named that
way dahil sila ay mga hydrolases that use a serine
residue as the key catalytic amino acid na responsible sa
pag-sira ng peptide bond.
4. LYASES
-which break bonds without using water and without
using oxidation.
- nagka-catalyze ng dissociation sa molecule, like
molecule A, into molecule B and C, without using water
katulad ng hydrolases at hindi din ito gumagamit ng
oxidation or reduction like an oxidoreductase would.
EXAMPLE:
CLEAVAGE OF ARGININOSUCCINATE INTO
ARGININE AND SUCCINATE
Yung reaction na ito ay nagte-takes place during the urea
cycle. At dahil doon ang specific reaction na nagka-
catalyzed ay tinatawag na argininosuccinate lyase. In
which it is the appropriate named dahil ang lyase ag
siyang nagka-catalyze sa pagsira ng argininosuccinate
molecule. Mahalaga na ma-recognize ito since ang lysase
ay hindi ginagamitan ng tubig or oxidation sa pagsira ng
bond, hence, kailangan muna nila mai-generate either a
double bond between two atoms o yung ring structure sa
molecule in order to work.
5. ISOMERASE
- which convert a molecule from one isomer to another.
EXAMPLE:
CONVERSION OF GLUCOSE-6-PHOSTATE TO
FRUCTOSE-6-PHOSPHATE
in which isa ito sa steps of glycolysis. Yung reaction na
iyon ay maka-catalyzed by an enzyme called
phosphoglucose isomerase. At kaya ito appropriate
named since it creates isomers of glucose molecules that
are phosphorylated.
6. LIGASES OR SYNTHETASES
- the two molecules are being ligate or join together
- catalyzes reactions between two molecules, A and B,
that are combining to form a complex between the two,
or AB.
EXAMPLE:
DNA REPLICATION
where in yung dalawang strands ng DNA are being
joined together. So in this reaction, yung molecule A and
B ay nagre-represent sa dalawang separated DNA
polymers, which are being joined to form a single strand.
At dahil doon, nagkakaroon ng catalyzation by an
enzyme called DNA ligase, kaya ito tinawag na DNA
ligase ay dahil ang specific na enzyme na nagwork sa
DNA strand ay ang ligase
Terminology Used with Enzymes
 Cofactors: May mga enzymes like pepsin and
trypsin na gawa lang sa polypeptide chains.
Yung iba naman ay may mga nonprotein
portions which is called cofactors. Ito yung mga
nonprotein parts ng enzymes na kailangan sa
catalytic function. Ang cofactor can be metallic
ions, like zinc and magnesium ion or mga
organic compounds. Kapag ang isang metal ion
ay cofactor, kaya nyang kumapit or magbind
directly sa protein or sa coenzyme.
 Coenzymes ang tawag sa mga organic
cofactors. These are frequently B vitamins that
act as cofactors. An important group of
coenzymes are the B vitamins, na sobrang
important sa activity ng karamihan ng mga
enzymes. Another na mahalagang coenzyme is
yung heme, na part ng oxidoreductase at ng
hemoglobin.
 Yung compound na kina-catalyze or pinapabilis
ng enzymes is called the substrate. Ito
madalas yung nagbibind sa surface ng enzyme
habang nag-undergo ng reaction. Kumakapit or
nagjojoin yung substrate sa specific portion ng
enzyme during the reaction, at yang specific
portion is called the active site
 Kung merong coenzymes ang specific enzyme,
madalas makikita yon sa active site. Active
site is three-dimensional cavity of the enzyme
na may mga specific chemical properties, so
that it can accommodate the substrate.
 Activation is any process na nagi-initiate or
nagpapataas, or nagtritrigger sa actions ng
enzyme. Pwedeng trough adding a cofactor sa
apoenzyme or cleaving ng polypeptide chain ng
proenzyme
 Inhibition is the opposite of activation. This is
a process that makes an active enzyme less
active or inactive. So ang isang compound ay
nagjojoin or nagbibind sa enzyme para
pababain yung activation rate nya.
Yung mga competitive inhibitors ay nagjojoin or
kumakapit sa active site ng enzyme surface. So
mapipigilan non yung binding ng substrate.
Noncompetitive inhibitors naman ay nagbi-
bind to some other portion ng enzyme surface. This
alter the tertiary structure ng mga enzyme para
yung catalytic effectiveness ng enzyme ay mawala.
That’s the reason kung bakit hindi pwedeng
magcatalyze ng enzyme habang nakabind pa yung
inhibitor
What Factors Influence Enzyme Activity?
Minemeasure ng enzyme activity kung gaano kataas
yung inincrease ng enzymes sa reaction rate ng
certain reactions. There are lots of factors na
nakakaapekto sa enzyme activity such as
concentration, temperature, and pH.
Enzyme and Substrate Concentration
Kung hahayaan natin na yung concentration ng
substrate ay constant, at tataasan natin yung
concentration ng enzyme, then the reaction rate
will increase linearly. So kung dodoble yung
enzyme concentration, dodoble din yung reaction
rate. Kung 3 times higher yung concentration ng
enzyme, 3 times higher din yung reaction rate and
so on. This is the case basically sa lahat ng enzyme
reactions dahil yung molar concentration ng
enzyme ay almost always mas mababa compared sa
substrate. And that is also the reason kung bakit
mas maraming molecules ng substrate ang present
compared sa molecules ng enzymes. Basta
constant yung substrate concentration,
temperature, at pH, always magi-increase
linearly yung reaction rate of an enzyme-
catalyzed reaction.
Kung yung concentration naman ng enzyme yung
constant and we will increase the concentration of
substrate, magkakaroon ng tinatawag na saturation
curve. So in this case, hindi nataas ng tuloytuloy
yung rate. Instead, may certain point lang kung
saan dun lang nagststay yung rate, kahit na i-
increase pa yung substrate concentration. This
happens because
sa saturation point, substrate molecules are bound
to all available active sites of the enzymes. So dahil
nangyari yung reaction sa active sites, once na
napuno yung mga yon, the reaction will then
proceed sa pinakamataas or maximum na reaction
rate. So kahit na i-increase pa yung substrate
concentration, hindi na tataas yung reaction rate
dahil wala nang mahanap na active sites yung
excess substrate to bind with. So, kapag yung
Enzyme concentration, temperature, and
pH are constant, the effect of substrate
concentration on the rate of an enzyme-
catalyzed reaction is saturation curve.
Temperature (Substrate and enzyme
concentrations and pH are constant)
Nakakaapekto ang temperature sa enzyme activity
dahil binabago ng temperature yung conformation
ng enzyme. In uncatalyzed reactions, the rate
usually increases habang tumataas yung
temperature. Sa enzyme-catalyzed reactions
naman, pag nagstart tayo sa low temperature,
magcacause muna yung increase in temperature ng
increase in rate. Pero sobrang sensitive ng protein
conformations when it comes to temperature
changes. Once na nareach na yung optimal
temperature or yung highest point, magkakaroon
na ng alteration or pagbabago sa enzyme
conformation once na tinaasan pa ulit yung
temperature. So may chance na hindi magfit or
magconform yung substrate sa changed enzyme
surface, kaya usually, bumababa yung rate ng
reaction.
Kung meron namang small temperature increase
above the optimum level, pwede ulit taasan yung
decreased rate by lowering the temperature,
because over a narrow temperature range, madalas
reversible yung changes sa enzyme conformation.
Pero kapag sobrang taas yung temperature above
the optimum, may point where the protein
denatures so irreversible na sya, and yung
polypeptide chain hindi na mababalik sa original
conformation nya. So at this point, completely
deactivated na yung enzyme
Kapag naman below the optimum temperature,
nagdedecrease yung reaction rate with decreasing
temperature. So nangyayari to madalas when we
preserve our foods through refrigeration. So
binabaan natin yung temperature para lumamig, so
once na we put let say yung food sa ref,
madedeactivate yung enzymes, and that is the
reason bakit hindi agad nasisira yung food pag nasa
ref.
pH (Substrate and enzyme concentrations and
temperature are constant)
Kapag nagbabago ang temperature, it is also
expected na magkakaroon ng ph related effects. Ph
influence the enzyme activity dahil binabago ng pH
ng environment ng protein yung conformation nya.
Laht ng enzyme ay nagfufunction with their certain
Ph. So tulad ng temperature, within narrow pH
range, reversible pa rin yung changes. Pero pag
sobrang taas or baba na yung pH values (either
acidic or basic), magiging denatured and
irreversible na yung enzymes. Pati yung enzyme
activity hindi na pwedeng irestore by changing
back sa optimal Ph
Mechanisms of Enzyme Action
Enzymes are highly specific for a substrate. About
100 years ago, sinuggest ni Arrhenius, which is a
Swedish scientist na pinapabilis daw ng catalysts
yung mga reactions by combining with the
substrate para magform ng isang uri ng
intermediate compound. Sa enzyme-catalyzed
reaction, this intermediate is called the enzyme–
substrate complex.
1. Lock-and-Key Model
Para mafigure out yung high substrate
specificity (the limitation of an enzyme to
catalyze specific reactions with specific substrates)
ng karamihan sa mga enzyme-catalyzed reactions,
maraming models ang prinoposed and one of these
is the Locke-and-Key Model. This was claimed na
itong model na to ay yung simplest at
pinakamadalas gamitin as reference. So sinasabi sa
model na to that enzyme is a rigid (or stiff,
unflexible) three-dimensional body. Yung surface
na naglalaman sa active sites ay may restricted
opening tas only one kind ng substrate yung kasya
dito, parang yung tamang susi lang yung magfifit
exactly sa lock para mabuksan. So this explains
the specificity of enzyme action by
comparing the active site to a lock and the
substrate to a key
According to this model, may particular shape yung
mga enzyme molecule kasi yung shape na yon is
important para mamaintain yung active site sa
exact conformation na kailangan para sa particular
reaction. An enzyme molecule is very large, siguro
they are made about 100 to 200 amino acid
residues, pero yung active site usually ay gawa
lang sa two or a few amino acid residues, na
makikita sa different areas sa chain.
2. Induced-Fit Model
Yung size and shape ng active site cavity ay
nagbabago kapag pumapasok yung substrate. To
explain this phenomenon, inintroduced ng
American biochemist na si Daniel Koshland yung
Induced-Fit Model where he compared the changes
na nangyayari sa shape ng cavity when it bind to
changes sa shape ng glove when a hand is inserted.
Bale this model explains the specificity of
enzyme action by comparing the active site
to a glove and the substrate to a hand. So,
midomodify ng enzyme yung shape ng active site
para iaccomodate yung substrate. So just like when
we wear gloves, nagcoconform yung gloves sa hand
natin.
Actually pareho lang yung lock-and-key and
induced-fit model na ineexplain yung phenomenon
of competitive inhibition. So nagfifit yung inhibitor
molecule sa active site cavity in the same way the
substrate does, so napreprevent makapasok yung
substrate. So ang kakalabasan, kahit anong reaction
yung expected na mangyayari sa substrate, hindi na
mangyayari.
3. Catalytic Power of Enzymes
The chemistry at the active site is actually the most
important factor sa enzyme action. So merong five
amino acids na nagpaparticipate sa active sites in
more than 65% of all cases. Karamihan sa mga
amino acids na ‘to have either acidic or basic side
chains. So acid–base chemistry often underlies the
mode of catalysis. Sabi nga, hindi kayang baguhin
ng enzymes yung thermodynamic relationships
between the substrates and the products of a
reaction, rather ,pinapabilis nila yung reaction.
So sa diagram ng hypothetical reaction may mga
reactants sa isang side and products naman sa
kabila. Yung thermodynamic relationship is yung
height difference between reactants and products.
Dapat mag-undergo sila sa transition state where
they are something in between. Madalas na
rinerefer to as “energy hill” na kailangang paakyatin
or pataasin. Yung energy na kailangan para
umakyat ay yung activation energy. Sobrang
powerful catalyst talaga ng enzymes kasi kaya
nilang pababain yung energy hill. Bale binabaan
nila yung activation energy
The way paano binababaan ng enzymes yung
activation energy is very specific sa enzyme at sa
reaction na kina-catalyze. There are only few amino
acids na nagaappear most of the active sites. Yung
specific amino acids sa active site at yung exact
orientation nila make it possible for the substrate(s)
na magbind sa active site at magreact para
makabuo ng products.
Example: papain is a protease, which is an enzyme
that cleaves peptide bonds like trypsin. May 2
important amino acids na present sa active site ng
papain. Yung histidine tumutulong sya to attract
the peptide and hold it in sa tamang orientation via
hydrogen bonding. Yung sulfur sa cysteine side
chain performs a type of reaction called a
nucleophilic attack sa carbonyl carbon ng
peptide bond. Ito ay isang chemical reaction kung
saan nagbobond ang electron-rich atom tulad ng
oxygen or sulfur sa electron-deficient atom like
carbonyl carbon. Naga-appear yung nucleophilic
attacks sa karamihan ng enzyme mechanisms, and
they are possible dahil sa precise arrangement ng
mga amino
acid side chains na nagpa-participate sa ganitong
uri ng organic reaction.
How Are Enzymes Regulated?
1. Feedback Control
Madalas nareregulate ang mga enzymes ng
environmental conditions. Yung Feedback control
is an enzyme regulation process kung saan
pinipigilan ng formation ng product yung earlier
reaction sa sequence. Yung reaction product ng
isang enzyme ay kayang icontrol yung activity ng
isa pa, lalo na sa mga complex system where
enzymes work cooperatively. Yun nga, yung final
product sa chain ay pwedeng pigilian yung activity
ng first enzyme through competitive, non
competitive, or other types ng inhibition. Kapag
mababa yung concentration ng ng final product,
bibilis lahat ng reaction. Pero habang tumataas
yung concentration, napipigilan yung actions ng
enzymes and eventually titigal na. So yung
pagsasamasama or accumulation ng final products
serves as a message or feedback na nagsasabi sa
enzymes to shut down dahil enough na yung final
product ng cells based sa needs nya. And with that,
kapag nagshutdown na yung enzyme, titigil na rin
yung entire process.
2. Proenzymes
May mga enzymes na prinoduced yung katawan
natin na nasa inactive form, ibig sabihin they do not
exhibit any action or activity. Para maging active
sila, kailangan magtangal ng small part ng kanilang
polypeptide chain. These inactive forms of enzymes
are called proenzymes or zymogens. Proenzymes
ang tawag kapag ang enzymes ay nasa inactive form
tas naging active after undergoing a chemical
change also called zymogens. Kapag zymogens
naman, vice versa nya lang yung proenzymes. So
ayon kapag natangal na yung excess polypeptide
chain, magiging active na yung enzyme.
For example, trypsin is manufactured sa pancreas
as inactive molecule trypsinogen, which is a
zymogen.
Kapag natangal na yung part na may 6-amino acid
residues sa N-terminal end, magiging fully active na
yung trypsin molecule. So kapag tinangal yung
fragment na yon, iiksi yung chain then magbabago
yung 3-dimensional structure or tertiary structure
ng chain, which is the reason paano nagiging active
form yung molecule.
Why does the body go through so much trouble?
Why not just make the fully active trypsin to begin
with?
Trypsin is a protease— pinapabilis nito yung
hydrolysis ng peptide bonds, so mahalagang
catalayst sya for the digestion ng proteins na
kinakain natin. Pero hindi naman okay na hatiin or
idivide ng trypsin yung proteins na gawa mismo ng
body natin. Kaya ginagawang inactive ng pancreas
yung trypsin. Magiging active lang yung trypsin sa
pancreas kapag nakapasok na sa digestive tract.
3. Allosterism
Minsan may mga regulations that takes place by
means of an event na nagngyari sa isang site bukod
sa active site, pero eventually maapektuhan rin non
yung active site. This type of interaction is called
allosterism, at yung mga enzyme na rineregulate ng
mechanism na to is called allosteric enzyme.
This is an enzyme kung saan yung binding ng
regulator sa isang site sa enzyme ay binabago yung
ability ng enzyme to bind the substrate sa active
site. Kung ang isang substance ay nagbond sa non-
covalently and reversibly sa isang site other that the
active site, maapektuhan non yung enzyme.
Pwedeng mainhibit nito yung enzyme action, which
is the negative modulation or pwede rin naming
mastimulate yung enzyme action or tinatawag na
positive modulation.
Yung substance na nagbi-bind sa allosteric enzyme
is called a regulator, tas yung site kung saan sya
nagbibind is called a regulatory site. In most cases,
allosteric enzymes contain more than one
polypeptide chain, the regulatory site is on one
polypeptide chain, and the active site is on another.
4. Protein Modification
Pwedeng macontrol ng protein modification yung
activity ng enzyme. Madalas yung modification is a
change sa primary structure, madalas by addition
ng functional group covalently bound to the
apoenzyme. Isa sa mga best example ng protein
modification is the activation or inhibition ng
enzymes by phosphorylation, which is a
biochemical process that involves the addition of
phosphate to an organic compound. So yung
phospohate group ay madalas nagbobond sa serine
or tyrosine residue. Kung walang phosphorylation,
magiging inactive or less active yung enzyme.
5. Isoenzymes
Pwede ring magkaroon ng regulation of enzyme
activity kapag yung parehong enzyme appears in
different forms sa magkaibang tissues. Example is
yung alkaline phosphatases of humans which have
at least three different genetic origins, like for
placental, intestinal, and liver/bone/kidney
enzymes. They are in different forms pero parehong
enzyme, and they are called isozymes or
isoenzymes. These are enzymes that perform the
same function pero meron silang magkakaibang
combination ng subunits, so magkakaiba yung
quaternary structures nila.
How Are Enzymes Used in Medicine?
The enzymes can efficiently catalyze various
biochemical reactions and promote the metabolism
of organisms under conditions in the normal body.
That’s why ginagamit din ang enzymes sa medicine
at pagproduce ng medications. For example, during
myocardial infarction, mineameasure yung number
of enzymes para madiagnose kung gaano kalala
yung heart attack. Minsan naman, part ng mga
post-operation routine yung pagadminister ng
enzyme in the form of tablet or capsule. Kunwari
pagkatpos ng duodenal or stomach ulcer
operations, patients are advised to take tablets
containing digestive enzymes kasi konti nalang or
wala na at all natira sa stomach nila after their
surgery
What Are Transition-State Analogs and
Designer Enzymes?
So we all know na binabaan ng enzyme yung
activation energy for a reaction, and this makes the
transition state more favorable. Nangyayari yon by
having an active site na sobrang fit sa transition
state conformation kaysa sa substrates or the
products. This is documented by using the
transition state analogs, molecules na with same
shape sa transition state ng substrate at ginagamit
din as enzyme inhibitors.
Abzymes
Immunoglobulins generated by using transition-
state analogs as antigens. So ito ay isang uri ng
antibody molecule na isinama sa enzyme to carry
out catalysis of some substrate. Recently, triny
gamitin yung Abzymes to fight against AIDS. Ang
plano is to produce a catalytic antibody that will
cleave the gp120 protein, which is part ng HIV virus
coat. The gp120 protein is responsible for the
binding of HIV to target cells.

Lysosomal storage disorders are a group of

approximately fifty inherited disorders na
nangyayari kapag may nawawalang enzyme that
that results sa inability ng katawan natin to recycle
the waste ng cells. Madalas na nagkakaroon ng LSD
is mga baby. Kadalasan yung mga taong may LSD
ay may intellectual and developmental disabilities,
blurry vision, bone problems, speech and hearing
impairment, hernia, heart disease, hyperactivity,
depression, pain and shortened life span.

 When alpha- amino acid are commonly written

in the un-ionized form, they are more properly
written in the Zwitterion form
 The specificity of enzymes also extends to
Stereopecificity
 Substrate specificity is when the limitation of
an enzyme to catalyze specific results with
specific substrate.
 Antidiuretic hormone = Vasopressin
 Fatty acids cannot denature proteins
 Peptide is a short polymer of amino acids
joined by peptide bond
 Tripeptide is a molecule containing three
amino acids joined by peptide bond
 Enzymes are extremely specific
 Ribozymes are enzymes that made up of
ribonucleic acid.
 Activation is the process that initiates or
increases the action of an enzyme.
 Carboxylpeptidase is an enzyme that
specifically catalyzes the hydrolysis only the
last amino acid on a protein chain.
 Organic cofactor are called Coenzymes
 The protein portion of the enzyme is called
Apoenzyme
 5 amino acids participate in the active sites
 C-terminal amino acid is the amino acid at the
end of the chain having the free -COO group
 N-terminal amino acid is the amino acid at the
end of the chain having the free -NH3 group.
 Substrate is the compound on which the
enzymes work on.
 Disulfide bonds connect the two-polypeptide
chain of human insulin?
 Hydrogen bond stabilizes tertiary structures
between polar groups on side chains of -C=O
groups and -N-H groups.
 Metal Ion coordination linked two side chains
with the same charge.