ENZIM

By
Mariany Razali
 Session Plan
• General Characteristics of Enzymes
• Enzyme Structure
• Enzyme Nomenclature
• Enzyme Function
• Enzyme Specificity
• Factors Affecting Enzyme Activity
• Enzyme Inhibition
• Regulation of Enzyme Activity
• Medical Uses of Enzymes
 Sifat-sifat enzim
• Hampir semua enzim adalah protein
• Enzim : suatu senyawa yang berstruktur protein baik murni
maupun protein yang terikat pada gugus non protein
 Enzymes denaturation due to pH or temperature change
• Bekerja spesifik
 Masing-masing sel pada tubuh manusia terdapat 1000 enzim yang berbeda
 Every reaction in the cell requires its own specific enzyme
• Larut dalam air
• Enzim sensitif dan labil terhadap panas
• Fungsi : katalis
• Enzim dapat dipresipitasi oleh ammonium sulfate and trichloroacetic
acid.
 Struktur Enzim
 Berdasarkan strukturnya, enzim terdiri atas komponen yang disebut apoenzim yang
berupa protein dan gugus protetik berupa non protein. Gugus prostetik dibedakan
menjadi koenzim dan kofaktor
 Simple enzim
- Tersusun hanya dari protein
 Enzim terkonjugasi
Terdiri dari :
– Apoenzyme
• Conjugate enzyme without its cofactor
• Protein part of a conjugated enzyme
• Termolabil
– Koenzim (Cofactor)
• Non-protein part of a conjugated enzyme
• Termostabil
• Apoenzym tidak dapat mengkatalis reaksi tanpa kofaktor.
– kombinasi apoenzym dengan kofaktor membuat enzim terkonjugasi berfungsi.
• Holoenzyme = apoenzyme + cofactor
– The biochemically active conjugated enzyme.
Berdasarkan strukturnya, enzim terdiri atas komponen yang disebut apoenzim
yang berupa protein dan gugus protetik berupa non protein. Gugus prostetik
dibedakan menjadi koenzim dan kofaktor
 Komponen penyusun enzim terdiri dari :
1. Apoenzim, bagian enzim aktif yang tersusun atas protein yang bersifat
termolabil (mudah berubah) terhadap faktor lingkungan
2. Kofaktor,yaitu komponen non protein yang berupa :
a. Ion-ion anorganik (aktivator).
Berupa logam yang berikatan lemah dengan enzim, Contoh ion logam (Zn2+,
Mg2+, Mn2+ , Ca 2+ & Fe2+). Ion klorida, ion kalsium merupakan ion anorganik
yang membantu enzim amilase mencerna karbohidrat (amilum)
b. Gugus prostetik
Senyawa organik yang berikatan kuat dengan enzim, FAD (Flavin Adenin
Dinucleotide), biotin, dan heme merupakan gugus prostetik yang mengandung
zat besi berperan memberi kekuatan ekstra pada enzim terutama katalase,
peroksidase, sitokrom oksidase.
c. Koenzim molekul organik non protein kompleks, ex: NAD (Nicotineamide
Adenine Dinucleotide), koenzim-A, ATP, dan vitamin yang berperan dalam
memindahkan gugus kimia, atom, atau elektron dari satu enzim ke enzim lain..
• Tidak semua enzim memiliki struktur yang lengkap terdiri dari apoenzim dan kofaktor.
Contoh enzim ribonuklease pankreas hanya terdiri atas polipeptida dan tidak mengandung
gugus kimiawi yang lain.
 Defenisi Enzim
Term Defenisi
Enzim (simpel) Protein only enzyme that facilitates a chemical reaction
Koenzim Compound derived from a vitamin (e.g. NAD+ ) that
assists an enzyme in facilitating a chemical reaction
Kofaktor Metal ion (e.g. Mg2+) that that assists an enzyme in
facilitating a chemical reaction
Apoenzim Protein only part of an enzyme (e.g. isocitrate
dehydrogenase) that requires an additional coenzyme to
facilitate a chemical reaction (not functional alone)
Haloenzim Combination of the apoenzyme and coenzyme which
together facilitating a chemical reaction (functional)
 Nomenklatur Enzim
Enzyme dinamakan menurut tipe reaksi yang
dikatalisis dan/atau substrat.
• Substrate = the reactant upon which the specific
enzyme acts (Enzim berikatan dengan substrate)
 Akhiran enzim –ase
– Lactase, amylase, lipase or protease
 Beberapa enzim pencernaan berakhiran –in
– Pepsin, trypsin & chymotrypsin
Berawalan dari tipe reaksi enzim yang katalisis
– Oxidase : redox reaction
– Hydrolase : Addition of water to break one component
into two parts
Identitas substrat sering digunakan bersamaan
dengan tipe reaksi.
– Pyruvate carboxylase, lactate dehydrogenase
 6 kelas utama enzim berdasarkan tipe reaksi yang dikatalisis
Oxidoreductase Redox reaction (reduction Examples are dehydrogenases catalyse
& oxidation) reactions in which a substrate is oxidised or
reduced

Transferase Transfer of a functional Transaminases which catalyze the transfer of

group from 1 molecule to amino group or kinases which catalyze the
another transfer of phosphate groups
Hydrolase Hydrolysis reaction Lipases catalyze the hydrolysis of lipids, and
proteases catalyze the hydrolysis of proteins
Lyase Addition / removal of atoms Decarboxylases catalyze the removal of
to / from double bond carboxyl groups
Isomerase Isomerization reaction Isomerases may catalyze the conversion of an
aldose to a ketose, and mutases transfer
functional group from one atom to another
within a substrate
Ligase Synthesis reaction (Joining Synthetases link two smaller molecules are
of 2 molecules into one, form a larger one
forming a new chemical
bond, coupled with ATP
hydrolysis)
 Enzyme – Substrate Complex
• Substrat berikatan dengan sisi aktif enzim
Enzyme-Substrate Complex dibentuk sementara
– Allows the substrate to undergo its chemical reaction much faster
 Model of Enzyme Action
1) Model kunci – dan anak kunci
Diusulkan oleh Emil Fisher pada tahun 1894, yang menyatakan bahwa bentuk molekul
substrat dengan sisi aktif enzim serupa dengan anak kunci dengan kuncinya.
The active site is fixed, with a rigid shape (LOCK)

• The substrate (KEY) must fit exactly into the rigid enzyme (LOCK)

• Complementary shape & geometry between enzyme and substrate

– Key (substrate) fits into the lock (enzyme)

• Upon completion of the chemical reaction, the products are released from the active site,
so the next substrate molecule can bind
2. Induced Fit Model

• Induced-fit model diusulkan pada tahun 1958 oleh Daniel E.

Koshland, Jr. yang menyatakan bahwa terikatnya substrat
menyebabkan perubahan konformasi pada bagian sisi aktif enzim.
(Many enzymes are flexible & constantly change their shape
– Perubahan sisi aktif untuk menerima dan menampung substrate
• Conformation change in the enzyme‟s active site to allow the substrate to bind

• Analogy: a glove (enzyme) changes shape when a hand (substrate) is inserted into it
 Sisi aktif enzim (Active Site)
• Sisi aktif enzim (active site) adalah bagian dari molekul enzim tempat
berikatannya substrat, untuk membentuk kompleks enzim substrat, dan
selanjutnya membentuk produk akhir.
• Sisi aktif suatu enzim berbentuk 3 dimensi „crevice-like‟, berupa lekukan
pada permukaan protein enzim, yang dibentuk dari struktur sekunder
dan tersier bagian protein enzim.
• Tempat substrat berikatan secara lemah (misalnya interaksi elektrostatik,
ikatan hidrogen, ikatan van der Waals, dan interaksi hidrofobik)
• Sebuah enzim dapat memiliki lebih dari satu active site
• Rantai samping asam amino dalam active site penting dl menentukan
spesifitas substrat
 Spesifisitas Enzim
• Absolute Specificity
– An enzyme will catalyze a particular reaction for only one substrate
– Most restrictive of all specificities
• Not common

– Catalase has absolute specificity for hydrogen peroxide (H2O2)

– Urease catalyzes only the hydrolysis of urea

• Group Specificity
– The enzyme will act only on similar substrates that have a specific
functional group

• Carboxypeptidase cleaves amino acids one at a time from the

carboxyl end of the peptide chain

• Hexokinase adds a phosphate group to hexoses

 Spesifisitas Enzim
• Linkage Specificity
– The enzyme will act on a particular type of chemical bond.
– The most general of the enzyme specificities

• Phosphatases hydrolyze phosphate–ester bonds in all types of phosphate esters

• Chymotrypsin catalyzes the hydrolysis of peptide bonds

• Stereochemical Specificity
– Enzim dapat membedakan diantara stereoisomers
– Chirality is inherent in an active site (as amino acids are chiral compounds)

• L-Amino-acid oxidase catalyzes reactions of L-amino acids but not of D-amino

acids
 Faktor-faktor Yang Mempengaruhi Kerja Enzim

4 faktor yang mempengaruhi aktivitas enzim:

1. Temperature
2. pH
3. Konsentrasi Substrat: [substrate]
4. Konsentrasi Enzim: [enzyme]
5. Inhibitor
 1. Temperature (t)

• Meningkatnya t , maka EKIN m e n i n g k a t .

• Setiap kenaikan suhu 10o C, kecepatan enzim
akan menjadi dua kali lipat, sampai batas suhu
tertentu.
– Increased reaction rate
– More collisions

• Optimum temperature (tOPT) , enzim

menunjukkan aktvitas maximum
• The tOPT for human enzymes = 370C

• Ketika t meningkat diatas tOPT

– Changes in the enzyme‟s tertiary structure
occur, inactivating & denaturing it (e.g.
fever)

• Little activity is observed at low t

 2. pH
• Optimum pH (pHOPT) , pH enzim
menunjukkan aktivitas maximum

• Semua enzim peka terhadap perubahan pH

– Perubahan pH (low or high) dapat
menyebabkan enzim denaturation &
loss of function

• Setiap enzim memiliki karakteristik

pHOPT which usually falls within
physiological pH range 7.0 - 7.5
• Digestive enzymes are exceptions:
– Pepsin (in stomach) – pHOPT = 2.0

– Trypsin (in SI) – pHOPT = 8.0

 3. Substrate Concentration
• Jika enzim konstan & substrate meningkat
– Kecepatan reaksi
meningkat hingga
bertemu saturation point
• At saturation the reaction rate stays the same
even if
the [substrate] is increased

– At saturation point substrate molecules are

bound to all available active sites of the enzyme
molecules

• Reaction takes place at the active site

– If they are all active sites are occupied the
reaction is going at its maximum rate
• Each enzyme molecule is working at its
maximum
capacity

– The incoming substrate molecules must “wait

their turn”
 4. Enzyme Concentration
• Jika substrat konstan dan enzim
meningkat maka kecepatan reaksi akan
meningkat
– The greater the [enzyme], the greater
the reaction rate

• RULE:
– The rate of an enzyme-catalyzed
reaction is always directly proportional
to the amount of the enzyme present

• In a living cell:
– The [substrate] is much higher
than the [enzyme]
• Enzymes are not consumed in the
reaction

• Enzymes can be reused many times