STRUCTURE ENZYMES MECHANISM AFFECTING FACTORS

ENZYME STRUCTURE

Cofactor Apoenzyme/ apoprotein Prostetic Group Coenzyme Holoenzyme

Cofactor: komponen non protein untuk membantu aktivitas enzim (beberapa berupa ion anorganik) Kofaktor berupa ion organik disebut coenzym Apoenzyme or apoprotein: Enzim yg memerlukan kofaktor tetapi tidak memilikinya.(Enzim tanpa kofaktor) Hanya tersusun dari protein,Ex. Pepsin Simple enzym.

PROSTETIC GROUP
Molekul non-protein yg diikat enzim untuk melakukan fungsinya. ex,. katalase

Prostetics Group
COFACTORS

COENZYMES

Such as the metal ions Mg2+, Cu+, Mn2+ or iron-sulfur clusters Inorganic

Senyawa organik Contoh: NADH Dilepaskan dari sisi aktif saat bereaksi

Space-filling model of the coenzyme NADH

Coenzymes are small organic molecules that transport chemical groups from one enzyme to another

Holoenzyme
Apoenzim yang dilengkapi kofaktornya

Merupakan enzim dalam keadaan aktif.

The active site Is the region on the enzyme where the substrate binds
Substate

Active site

Enzyme

Figure 8.16

(a)

Karakteristik sisi aktif enzim

Merupakan bagian kecil dari enzim Sisi aktif merupakan suatu cekukan yang bersifat 3 dimensi. memberikan lingkungan mikro yg sesuai untuk terjadinya suatu reaksi kimia substrat terikat pada sisi aktif dengan interaksi / ikatan yang lemah. Spesifitas enzim dipengaruhi oleh asam amino yg menyusun sisi aktif suatu enzim

TEORI CARA KERJA ENZIM

Lock and Key theory

Induced Fit theory

Induced fit of a substrate

Brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction

Enzyme- substrate complex Figure 8.16 (b)

Induced Fit theory

Sisi aktif mengubah konformasi (bentuknya) agar cocok dengan bentuk substratnya. Mempertimbangkan fleksibilitas protein

Induced Fit Theory

"the Lock and Key" Model

Both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one and other.(Bentuk sisi aktif enzim pas dg bentuk substrat.)

The catalytic cycle of an enzyme

2 Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. 3 Active site (and R groups of its amino acids) can lower EA and speed up a reaction by acting as a template for substrate orientation, stressing the substrates and stabilizing the transition state, providing a favorable microenvironment, participating directly in the catalytic reaction.

1 Substrates enter active site; enzyme changes shape so its active site embraces the substrates (induced fit).

Substrates

Enzyme-substrate complex

6 Active site Is available for two new substrate Mole. Enzyme

Products are Released. Products

Figure 8.17

4 Substrates are Converted into Products.

Faktor-Faktor yg mempengaruhi kerja Enzim (riyandhanu,haris,rahnata)

Konsentrasi Enzim Konsentrasi Substrat Suhu pH Konsentrasi air Inhibitor Aktivator

Konsentrasi Enzim

Kecepatan reaksi dipengaruhi oleh konsentrasi enzim, makin besar konsentrasi enzim makin tinggi pula kecepatan reaksi Konsentrasi enzim berbanding lurus dengan kecepatan reaksi

Concentration of Enzyme

Concentration of Substrate

Peningkatan konsentransi substrat dapat meningkatkan kecepatan reaksi bila jumlah enzim tetap. Namun pada saat sisi aktif semua enzim berikatan dengan substrat, penambahan substrat tidak dapat meningkatkan kecepatan reaksi enzim selanjutnya.

Concentration of Substrate

Effects of Temperature and pH

Each enzyme
Has an optimal temperature in which it can function
Optimal temperature for typical human enzyme Rate of reaction Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria

80 40 Temperature (C) (a) Optimal temperature for two enzymes 0 20

100

Figure 8.18

Pengaruh Suhu pada aktivitas Enzim

Umumnya, Enzim akan terdenaturasi pada suhu yang terlalu tinggi. Pada suhu yg terlalu rendah enzim umumnya akan menjadi inaktif tetapi dapat kembali aktif apabila suhu normal kembali.

 Has an optimal pH in which it can function

Optimal pH for pepsin (stomach enzyme) Rate of reaction

Optimal pH for trypsin (intestinal enzyme)

5 3 4 0 2 1 (b) Optimal pH for two enzymes

Figure 8.18

Gerry, aryo, hafiz: ATP (pengertian,struktur, fungsi dalam metabolisme) Adi,azhar,rafif: metabolic reaction (hydrolysis,condensation,) Rilo,tegar,novrian: OxidasiReduction Ihsan,pinayungan,vlady: Transphosphorylation Bagus,thareq,raka : Coenzym Nadzir,ghazali,iqbal: other metabolic reaction (salah satunya:

Azka dewa, dhito,kharist: ATP (pengertian,struktur, fungsi dalam metabolisme) Insan, reynaldy,roni: metabolic reaction (hydrolysis,condensation,) Refta, barkah, alfin: metabolic reaction (Oxidasi-Reduction) Ivan, frans,Faiz: metabolic reaction (Transphosphorylation) Novan,Alan, Reyshaldy: Coenzym Parama, Shiosi, Azka Hanif: other metabolic reaction (salah satunya:

Enzyme Inhibitors Competitive inhibitors

Bind to the active site of an enzyme, competing with the substrate

Substrate Active site

A substrate can bind normally to the active site of an enzyme.

Enzyme

(a) Normal binding A competitive inhibitor mimics the substrate, competing for the active site.

Competitive inhibitor

Figure 8.19

(b) Competitive inhibition

INHIBITOR KOMPETITIF
Molekul penghambat yang strukturnya mirip substrat, sehingga molekul tersebut berkompetisi dengan substrat untuk bergabung pada sisi aktif enzim.

Contoh : sianida bersaing dengan oksigen untuk mendapatkan Hemoglobin pada rantai akhir respirasi.
Inhibitor kompetititf dapat diatasi dengan penambahan konsentrasi substrat.

Noncompetitive inhibitors
Bind to another part of an enzyme, changing the function

A noncompetitive inhibitor binds to the enzyme away from the active site, altering the conformation of the enzyme so that its active site no longer functions. Noncompetitive inhibitor

Figure 8.19 (c) Noncompetitive inhibition

INHIBITOR NON KOMPETITIF

Molekul penghambat yang bekerja dengan cara melekatkan diri pada bagian bukan sisi aktif enzim. Inhibitor ini menyebabkan sisi aktif berubah sehingga tidak dapat berikatan dengan substrat. Inhibitor nonkompetitif tidak dapat dipengaruhi oleh konsentrasi substrat.

Aktivator Enzim
Molekul atau ion yang meningkatkan aktifitas enzim. Yaitu: Kofaktor atau koenzim

ENRICHMENT (PENGAYAAN)

Regulation of enzyme activity helps control metabolism A cells metabolic pathways

Must be tightly regulated

Allosteric Regulation of Enzymes

Allosteric regulation
Is the term used to describe any case in which a proteins function at one site is affected by binding of a regulatory molecule at another site. (Fungsi protein pada suatu situs yang dipengaruhi oleh molekul yang terikat pada situs lain)

Allosteric Activation and Inhibition

Many enzymes are allosterically regulated

 They change shape when regulatory molecules bind to specific sites, affecting function
Allosteric activater Allosteric enyzme Active site stabilizes active from with four subunits(one of four)

Regulatory site (one of four)

Activator Active form Stabilized active form

Allosteric activater stabilizes active form

Oscillation

Figure 8.20

NonInhibitor Stabilized inactive Inactive form functional form active site (a) Allosteric activators and inhibitors. In the cell, activators and inhibitors dissociate when at low concentrations. The enzyme can then oscillate again.

Cooperativity
Is a form of allosteric regulation that can amplify enzyme activity (menguatkan aktivitas enzim)
Binding of one substrate molecule to active site of one subunit locks all subunits in active conformation.

Substrate

Inactive form

Stabilized active form

(b) Cooperativity: another type of allosteric activation. Note that the inactive form shown on the left oscillates back and forth with the active form when the active form is not stabilized by substrate. Figure 8.20

Feedback Inhibition

In feedback inhibition
The end product of a metabolic pathway shuts down the pathway

Feedback inhibition
Active site available Initial substrate (threonine) Threonine in active site Enzyme 1 (threonine deaminase) Intermediate A Feedback inhibition Active site of Enzyme 2 enzyme 1 no longer binds threonine; Intermediate B pathway is Enzyme 3 switched off

Isoleucine used up by cell

Intermediate C
Isoleucine binds to allosteric site Enzyme 4

Intermediate D
Enzyme 5

Figure 8.21

End product (isoleucine)

Thanks for your attention