Enzyme: Oleh Yana Cahyana Stp.,Dea.,Ph.D

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ENZYME

OLEH
YANA CAHYANA STP.,DEA.,Ph.D
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Outline
- Introduction
- Catalytic power, specificity, &
regulation
- Kinetics of enzyme-catalysed
reaction
- Enzyme inhibition
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Introduction
Enzymes are fundamental to biochemistry, the food
sciences and biotechnology

Much of biotechnology is concerned either with


producing or using enzymes

Applications are in a wide range of sectors particularly the food industry

Any practising biotechnologist, biochemist or food


scientist will work with enzymes at some point
Knowledge of the fundamentals of enzymology is
important
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Nama :

Introduction

-ase : invertase, triosa fosfat dehidrogenase


-in : pepsin, chymotrypsin

Lisozim?

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Introduction

Karakteristik enzim
-Katalisator reaksi
-Mengubah substrat jadi produk
-Protein
-Bekerja spesifik
-Berat molekul (BM) enzim>>>> (BM) substrat
-Mempunyai gugus dan ruang aktif
-Mempunyai bagian non protein
-Kompleks E-S merubah bentuk ruang aktif dan substrat

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Introduction
Enzim bekerja dengan menurunkan energi aktifasi

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Catalytic power, specificity, &


regulation
- Accelerating reaction rate as much as 1016 over
uncatalysed levels
ex urease catalyses the hydrolysis of urea :

Catalysed reaction : 3 x104/sec


Uncatalysed one : 3 x 10-10/sec
Catalytic power of urease =1014

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Catalytic power, specificity, &


regulation
-Molecular
recognition
based
on
structural
complementarity
-Specific site on the enzyme where substrate binds and
catalysis occurrs is called the active site
-Some enzymes rely solely on their amino acid residues,
others require cofactor either metal ions (Fe2+,Fe3+, Mg2+,
Cu2+, Mg2+, Se) or organic molecules (coenzyme, ex:
vitamin).

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Enzyme Kinetics
-Pengaruh suhu pada aktifitas enzim

-Pengaruh pH pada aktifitas enzim

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Enzyme Kinetics
-Pengaruh konsentrasi enzim

-Pengaruh konsentrasi substrat

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Enzyme Kinetics
-Michaelis-Menten Equation

v= kecepatan reaksi enzimatis, Vmax=kecepatan maksimum


Kmax=konstanta Michaelis-Menten, [S]=konsentrasi substrat
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Enzyme Kinetics
Konstanta Michaelis-Menten (Km)
-Salah satu ciri enzim
-Menggambarkan afinitas enzim terhadap substrat
Km

afinitas

-Km <10-6M sangat penting dalam metabolisme,


Km >10-2M dianggap kurang penting
-Kerja penghambatan enzim

Nilai Km
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Konstanta Michaelis-Menten (Km)

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Enzyme Kinetics
Transformation of Michaelis-Menten equation :
Lineweaver-burk double reciprocal plot

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Enzyme Unite
-Aktifitas enzim= banyaknya substrat yang dirubah menjadi produk
oleh sejumlah enzim
-Aktifitas enzim dinyatakan dalam unit (U)
1 unit= jumlah enzim yg dapat mengkatalisis 1 mol substrat per
menit pada kondisi tertentu
Specific activity =

Enzyme activity (U)


Amount of protein present (mg)

Cellulase
-Amylase
Polygalacturonase
Glucoamylase
-1,3-Glucanase
Protease

1000 U/g
200 U/g
280 U/g
570 U/g
1970 U/g
2000 U/g
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Enzyme Inhibition
Many compounds can inhibit enzymes
Highly reactive chemicals can form covalent
bonds with reactive groups on the enzyme and
irreversibly inhibit the enzyme
Other molecules interact with the enzyme in
reversible ways to produce inhibition

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Enzyme Inhibition

Reversible
(Ikatan non kovalen)

Irreversible
(Ikatan kovalen)

-Kompetitif
-Non kompetitif
- Kombinasi

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Enzyme Inhibition
Penghambatan Kompetitif
-Inhibitor bersaing dengan substrat
memperebutkan ruang aktif yang
sama

Contoh:
Pemberian etanol bagi yang keracunan
metanol

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Enzyme Inhibition
Penghambatan Non-Kompetitif
inhibitors bind to the enzyme-substrate complex and block the catalytic step

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Enzyme Inhibition
Penghambatan Kombinasi (Campuran)

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Enzyme Inhibition
Penghambatan Irreversible
Penicilin menghambat glycoprotein peptidase
dalam croslinking peptidoglikan untuk sintesa
dinding sel

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