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    Enzim

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    ribi
    This document provides an overview of enzymes, including their catalytic power and specificity, kinetics of enzyme-catalyzed reactions, and inhibition. It discusses how enzymes accelerate reactions by lowering activation energy. Enzymes have high specificity due to complementary binding with substrates. Kinetics are influenced by temperature, pH, enzyme and substrate concentration. The Michaelis-Menten equation describes reaction kinetics, and constants like Km indicate enzyme-substrate affinity. Enzymes can be inhibited reversibly or irreversibly through competitive, non-competitive, or mixed inhibition.

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    Enzim

    Uploaded by

    ribi
    73 views21 pages
    This document provides an overview of enzymes, including their catalytic power and specificity, kinetics of enzyme-catalyzed reactions, and inhibition. It discusses how enzymes accelerate reactions by lowering activation energy. Enzymes have high specificity due to complementary binding with substrates. Kinetics are influenced by temperature, pH, enzyme and substrate concentration. The Michaelis-Menten equation describes reaction kinetics, and constants like Km indicate enzyme-substrate affinity. Enzymes can be inhibited reversibly or irreversibly through competitive, non-competitive, or mixed inhibition.

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    This document provides an overview of enzymes, including their catalytic power and specificity, kinetics of enzyme-catalyzed reactions, and inhibition. It discusses how enzymes accelerate reactions by lowering activation energy. Enzymes have high specificity due to complementary binding with substrates. Kinetics are influenced by temperature, pH, enzyme and substrate concentration. The Michaelis-Menten equation describes reaction kinetics, and constants like Km indicate enzyme-substrate affinity. Enzymes can be inhibited reversibly or irreversibly through competitive, non-competitive, or mixed inhibition.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    73 views21 pages

    Enzim

    Uploaded by

    ribi
    This document provides an overview of enzymes, including their catalytic power and specificity, kinetics of enzyme-catalyzed reactions, and inhibition. It discusses how enzymes accelerate reactions by lowering activation energy. Enzymes have high specificity due to complementary binding with substrates. Kinetics are influenced by temperature, pH, enzyme and substrate concentration. The Michaelis-Menten equation describes reaction kinetics, and constants like Km indicate enzyme-substrate affinity. Enzymes can be inhibited reversibly or irreversibly through competitive, non-competitive, or mixed inhibition.

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    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    of 21

    ENZYME

    OLEH

    YANA CAHYANA STP.,DEA.,Ph.D


    Kuliah biokim TIP
    Outline
    - Introduction
    - Catalytic power, specificity, &
    regulation
    - Kinetics of enzyme-catalysed
    reaction
    - Enzyme inhibition

    Kuliah biokim TIP


    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

    Kuliah biokim TIP


    Introduction
    Nama :
    -ase : invertase, triosa fosfat dehidrogenase
    -in : pepsin, chymotrypsin
    Lisozim?

    Kuliah biokim TIP


    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

    Kuliah biokim TIP


    Introduction
    Enzim bekerja dengan menurunkan energi aktifasi

    Kuliah biokim TIP


    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

    Kuliah biokim TIP


    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).

    Kuliah biokim TIP


    Enzyme Kinetics
    -Pengaruh suhu pada aktifitas enzim

    -Pengaruh pH pada aktifitas enzim

    Kuliah biokim TIP


    Enzyme Kinetics
    -Pengaruh konsentrasi enzim

    -Pengaruh konsentrasi substrat

    Kuliah biokim TIP


    Enzyme Kinetics
    -Michaelis-Menten Equation

    v= kecepatan reaksi enzimatis, Vmax=kecepatan maksimum


    Kmax=konstanta Michaelis-Menten, [S]=konsentrasi substrat

    Kuliah biokim TIP


    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

    Kuliah biokim TIP


    Konstanta Michaelis-Menten (Km)

    Kuliah biokim TIP


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

    Kuliah biokim TIP


    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
    Enzyme activity (U)
    Specific activity = Amount of protein present (mg)

    Cellulase 1000 U/g


    -Amylase 200 U/g
    Polygalacturonase 280 U/g
    Glucoamylase 570 U/g
    -1,3-Glucanase 1970 U/g
    Protease 2000 U/g
    Kuliah biokim TIP
    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

    Kuliah biokim TIP


    Enzyme Inhibition

    Reversible Irreversible
    (Ikatan non kovalen) (Ikatan kovalen)

    -Kompetitif
    -Non kompetitif
    - Kombinasi

    Kuliah biokim TIP


    Enzyme Inhibition
    Penghambatan Kompetitif

    -Inhibitor bersaing dengan substrat


    memperebutkan ruang aktif yang
    sama

    Contoh:
    Pemberian etanol bagi yang keracunan
    metanol

    Kuliah biokim TIP


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

    Kuliah biokim TIP


    Enzyme Inhibition
    Penghambatan Kombinasi (Campuran)

    Kuliah biokim TIP


    Enzyme Inhibition
    Penghambatan Irreversible

    Penicilin menghambat glycoprotein peptidase


    dalam croslinking peptidoglikan untuk sintesa
    dinding sel

    Kuliah biokim TIP

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