slide1 n.
Skip this Video
Loading SlideShow in 5 Seconds..
Struktur Enzim PowerPoint Presentation
Download Presentation
Struktur Enzim

Loading in 2 Seconds...

play fullscreen
1 / 44

Struktur Enzim - PowerPoint PPT Presentation

  • Uploaded on

Cakupan Isi Tugas Kelompok 1. Enzyme : Introduction a. Fungsional properties b. Enzyme Nomenclatur c. Enzyme Specificity d. Enzyme Regulation e. Activation Energy. Struktur Enzim. Apoenzyme + Coenzyme = Holoenzyme

I am the owner, or an agent authorized to act on behalf of the owner, of the copyrighted work described.
Download Presentation

PowerPoint Slideshow about 'Struktur Enzim' - snana

Download Now An Image/Link below is provided (as is) to download presentation

Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author.While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server.

- - - - - - - - - - - - - - - - - - - - - - - - - - E N D - - - - - - - - - - - - - - - - - - - - - - - - - -
Presentation Transcript

Cakupan Isi Tugas Kelompok 1. Enzyme : Introduction a. Fungsional properties b. Enzyme Nomenclatur c. Enzyme Specificity d. Enzyme Regulation e. Activation Energy

struktur enzim
Struktur Enzim

Apoenzyme + Coenzyme = Holoenzyme

Bagian protein Grup prostetik Enzim lengkap

(tidak aktif) (tidak aktif) (aktif)


the protein part of the enzyme molecule

    • Struktur protein enzimsangatkompleksdanberfungsimenyediakanlingkunganuntukkelangsunganreaksidenganmekanismetertentu
    • Fungsi lain adalahsebagaitempat patron (template) substrat, dankarenanya protein enzimberfungsimengenalsubstrat yang dipertimbangkanmenjadidasarspesifitasenzim
  • Cofactor

the additional chemical groups appearing in those enzymes that are conjugated proteins.


These cofactors are required for enzyme activity and may consist of metal ions or complex organic molecules. Some enzymes require both types of cofactors.

Cofactors ( bukan protein) can be divided into three groups

a. ygterikatkuat pd

protein - Prosthetic group

-b. ygmudahdipisahkan)

- coenzyme ( berupabhnorganik)

- Metal Activators

Prosthetic group
    • In the enzyme molecule, the cofactor may be weakly attached to the apoenzyme, or it may be tightly bound to the protein. If it is tightly bound, the cofactor is called a prosthetic group
    • Example: bagian porphyrin (moiety) dari hemoprotein peroxidase dan flavin-adenine dinucleotide dalam succinic dehydrogenase
  • Coenzyme
    • When the cofactor of an enzyme is a complex organic molecule other than a protein, the cofactor is called a coenzyme
    • Example: NAD+, NADP+, tetrahydrofolic acid dan thyamin pyrophosphate
    • When the cofactor of an enzyme is a metal ion, such as the ions of magnesium, zinc, ion or manganese), the cofactor is called an activator
    • Examples: K+, Mn+2, Mg+2, Ca+2dan Zn+2
  • Isoenzyme
    • Enzymes that perform the same catalytic function in different body tissues or different organisms, but which have different sequences of amino acids in various portions of their polypeptide chain are called isoenzymes. Isoenzymes can be separated from one another by electrophoresis.

Enzyme classes .

A system of classification has

been developed that takes into account both

their reaction specificity and their substrate

specificity. Each enzyme is entered in the Enzyme

Catalogue with a four-digit Enzyme

Commission number (EC number). The first

digit indicates membership of one of the six

major classes. The next two indicate subclasses

and subsubclasses. The last digit indicates

where the enzyme belongs in the subsubclass.



Enzymes with similar reaction specificities

are grouped into each of the sixmajor classes

1. The oxidoreductases (class 1) catalyze the

transfer of reducing equivalents from one redox

system to another.

2.The transferases (class 2) catalyze the transfer of other groups from one molecul to another.

. Oxidoreductases and transferases generally require coenzymes (see pp.104ff.).

3. The hydrolases (class 3) are also involved in group transfer, but the acceptor is always water molecule.


4. Lyases (class 4, often also referred to as“synthases”) catalyze reactions involving eitherthe cleavage or formation of chemical bonds, with double bonds either arising of disappearing.

5. The isomerases (class 5) move groups within a molecule, without changing the gross composition of the substrate.

6. The ligation reactions catalyzed by ligases (“synthetases,” class 6) are energy-dependent and are therefore always coupled to the hydrolysis of nucleoside triphosphates.


For example, lactate dehydrogenase(see pp. 98–101) has the EC number 1, oxidoreductases; subclass 1.1, CH–OHgroup as electron donor; sub-subclass 1.1.1,NAD(P)+ as electron acceptor).


ENZIM danKinerjanya, dipengaruhi :


KonsentrasiSubstrat ----- MichaelisMenten

----- Lineweaver Burk

3. Suhu

4. pH

5. Inhibitor

a. HambatanIreversibel

b. HambatanReversibel – b.1. hambatanbersaing

b.2. Hambatantidakbersaing

c. HambatanAlosterik

6. Kovaktor a. gugusProsterik, b. koenzim, c. Aktivator

7. Vitamin vsEnzim