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What are enzymes? How are enzymes named and classified? What factors influence enzyme activity?

What are the mechanisms of enzyme action and how are they regulated? How are enzymes used in medicine?

What Are Enzymes?

They are large molecules that increase the rates of chemical reactions without undergoing any change. They are biological catalysts. Without them, life would not be possible. The vast majority are globular proteins. Some are made of ribonucleic acids, called RIBOZYMES, which catalyze the self-cleavage of certain portions of their own molecules.

What Are Enzymes?

Enzymes do not change the position of equilibrium. They cause reactions to take place faster by

lowering the activation energy.

They are remarkable in 2 respects: 1. They are extremely effective, increasing reaction rates by 109 1020. (eg. Oxidation of glucose) 2. Most of them are extremely specific.

How Are Enzymes Named and Classified?

1. Oxidoreductases catalyze redox reactions.

How Are Enzymes Named and Classified?

2. Transferases catalyze the transfer of a group of atoms, such as from one molecule to another.

How Are Enzymes Named and Classified?

3. Hydrolases catalyze hydrolysis reactions.

How Are Enzymes Named and Classified?

4. Lyases catalyze the addition of two groups to a double bond or the removal of two groups from adjacent atoms to create a double bond.




How Are Enzymes Named and Classified?

5. Isomerases catalyze isomerization reactions.

How Are Enzymes Named and Classified?

Phosphoglycerate mutase

How Are Enzymes Named and Classified?

6. Ligases, or synthetases, catalyze the joining of two molecules.


Terminology Used With Enzymes

Some enzymes are purely peptides. Others contain nonprotein portions. Cofactors may be metallic ions (Zn+2 or Mg+2) or organic compounds (coenzymes). The substrate is the compound on which the enzymes works. The specific portion of the enzyme on which the substrate binds is the active site. Cofactors are located in the active site.


Vitamin Coenzyme Reaction type Coenzyme class SOURCE: Compiled from data contained in Horton, H. R., et al. (2002). Principles of Biochemistry , 3rd edition. Upper Saddle River, NJ: Prentice Hall. Oxidative B 1 (Thiamine) TPP Prosthetic group decarboxylation Oxidation/Reductio B 2 (Riboflavin) FAD Prosthetic group n B 3 (Pantothenate) B 6 (Pyridoxine) B 12 (Cobalamin) CoA - Coenzyme A PLP Acyl group transfer Cosubstrate Transfer of groups to and from amino acids Prosthetic group

5-deoxyadenosyl cobalamin NAD +

Tetrahydrofolate Biotin

Intramolecular rearrangements

Prosthetic group

Folic acid Biotin

Oxidation/Reductio Cosubstrate n One carbon group Prosthetic group transfer

Carboxylation Prosthetic group

Terminology Used with Enzymes

Activation any process that initiates or increases the action of an enzyme (by addition of a cofactor or by cleavage of a proenzyme


Terminology Used with Enzymes

Inhibition any process that makes an enzyme less active or inactive a. Competitive b. Noncompetitive


AIDS Virus


Factors Influencing Enzyme Activity

Enzyme activity- a measure of how much reaction rates are increased A. ENZYME & SUBSTRATE CONCENTRATION

If the substrate concentration is kept constant while enzyme concentration is increased, the rate increases linearly.

Factors Influencing Enzyme Activity


If all the active

sites are occupied, no further increase in the rate is possible


Factors Influencing Enzyme Activity


OPTIMUM TEMPERATURE: Most enzymes from bacteria and higher organisms around 37C Enzymes of those that live at the ocean floor around 2 C Those that live in ocean vents under extreme conditions 90-105 C


Factors Influencing Enzyme Activity

C . pH