Study of Enzymes & Coenzymes

Lecture No. 6

How important are enzymes?

Enzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products, without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. Enzymes work by lowering the activation energy of a reaction, thus allowing the reaction to proceed much faster.

Maltase

Terminologies
Substrate substance reacted upon by an enzyme Apoenzyme is an enzyme without its cofactor; it is the protein molecule to which a coenzyme will bind to produce the holoenzyme. Ex. RNA polymerase Holoenzyme the active and operative form of an enzyme. This is the complete fully functioning enzyme. It is the combination of an apoenzyme with its cofactor. Proenzymes are inactive precursors of enzymes. Ex. Zymogen, pepsinogen Kinase substance used to activate the proenzyme. Coenzyme is an organic non-protein molecule that is functional art of an enzyme. They are generally defined as cofactors. Antienzyme is a substance that neutralizes or counteracts the action of an enzyme or they refer to an inhibitory enzyme or an antibody to an enzyme that retards, inhibits, or destroys enzymic activity. Isoenzyme or isozymes are enzymes that differ in amino acid sequence but catalyze the same chemical reaction (LDH1-5)

Class Class Name 1 2 3 4 5 6

Examples by trivial name

Oxidoreductase Dehydrogenase, oxidase, peroxidase, catalase Transferase Hydrolase Lyases Isomerase Ligases Kinase, transaminase, transketolase Esterase, peptidase, digestive enzymes Decarboxylase, aldolase, deaminase, fumarase Epimerase, mutase Carboxylase, acetyl CoA carboxylase

Other Coenzymes
Vitamin Niacin Pyridoxine Lipoic acid Vitamin B12 Coenzyme NAD, NADP Pyridoxal phosphate Lipoamide Adenosyl cobalamine Function
Oxidation-reduction Various reactions involved in AA activation Acyl group activation;oxidation-reduction Isomerization and methyl group transfer

Chymotrypsin (Spacefill)

Other Disorders of Enzymatic Defect Metabolic Disorder Agammaglobulinemia Alkaptonuria Gout Hemohilia A, B, & G Histidinemia Enzymatic defect Inability to form gamma globulins Absence of hepatic homogentisic acid Excessive production of uric acid Deficiency of clotting factors Deficiency of histidase

More Metabolic Disoders

Sickle cell anemia Thalassemia Von Gierkes disease Porphyria Presence of abnormal hemoglobins Presence of abnormal hemoglobins Deficiency of glucose-6phosphatase Increased excretion of uroporphyrins resulting to lavender teeth, burgundy red urine Absence of decarboxylase enzyme for branched chain amino acids

Maple syrup disease

Summary
Enzymes are biologic catalysts that increase the rates of biochemical processes but are themselves unchanged. Most (but not all) enzymes are proteins. In enzyme catalysis, one or more substrates are bound at the active sites of an enzyme, to form the enzyme-substrate complex; products are then released. The rate of chemical reaction is determined by reactant concentration and by the rate constant. All catalysts function by lowering the activation energy for a reaction. In doing so, they do not affect chemical equilibrium but only increase rates. Many enzymes utilize coenzymes in their functions; others require specific metal ions. A number of coenzymes are closely related to vitamins required in the diet.