• Enzyme they are protein catalysts that increase rate of reactions without being changed

• They have 2 names the short name and the systematic name
1. Short name
• Ending of name has “ase” attached to the substrate of the reaction
2. Systematic name
• Enzymes are classified in class subclass  sub subclass
• We have a classification number for each enzyme
 6 major classes of enzymes
1. Oxidoreductases catalyses oxidation- reduction reactions (lactate dehydrogenase)
2. Transferases catalyses transfer of C-, N-, P- containing groups (Serine hydroxymethyl transferase)
3. Hydrolases Catalyze cleavage of bonds by addition of water (urease)
4. Lyases Catalyze cleavage of C–C, C–S, and certain C–N bonds no H2o (Pyruvate decarboxylase)
5. Isomerases rearrangement of bonds (Methylmalonyl CoA mutase)
6. Ligases same as biosynthesis Catalyze formation of bonds between carbon and O, S, and N coupled to hydrolysis of high energy phosphates
(Pyruvate carboxylase)
 Enzyme properties
1. Active sites
• Region where substrate binds
• There formed by folding protein containing a.a side chains
• Substrate binds the enzyme forming enzyme-substrate complex
• This binding causes conformational change to enzyme forming enzyme-product complex
• This dissociates into enzyme and product
2. Catalytic efficiency
• Catalysed reactions are highly efficient
• They proceed 10^3-10^8 times faster then un catalysed
• Turnover number/ kcat is the number of molecules of substrate converted to product per enzyme molecule per second
3. Specificity
• Enzymes are specific, interacting with one or few substrates
• Catalyze one chemical reaction, enzymes made in cell determine cell reactions
4. Location within the cell
• Many enzymes are localized in specific organelles within the cell
• This compartmentalization serves to isolate the reaction substrate or product from other competing reactions
• This provides a favorable environment for the reaction and organizes the thousands of enzymes present in the cell into purposeful pathways.
5. Regulation
• Enzyme activity can be regulated, that is, increased or decreased, so that the rate of product formation responds to cellular need
6. Holoenzymes, apoenzymes, cofactors, and coenzymes
• Some enzymes require molecules other than proteins
• Holoenzyme refers to the active enzyme with its nonprotein component
• Apoenzyme enzyme without its nonprotein moiety its inactive
• Cofactor If the nonprotein moiety is a metal ion, such as Zn2+ or Fe2+
• Coenzyme derived from vitamins, it’s a small organic molecule
• Cosubstrates Coenzymes that only transiently associate with the enzyme, dissociate from the enzyme in an altered state
• Prosthetic group coenzymes that are permanently associated with the enzyme and returned to its original form (non-protein group)
 FACTORS AFFECTING REACTION VELOCITY
• Substrate concentration
1. Maximal velocity
• The rate/velocity of a reaction The number of substrate molecules converted to product per unit time
• Velocity is usually expressed as number of product formed per minute
• The rate of an enzyme catalyzed reaction increases with substrate concentration until a maximal velocity is reached
• The leveling off of the reaction rate at high substrate concentrations reflects all enzyme active sites being saturated by substrate
2. Hyperbolic shape of the enzyme kinetics curve
• Most enzymes show Michaelis Menten kinetics
• The plot of initial reaction velocity against substrate concentration , is hyperbolic (same as oxygen dissociation curve of myoglobin)
• Allosteric enzymes do not follow Michaelis Menton kinetics and show a sigmoidal curve (same as oxygen dissociation curve of hemoglobin)
• Sigmoidal more then one polypeptide chain, multimerec
• Temperature
1. Increase of velocity with temperature
• Reaction velocity increases with temperature until a peak velocity is reached
• Increase is a result of increased number of molecules having sufficient energy to pass over energy barrier and form products of the reaction
2. Decrease of velocity with higher temperature
• Further increase of temperature causes a decrease in reaction velocity as a result of temperature induced denaturation of the enzyme
 pH
1. Effect of pH on the ionization of the active site
• The concentration of protons affects reaction velocity
• Catalytic process require that the enzyme and substrate have specific chemical groups either a ionized or un ionized state must be present
• For example, catalytic activity may require that an amino group of the enzyme be in the protonated form (–NH3+). At alkaline pH, this group is
deprotonated, and the rate of the reaction declines
2. Effect of pH on enzyme denaturation
• Extremes of pH can also lead to denaturation of the enzyme
• The structure of the catalytically active protein molecule depends on the ionic character of the amino acid side chains.
3. Variable pH optimum
• pH of max enzyme activity is different in enzymes
• It reflects the [H+] at which the enzyme functions in the body
 Characteristics of Km:
• Km, the Michaelis constant, is characteristic of an enzyme and its particular substrate
• reflects the affinity of the enzyme for that substrate
• Km does not vary with enzyme concentration
• Low km means high activity
• High km means low activity
 VITAMIN OTHER NAMES ACTIVE FORM FUNCTION
Vitamin C Ascorbic acid Ascorbic acid Antioxidant Coenzyme for
hydroxylation reactions
Proline → hydroxyproline
Lysine →
hydroxylysine
Vitamin B6 Pridoxine Pyridoxal phosphate Coenzyme for enzymes,
Pyridoxamine particularly in amino acid
Pyridoxal metabolism
Vitamin B1 Thiamine Thiamine pyrophosphate Coenzyme of enzymes
catalyzing: Pyruvate → acetyl
CoA α-Ketoglutarate →
Succinyl CoA
Niacin Nicotinic acid NAD+ Electron transfer
Nicotinamide NADP+
Vitamin B2 Riboflavin FMN Electron transfer
FAD
Biotin — Enzyme-bound biotin Carboxylation reactions

Pantothenic acid — Coenzyme A Acyl carrier