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ENZYMES AND SUBSTRATES

Enzyme = Functional protein

Has all the properties of a protein


(macromolecule, heat, pH)

Functions as biocatalyst
Biocatalyst:
- substrate specific
- reaction specific
- can be regulated in the body

Inorganic catalyst
- resistant to heat
- not specific to certain substr/reaction
- Pt, Zn, H+
Cellular enzymes exist in compartments

Carry out activities in organelles, membranes


and cytosol

Enzymes in blood for coagulation process


Enzymes catalyze conversion of substrates
into products

E + S  ES  E + P

E interacts with S to for ES complex


Mechanism of interaction ;
1. Emil Fischer
Lock and Key Model

2. Koshland
Induced fit model
Enzyme undergoes conformational change
Active site, substrate site, catalytic site

Specific area on enzyme surface that binds


to substrate to form E-S complex, before
enzyme reaction takes place
Why are enzymes essential to body
Homeostasis?

- At body temp. biochem. processes


have to proceed fast enough to
meet needs of the body

- Enzymes (unlike inorganic catalysts)


can be regulated in the body
Inborn Error of Metabolism is caused

enzyme abnormality
What is enzyme activity?

Enzyme activity measured by velocity of


enzyme reaction (v)

v = amount of product per time unit


(sec. minute)
Also

v = remaining substrate per time unit


FACTORS THAT AFFECT REACTION RATE
A.Substrate Concentration
v = velocity

Vm = maximum velocity

When enzyme conc kept constant,

v will >> with increasing [S]

Vm reached when enzyme molecules


are saturated with S
B. Temperature
Temperature >>  v increased

Heat will cause increase of kinetic energy

Incr collision of E and S  ES  P

Vm is reached at optimum temp.

Raising temp beyond opt.temp. will damage


enzyme protein  enz activity decreased
C. Acidity, pH

Enzymes have specific optimum pH


Pepsin ~ pH = 1

Trypsin ~ pH = 7-8

Enzymes denature at high or low pH


relative to optimum pH
ENZYME REGULATION
A. Competitive Inhibition

- Similarity between S and I

- S and I compete for active site

- Enzyme reaction inhibited when I binds


to active site  no P formation
E + I  EI  E + I

- E not destroyed.
After release, can react with substrate

- Excess substrate eliminates effect of I

- Enzyme reaction can reach Vmax

Example: Inh of succinate DH by malonate


B. Non-competitive Inhibition

- Inhibitor very different from S


- I can bind on E outside of active site
- I causes E denaturation
- Ex. : Hg, Pb
ZYMOGEN, PROENZYME
- Active site located in the interior of E molecule
- Can be exposed to the surface upon activation

- Trypsinogen  Trypsin

Zymogen prevents self digestion of tissues on its


way from site of formation to site of E reaction.
COENZYMES, COFACTORS
Non-protein molecule needed for enzyme activity

A. Metal ions: Zn2+, Fe2+, Mg2+

B. Organic molecules = Coenzymes


Derivatives of vitamin B

- Holoenzyme + Enzyme + Coenzyme (Cofactor)

- Apoenzyme = Protein portion of holoenzyme


Vitamin Coenzyme Activity

Nicotinic acid NAD Oxid-Reduct


Riboflavin FAD Oxid-Reduct
Thiamine Thiamine PP Decarboxylation
Pantothenic acid Coenzyme A Activation of FA
Biotin Biotin CO2 binding