Biological catalysts

1. Increase rate of reaction by lowering activation

pH
energy.
Temperature Deviation from optimum pH
Temperature increases beyond -> enzyme denaturation
2. Actually not used up in the biochemical reaction.
optimal level -> enzyme (more deviation) or change
Enzyme-substrate interactions denaturation -> active site in active site (less deviation)
1. Enzyme + substrate = enzyme-substrate altered -> substrate cannot -> substrate cannot bind ->
complex. Factors affecting rate of bind -> no enzyme-substrate no enzyme-substrate
2. Reaction takes place to form products. enzyme-activity complex. complex.
3. Products released to medium and enzyme
released.
4. Free enzyme again enter into another reaction. Substrate concentration
Concentration of substrate increases ->
Lock and Key model rate of reaction increases -> more
substrate -> all active sites of enzyme
saturated -> addition of further substrate
has no effect on reaction rate.

Enzyme Inhibitors
concentration Two types: competitive and
Concentration of enzyme non-competitive
Induced Fit model
increases -> rate of Competitive inhibitors:
reaction increases -> affect initial rate but not
more enzyme-substrate maximal rate.
complex -> more enzyme Non-competitive
-> substrate limited -> no inhibitors: affect maximal
further increase in rate rate.
(rate constant).
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