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BIOA01H3 (699)
Lecture

biochem lec 3.docx

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Department
Biological Sciences
Course
BIOA01H3
Professor
Mark Fitzpatrick
Semester
Winter

Description
Allosteric – shape of enzyme and substrate fit (lock and key) Inhibitors  - Causes a loss of catalytic activity  - Changes the proteins structure  - May be competitive or non-competitive  - Some of these effects are irreversible Competitive Inhibitors - They have similar structures to the substrate and competes with it for the active site, the effect can be reversed with an increase in the substrate concentration Non-competitive Inhibitors  - Does not have a structure like the substrate but it binds to the enzyme, not necessarily the active site.  - It changes the shape of the enzyme and active site, therefore no reaction occurs  - The effect is irreversible and therefore the substrate cannot fit the altered active site which than leaves it inactive. DNA/Nuclei
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