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- Enzymes and the active site (article) | Khan Academy
The answer depends on the enzyme Some enzymes speed up chemical reactions by bringing two substrates together in the right orientation Others create an environment inside the active site that's favorable to the reaction (for instance, one that's slightly acidic or non-polar)
- Enzymes (video) | Cellular energetics | Khan Academy
An enzyme is just a special chemical This means that it can react and form temporary bonds The same way sodium and chlorine come together, enzymes and their substrates can come together Hope this helps!
- More enzyme types and mechanisms of catalysis (article) | Khan Academy
Kinases: Transfer phosphate groups, often from ATP, to substrates This is very important for activating and inactivating enzymes in biochemical pathways Aminotransferases: Transfer amino groups between amino acids and keto acids
- Enzymes review (article) | Khan Academy
Each type of enzyme typically only reacts with one, or a couple, of substrates Some enzymes are more specific than others and will only accept one particular substrate
- Induced fit model of enzyme catalysis (video) | Khan Academy
Now since enzymes have unique active sites, we say that enzymes are specific to certain substrates, and by extension certain reactions But let's dive a little deeper into what happens when enzymes and substrates bind to each other and how that binding pattern changes as a reaction progresses
- SN1 mechanism: Kinetics and substrates - Khan Academy
It looks like your browser doesn't support embedded videos Don't worry, you can still download it and watch it with your favorite video player! Download Video: SN1 mechanism: Kinetics and substrates
- Effect of substrate on the rate of SN1 reaction-Part 2
This video is in continuation to part one and talks about the reason behind the reluctance of a phenylic or vinylic substrate to react via SN1 mechanism while the allylic and benzylic substrates easily react via SN1
- Cooperativity and the Hill coefficient (article) | Khan Academy
The binding of an allosteric regulator can lead to changes in the enzyme’s shape or conformation, influencing how efficiently it binds to substrates or catalyzes reactions
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