Biology HL
Biology HL
4
Chapters
553
Notes
Theme A - Unity & diversity
Theme A - Unity & diversity
Theme B - Form & Function
Theme B - Form & Function
Theme C - Interaction &  Interdependence
Theme C - Interaction & Interdependence
Theme D - Continuity & Change
Theme D - Continuity & Change
IB Resources
Theme C - Interaction &  Interdependence
Biology HL
Biology HL

Theme C - Interaction & Interdependence

Understanding Competitive Inhibition And Its Real-World Implications

Word Count Emoji
490 words
Reading Time Emoji
3 mins read
Updated at Emoji
Last edited on 14th Jun 2024

Table of content

Basics of competitive inhibition 🎯

  • Happens when an inhibitor binds reversibly to an enzyme's active site.
  • As long as the inhibitor stays bound, the enzyme's usual substrate can't bind.
  • The result? The enzyme can't do its job (catalyse its reaction).

💡 Fun Fact: Imagine a parking spot that both a sports car (substrate) and a truck (inhibitor) want to use. If the truck parks there, the sports car can't fit. But, if the truck drives away, the sports car can park. Similarly, enzymes have “parking spots” called active sites. If the inhibitor gets there first, the substrate can't bind.

How competitive inhibitors work 🔬

  • They're like sneaky doppelgangers! They look a lot like the enzyme's substrate.
  • Unlike the substrate, they don't turn into products, so they hang around longer.

💡 Real-World Analogy: Think of the substrate as a key that fits perfectly into a lock (the active site) and opens a door. The competitive inhibitor is like a fake key that fits the lock but can't open the door.

Inhibitor concentration matters 📊

  • More inhibitors = More inhibition.
  • Few inhibitors + Lots of substrate = Less inhibition, because the substrate usually gets to the active site first.

💡 Think of it like a race: If there are more racers (substrates) than obstacles (inhibitors), the chances of a racer winning increase!

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IB Resources
Theme C - Interaction &  Interdependence
Biology HL
Biology HL

Theme C - Interaction & Interdependence

Understanding Competitive Inhibition And Its Real-World Implications

Word Count Emoji
490 words
Reading Time Emoji
3 mins read
Updated at Emoji
Last edited on 14th Jun 2024

Table of content

Basics of competitive inhibition 🎯

  • Happens when an inhibitor binds reversibly to an enzyme's active site.
  • As long as the inhibitor stays bound, the enzyme's usual substrate can't bind.
  • The result? The enzyme can't do its job (catalyse its reaction).

💡 Fun Fact: Imagine a parking spot that both a sports car (substrate) and a truck (inhibitor) want to use. If the truck parks there, the sports car can't fit. But, if the truck drives away, the sports car can park. Similarly, enzymes have “parking spots” called active sites. If the inhibitor gets there first, the substrate can't bind.

How competitive inhibitors work 🔬

  • They're like sneaky doppelgangers! They look a lot like the enzyme's substrate.
  • Unlike the substrate, they don't turn into products, so they hang around longer.

💡 Real-World Analogy: Think of the substrate as a key that fits perfectly into a lock (the active site) and opens a door. The competitive inhibitor is like a fake key that fits the lock but can't open the door.

Inhibitor concentration matters 📊

  • More inhibitors = More inhibition.
  • Few inhibitors + Lots of substrate = Less inhibition, because the substrate usually gets to the active site first.

💡 Think of it like a race: If there are more racers (substrates) than obstacles (inhibitors), the chances of a racer winning increase!

Unlock the Full Content! File Is Locked Emoji

Dive deeper and gain exclusive access to premium files of Biology HL. Subscribe now and get closer to that 45 🌟