Enzim (Cara Kerja Enzim dan Macam Inhibitor)

wety yuningsih

4 Jul 202006:40

Summary

TLDRIn this educational video, Weti Dwi Yuningsih explores enzyme mechanisms, focusing on the lock and key model and induced fit theory. She explains how enzymes are specific to substrates and how inhibitors, both competitive and non-competitive, interfere with enzyme function. Competitive inhibitors resemble substrates and compete for binding, while non-competitive inhibitors bind elsewhere on the enzyme, preventing substrate interaction. The video also hints at upcoming topics, including metabolism, catabolism, and anabolism, encouraging viewers to stay tuned for more.

Takeaways

🔬 The script discusses the working mechanism of enzymes, focusing on two theories: the lock and key model and the induced fit theory.
🔑 In the lock and key model, enzymes are compared to a lock that only one specific key (substrate) can fit, highlighting enzyme specificity.
🧬 The induced fit theory suggests that the enzyme's active site adjusts its shape to fit the substrate, allowing for binding and reaction.
🚫 The script explains enzyme inhibitors, which are molecules that decrease enzyme activity by binding to enzymes.
⛔️ Competitive inhibitors are similar in shape to the substrate and compete with it for binding to the enzyme's active site.
💊 An example of a competitive inhibitor is carbon monoxide, which competes with oxygen for binding to hemoglobin, potentially causing carbon monoxide poisoning.
🚫 Non-competitive inhibitors bind to a different part of the enzyme, preventing the substrate from binding to the active site, regardless of the substrate's shape.
💊 An example of a non-competitive inhibitor is penicillin, which binds to an enzyme and prevents bacterial growth by inhibiting cell division.
📚 The script mentions a quiz question about the lock and key model, emphasizing the enzyme's shape matching the substrate for specificity.
📈 The script hints at upcoming material on metabolism, including the concepts of catabolism and anabolism.
👍 The presenter encourages viewers to like and subscribe for more educational content and ends with a polite sign-off.

Q & A

What are the two main mechanisms by which enzymes operate?
-The two main mechanisms by which enzymes operate are the 'Lock and Key' theory and the 'Induced Fit' theory.
Can you explain the 'Lock and Key' theory of enzyme action?
-The 'Lock and Key' theory suggests that the enzyme acts as a lock and the substrate as a key. A specific enzyme only fits with a specific substrate, forming an enzyme-substrate complex that leads to the desired product.
How does the 'Induced Fit' theory differ from the 'Lock and Key' theory?
-Unlike the 'Lock and Key' theory, the 'Induced Fit' theory states that the enzyme's active site changes shape to fit the substrate. This allows the enzyme and substrate to bind even if they are not initially perfectly complementary in shape.
What is an enzyme inhibitor, and what are the two types discussed?
-An enzyme inhibitor is a substance that decreases the activity of an enzyme. The two types discussed are competitive inhibitors and non-competitive inhibitors.
How do competitive inhibitors affect enzyme activity?
-Competitive inhibitors have a similar shape to the substrate and compete with the substrate for binding to the enzyme's active site. This prevents the substrate from binding, thereby reducing enzyme activity.
What is a real-life example of a competitive inhibitor?
-A real-life example of a competitive inhibitor is carbon monoxide, which competes with oxygen to bind with hemoglobin, potentially leading to carbon monoxide poisoning.
What is the mechanism of non-competitive inhibitors?
-Non-competitive inhibitors bind to a different part of the enzyme, not the active site. This binding changes the enzyme's shape, making it impossible for the substrate to bind and thus inhibiting enzyme activity.
Can you provide an example of a non-competitive inhibitor in real life?
-Penicillin is an example of a non-competitive inhibitor. It binds to bacterial enzymes and prevents them from synthesizing cell walls, thereby inhibiting bacterial growth.
What is the significance of enzyme specificity?
-Enzyme specificity ensures that each enzyme only catalyzes a specific reaction with a specific substrate, which is crucial for the regulation and efficiency of biochemical processes in the body.
What topics will be covered in the next session, according to the script?
-The next session will cover the topics of metabolism, including the definition of metabolism and the differences between catabolism and anabolism.

Outlines

00:00

🔬 Enzyme Function and Inhibitors

This paragraph discusses the function of enzymes and the types of inhibitors. It begins with an introduction to Weti Dwi Yuningsih and the topic of enzymes. The script then explains two theories of enzyme function: the lock and key model, where an enzyme (the lock) has a specific shape that fits a substrate (the key), and the induced fit model, where the enzyme's active site changes shape to accommodate the substrate. The paragraph continues to describe competitive inhibitors, which resemble the substrate and compete for binding to the enzyme, using carbon monoxide's competition with oxygen for binding to hemoglobin as an example. Non-competitive inhibitors are also mentioned, which bind elsewhere on the enzyme, preventing substrate binding. The paragraph concludes with an example of non-competitive inhibition in the form of penicillin, an antibiotic that inhibits bacterial growth by binding to the enzyme's active site.

05:00

📚 Understanding Enzyme Specificity and Metabolism

In this paragraph, the script focuses on the specificity of enzyme action and introduces the concept of metabolism. It reiterates the lock and key theory, emphasizing the enzyme's active site's shape complementarity with the substrate. The paragraph then presents an image to illustrate the enzyme-substrate relationship and asks the audience to consider the specificity of enzyme action. The script wraps up with a teaser for the next topic, which will cover the meaning of metabolism and the difference between catabolism and anabolism. The speaker also encourages the audience to like and subscribe for more educational content and ends with a polite apology and a traditional Islamic greeting.

Mindmap

Keywords

💡Enzyme

Enzymes are biological catalysts that speed up chemical reactions in living organisms. They play a crucial role in the video's theme by being the main subject of discussion. In the script, the function and mechanism of enzymes are explained, highlighting their specificity and the way they interact with substrates.

💡Substrate

A substrate is a molecule upon which an enzyme acts. It is essential to the function of enzymes, as described in the video where the substrate is compared to a key that fits into a lock (the enzyme's active site), illustrating the specificity of enzyme-substrate interactions.

💡Lock-and-Key Model

The Lock-and-Key Model is a theory that explains how enzymes and substrates interact. The video script mentions this model, describing the enzyme's active site as a lock that can only be fitted by a specific key, which is the substrate, emphasizing the precise fit required for the reaction to occur.

💡Induced Fit Theory

The Induced Fit Theory is another model discussed in the video that explains enzyme-substrate interactions. According to the script, unlike the Lock-and-Key Model, the enzyme's active site is flexible and can adjust its shape to fit the substrate, allowing for a dynamic interaction between the enzyme and substrate.

💡Competitive Inhibitor

A competitive inhibitor is a molecule that resembles the substrate and competes with it for binding to the enzyme's active site. The script provides the example of carbon monoxide competing with oxygen for binding to hemoglobin, which illustrates the inhibitor's effect on enzyme function.

💡Non-Competitive Inhibitor

A non-competitive inhibitor binds to a site on the enzyme other than the active site, affecting the enzyme's ability to bind to the substrate. The video script mentions penicillin as an example of a non-competitive inhibitor that affects bacterial enzyme function, thereby inhibiting bacterial growth.

💡Hemoglobin

Hemoglobin is a protein in red blood cells that carries oxygen. In the script, it is used as an example to explain how a competitive inhibitor like carbon monoxide can interfere with the binding of oxygen, leading to carbon monoxide poisoning.

💡Carbon Monoxide Poisoning

Carbon Monoxide Poisoning is a medical condition resulting from the binding of carbon monoxide to hemoglobin, preventing oxygen transport. The script uses this as an example of how competitive inhibitors can have severe biological consequences.

💡Penicillin

Penicillin is an antibiotic that acts as a non-competitive inhibitor of bacterial enzymes. The script explains its function in inhibiting bacterial growth by binding to enzymes and preventing their activity, which is crucial for bacterial reproduction.

💡Metabolism

Metabolism refers to the set of life-sustaining chemical reactions in cells. The script mentions an upcoming discussion on metabolism, including the concepts of catabolism and anabolism, indicating a broader context of biochemical processes beyond enzyme function.

💡Catabolism and Anabolism

Catabolism and anabolism are two opposing metabolic processes. Catabolism involves breaking down molecules to release energy, while anabolism is the construction of molecules. The script teases a future discussion on these concepts, which are fundamental to understanding the overall theme of biochemical reactions.

Highlights

Introduction to the discussion about enzymes and inhibitors.

Explaining the working mechanism of enzymes with two theories: lock and key and induced fit.

Lock and key theory describes enzymes as a lock that only fits one specific substrate.

Induced fit theory suggests that the enzyme's active site adjusts to fit the substrate.

Enzymes work specifically with one substrate, showcasing their specificity.

Introduction to enzyme inhibitors and their role in blocking enzyme activity.

Competitive inhibitors have a similar shape to the substrate, competing for the enzyme's active site.

Carbon monoxide competes with oxygen for binding to hemoglobin, causing carbon monoxide poisoning.

Non-competitive inhibitors bind elsewhere on the enzyme, preventing substrate binding.

Penicillin as an example of a non-competitive inhibitor, inhibiting bacterial growth.

Differences between competitive and non-competitive inhibitors explained.

A quiz question on the lock and key theory as an explanation for enzyme function.

Clarification of the enzyme's active site shape matching the substrate shape.

A visual aid is presented to explain the specificity of enzyme action.

Transition to the next topic: metabolism, including catabolism and anabolism.

An invitation for viewers to like, subscribe, and look forward to the next video on metabolism.

A closing remark with a polite apology and a religious blessing.