BIOLOGI SMA Kelas 12 - Metabolisme Part 1 (Enzim) | GIA Academy

0:00 Hi Love [Music] hello friends welcome back to the Kia Academy youtube channel Hopefully friends are always healthy and continue to be enthusiastic in everyday life there are various activities that are carried out these activities can affect the condition of our bodies physical activities such as the following sports will certainly make our bodies fit while relaxing activities while snacking if

0:46 done continuously will form fat deposits in the stomach and the body becomes overweight approximately what causes the body size of people who rarely and people who often do physical activity to be different turns out this is related to the body's metabolic process How does this process occur in our body we will learn it in this video Hi so we will learn the body's metabolic process especially the enzyme part keep watching the video okay Well What is metabolism metabolism is a series of chemical reactions that take place in the cells of living things that can be

1:32 converted into energy for survival so when we eat the metabolic process will process nutrients from food that has been absorbed by the body to be converted into energy the speed of this metabolic process will be influenced by enzymes as biocatalysts meaning Enzymes can accelerate biological reactions without experiencing changes in chemical structure enzymes are chemical compounds or special proteins that accelerate chemical reactions in the body by lowering activation energy we can pay attention to the following graph The click work graph shows that enzymes work by lowering the activation energy. Activation energy is the energy

2:19 required for a reaction to occur. A decrease in activation energy can be seen from the difference in energy required in a reaction assisted by enzymes and not assisted by enzymes. By using enzymes, the activation energy required is less than that without enzymes. This causes the reaction to occur faster with less free energy required. Based on the components of the enzyme, it is divided into two types, namely simple enzymes which only consist of proteins. Complex enzymes or better known as holoenzymes. Coenzymes consist of several components, namely protein components or enzymes that are thermolabile

3:05 or not heat resistant so they are easily denatured. Non-protein components or prosthetic groups are thermostable or not easily damaged by heat. These components are in the form of coenzymes, which are organic compounds, for example, vitamin Ennard and coenzyme A. Cofactors are inorganic metal compounds, for example, metal ions such as Cu, Fe, Mn, Zn. cake000.com [Music] Hi, this is the structure of a holoenzyme with the components that make it up. Apoenzymes, coenzymes, and cofactors in addition to components that can attach to enzymes. Enzymes have an active side, namely a

3:51 part or place on the enzyme that functions as a place for substrate attachment. The allosteric side is the side In addition to the active side of the enzyme that can bind to the enzyme activator This side can be disturbed by non-competitive inhibitors in addition there are also competitive inhibitors whose structure is similar to the substrate the substrate attaches to the active side of the enzyme and will produce a new product the work of the enzyme is very specific because the active side of the enzyme is very selective to the chemical form of the substrate that will be catalyzed the bond formed between the enzyme and the substrate is weak so that the reaction can take place back and forth [Music] Hi friends enzymes have the

4:37 following properties enzymes only change the reaction rate meaning the enzyme does not change the final product formed or affect the reaction balance only increases the rate of a reaction enzymes work specifically meaning the enzyme only affects certain substrates For example the enzyme maltase can only break down maltose into glucose enzymes are proteins so their work is influenced by PH and temperature at high temperatures the enzyme will be denatured or changes in the protein structure occur while at low temperatures the work of the enzyme will be inhibited enzymes work back and forth or reversibly meaning Enzymes can catalyze the decomposition of a compound into another compound or vice

5:24 versa catalyze the arrangement of these compounds into the original compound In addition in the body's metabolic process n is only needed in small amounts enzymes in the form of colloids can react with acid substrates or base and can be used repeatedly [Music] the mechanism of enzyme action occurs when a substrate molecule collides with the right enzyme molecule, then the super will attach to the enzyme to form an enzyme-substrate complex and result in a reaction that ends with the formation of a product molecule.

6:09 There are two theories that explain how enzymes work, namely the lock and key theory or lo kenkey and the theory of induced fixity or indospeed. Let 's discuss these theories one by one [Music] first, the lock and key theory explains that enzymes are likened to a lock because they have a small part that can bind to the substrate. This part is called the active site. Meanwhile, the substrate is likened to a key because it can bind precisely to the active site of the enzyme. The substrate will attach to the enzyme to form an enzyme-substrate complex and result in a reaction that ends with the formation of a product molecule. The relationship between the enzyme and the substrate

6:55 forms a weak bond. If the enzyme is damaged due to the influence of temperature or pH, the shape of the active site of the enzyme will change, causing the substrate to no longer be suitable for the enzyme. Next, the theory of induced fixity states that the active site of the enzyme can change shape according to its substrate or is flexible. If a subset enters the active site of the enzyme, the enzyme will change shape precisely when binds to the substrate to form an enzyme-substrate complex and an enzyme-product complex until the product can leave the Steve enzyme side now friends can understand these two theories, yes,

7:43 further we will discuss the factors that influence how enzymes work, enzyme work can be influenced by several factors, the following temperature changes in pH, enzyme concentration, substrate concentration, binding agents or activators and inhibitors or inhibitors increase in temperature, each enzyme has a specific optimum temperature, temperatures that are too high in enzymes can cause protein denaturation and temperatures that are too low can inhibit the rate of enzyme reactions at temperatures of 0° Celsius or below will be inactive, but the enzyme is not damaged, but if the

8:28 enzyme temperature exceeds the optimum limit, the enzyme will be damaged or denatured, for example, enzymes in humans have an optimal temperature of 35-40 degrees Celsius, while there are bacteria that live in hot water that have an optimum temperature of 70° Celsius, the second factor is changes in pH or acidity, changes in pH result in the active side of the enzyme also changing so that it can prevent the substrate from binding to the active side of the enzyme. In addition, changes in pH also result in the denaturation process in enzymes, for example, the ptyalin enzyme in the mouth works at a neutral pH, the pepsin enzyme in the stomach works at an acidic pH, while the trypsin enzyme in the intestine works at an alkaline pH The

9:18 third factor is enzyme concentration, enzyme concentration and reaction rate are linearly connected, the greater the enzyme concentration, the reaction rate will increase. The relationship between enzyme concentration and reaction rate is shown in the following graph. Next, the substrate concentration is called the substrate concentration in a reaction. It will increase the reaction rate if the amount of enzyme in the reaction remains the same. If the enzyme is too little and the substrate is too much, the reaction will run slowly and even there will be substrates that are not catalyzed. The relationship between enzyme concentration and substrate and reaction rate is shown in the following graph. The

10:06 next factor is a binding agent or activator. An activator is a substance that functions to stimulate or accelerate enzyme reactions. Examples of activators include salts and alkali metals in dilute conditions of around two percent to five percent and metal ions ( Cl ). We know that under normal conditions, enzymes will only be active if the active site matches the substrate. If the substrate does not match the active site, the enzyme cannot react. With the presence of an activator attached to the enzyme side, the enzyme will be active and the active site of the enzyme will change shape according to its substrate to produce a product. The

10:52 last factor is an inhibitor or inhibitor. Inhibitors are divided into two, namely: First, competitive inhibitors are inhibitors that bind strongly to the active site of the enzyme. The structure of competitive inhibitors is similar to the structure of the substrate so that these inhibitors compete with the substrate to bind to the active site of the enzyme. Inhibitors This competitive inhibitor can be eliminated by adding the substrate concentration, for example this inhibitor is oxalosuccinate, secondly non-competitive inhibitors are inhibitors that bind to the allosteric side or side other than the active side of the enzyme, this inhibitor causes the active side of the enzyme to change so that the substrate

11:38 cannot bind to the active side of the enzyme Hi, this inhibitor cannot be eliminated even by adding the substrate, for example this inhibitor is the antibiotic penicillin Well, friends, here is the table of differences between competitive inhibitors and non-competitive inhibitors according to our previous discussion Hi, can you understand? [Music] so that friends understand better Let's solve the following example questions, the first question is given several statements, we are asked to determine the correct statement about enzymes

12:25 because the statement in the question is related to temperature, so we remember the relationship between enzymes and temperature, we know that each enzyme has a specific optimum temperature, enzymes at a temperature of 0° Celsius or below will be inactive, but the enzyme is not damaged, but if sweety exceeds the optimum limit, the enzyme will be damaged or denatured, so the correct statement about the relationship between enzymes and temperature is shown by numbers 1, 3, and 4, the answer is C, the second question contains a graph that states the relationship between activity and changes in PH, we are asked to analyze the statement that corresponds to the graph. Similarly, with temperature,

13:12 each enzyme has a specific optimum PH Changes in pH cause the active side of the enzyme to change so that it can prevent the binding of the substrate to the active side of the enzyme. In addition, changes in pH also cause the denaturation process in enzymes, for example, the ptyalin enzyme in the mouth works at a neutral pH or 7. The pepsin enzyme in the stomach works at a small acidic pH of seven, while the trypsin enzyme in the intestine works at a large alkaline pH of seven. Well, based on the graph in the question, the enzyme works optimally at a pH of 7 or neutral, so the correct answer is B [Music] Okay, friends, in this video we have learned everything about enzymes, starting

13:59 from the components and structure of enzymes, the properties of enzymes, pain about enzymes, to the factors that influence enzyme activity. Hopefully, it can be understood. That's our discussion about the metabolism of the enzyme section. We will continue the discussion about catabolism in the next video. Wait, see you later [Music] Hi, hi