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Describe the function of enzymes.

Enzymes are biological catalysts made of proteins. They speed up reactions without being used up themselves. Some of the essential reactions they catalyze include respiration, photosynthesis, protein synthesis, and digestion.

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"Describe the function of enzymes."	"Enzymes are biological catalysts made of proteins. They speed up reactions without being used up themselves. Some of the essential reactions they catalyze include respiration, photosynthesis, protein synthesis, and digestion."
"Describe the induced fit model of enzyme action."	"The induced fit model of enzyme action suggests that the enzyme's active site is not a perfect fit for the substrate, but rather it changes shape in response to the substrate's presence to achieve a complementary fit."
"How does the lock and key model differ from the induced fit model?"	"The lock and key model suggests that the enzyme's active site is a perfect fit for the substrate, like a key in a lock. In contrast, the induced fit model suggests that the enzyme's active site changes shape to fit the substrate."
"How does temperature affect enzyme activity?"	"If the temperature is too low, there is not enough kinetic energy for successful collisions between the enzyme and the substrate. If the temperature is too high, enzymes denature, the active site changes shape, and enzyme-substrate complexes cannot form."
"How does pH affect enzyme activity?"	"Too high or too low a pH will interfere with the charges in the amino acids in the active site, causing the enzyme to denature."
"How do substrate and enzyme concentrations affect enzyme activity?"	"If there is not enough substrate, the reaction will be slower due to fewer collisions between the enzyme and substrate. If there are not enough enzymes, the enzyme active sites will become saturated with substrate and unable to work any faster."
"What is the role of competitive inhibitors in enzyme activity?"	"Competitive inhibitors are the same shape as the substrate and can bind to the active site, preventing the substrate from binding and the reaction from occurring. Adding more substrate can out-compete the inhibitor."
"What is the role of non-competitive inhibitors in enzyme activity?"	"Non-competitive inhibitors bind to the enzyme away from the active site, causing the active site to change shape. As a result, the substrate can no longer bind, regardless of how much substrate is added."
"Define the term 'active site' in the context of enzymes."	"The active site is a part of an enzyme that attaches to a substrate to catalyze a reaction. It is specific and unique in shape due to the specific folding and bonding in the tertiary structure of the protein."
"Do enzymes attach to all substrates or only to those that are complementary in shape?"	"Enzymes can only attach to substrates that are complementary in shape due to the specific active site."
"How do enzymes lower the activation energy needed for a reaction to occur?"	"When enzymes attach to the substrate, they can lower the activation energy needed for the reaction to occur, and therefore speed up the reaction."
"Define the 'Lock & Key Model' of enzyme action."	"The Lock & Key Model suggests that the enzyme is like a lock and that the substrate is like a key that fits into it due to their complementarity in shape. This model suggests that the enzyme active site is a fixed shape and that due to random collision, the substrate can collide and attach to the enzyme."
"Are enzymes considered globular or fibrous proteins?"	"Enzymes are considered globular proteins."
"What stage in protein development results in a unique 3D structure held in place by hydrogen, ionic, and disulfide bonds?"	"The tertiary stage in protein development results in a unique 3D structure held in place by hydrogen, ionic, and disulfide bonds."
"Describe the enzyme-substrate complex."	"The enzyme-substrate complex is formed when an enzyme binds to its substrate. The charged groups within the active site are thought to distort the substrate and therefore lower the activation energy. The products are then released, and the enzyme active site is empty and ready to be reused."
"Define the Induced Fit Model."	"The Induced Fit Model suggests that the enzyme active site is induced, or slightly changes shape, to mold around the substrate. When the enzyme-substrate complex occurs, due to the enzyme molding around the substrate, it puts strain on the bonds and therefore lowers the activation energy. The products are then removed, and the enzyme active site returns to its original shape."
"How does the Induced Fit Model differ from the Lock and Key Model?"	"The Induced Fit Model suggests that the active site changes shape and then becomes complementary in shape, whereas the Lock and Key Model suggests enzymes are a fixed shape, and the active site does not change."
"Do enzymes have a specific function?"	"Yes, enzymes have a specific function. For example, Hexosaminidase is an enzyme present in blood that breaks down gangliosides, a type of lipid found on the cell surface of membranes of nerve cells. It does not break down other lipids."
"Why does Hexosaminidase only break down gangliosides?"	"Hexosaminidase only breaks down gangliosides because enzymes are highly specific. They have an active site that is complementary to a specific substrate, in this case, gangliosides. This specificity is due to the unique shape and structure of the enzyme, which allows it to bind only to a specific substrate and catalyze a specific reaction."

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[{"id":1274954,"front":"Describe the function of enzymes.","back":"Enzymes are biological catalysts made of proteins. They speed up reactions without being used up themselves. Some of the essential reactions they catalyze include respiration, photosynthesis, protein synthesis, and digestion.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"Enzymes are proteins that act as catalysts in biological reactions. They increase the rate of these reactions by lowering the activation energy required for the reaction to occur. Enzymes are highly specific, meaning they only catalyze specific reactions. They can be involved in various processes such as respiration, photosynthesis, protein synthesis, and digestion. Enzymes are not consumed or altered during the reaction and can be reused multiple times.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275044,"front":"Describe the induced fit model of enzyme action.","back":"The induced fit model of enzyme action suggests that the enzyme's active site is not a perfect fit for the substrate, but rather it changes shape in response to the substrate's presence to achieve a complementary fit.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"The induced fit model proposes that the active site of an enzyme is not initially a perfect match for the substrate. Instead, the enzyme undergoes a conformational change upon substrate binding, allowing for a more complementary fit. This dynamic interaction enhances the enzyme's catalytic activity by promoting the formation of the enzyme-substrate complex and facilitating the chemical reaction. The induced fit model highlights the flexibility and adaptability of enzymes in optimizing their interactions with substrates.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275067,"front":"How does the lock and key model differ from the induced fit model?","back":"The lock and key model suggests that the enzyme's active site is a perfect fit for the substrate, like a key in a lock. In contrast, the induced fit model suggests that the enzyme's active site changes shape to fit the substrate.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"The lock and key model proposes a static interaction between enzyme and substrate, while the induced fit model suggests dynamic conformational changes in the enzyme's active site upon substrate binding. This impacts our understanding of enzyme-substrate interactions and the specificity of enzymatic reactions.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275082,"front":"How does temperature affect enzyme activity?","back":"If the temperature is too low, there is not enough kinetic energy for successful collisions between the enzyme and the substrate. If the temperature is too high, enzymes denature, the active site changes shape, and enzyme-substrate complexes cannot form.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"Temperature affects enzyme activity because it impacts the kinetic energy of molecules. At low temperatures, there's insufficient energy for effective enzyme-substrate collisions. High temperatures cause denaturation, altering the enzyme's active site and preventing substrate binding.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275094,"front":"How does pH affect enzyme activity?","back":"Too high or too low a pH will interfere with the charges in the amino acids in the active site, causing the enzyme to denature.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"pH affects enzyme activity because enzymes have an optimal pH at which they function best. Deviating from this optimal pH can disrupt the charges in the amino acids within the enzyme's active site. This disruption can lead to denaturation of the enzyme, rendering it inactive. Therefore, maintaining the appropriate pH is crucial for proper enzyme function.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275111,"front":"How do substrate and enzyme concentrations affect enzyme activity?","back":"If there is not enough substrate, the reaction will be slower due to fewer collisions between the enzyme and substrate. If there are not enough enzymes, the enzyme active sites will become saturated with substrate and unable to work any faster.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"Substrate concentration affects enzyme activity because enzymes can only work on substrates they come into contact with. If there is a low substrate concentration, there will be fewer collisions between the enzyme and substrate, resulting in slower reaction rates. On the other hand, enzyme concentration affects activity because enzymes have a limited number of active sites. If there is a low enzyme concentration, the active sites may become saturated with substrate, limiting the rate at which the reaction can occur.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275123,"front":"What is the role of competitive inhibitors in enzyme activity?","back":"Competitive inhibitors are the same shape as the substrate and can bind to the active site, preventing the substrate from binding and the reaction from occurring. Adding more substrate can out-compete the inhibitor.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"Competitive inhibitors interfere with enzyme activity by competing with the substrate for the enzyme's active site. This competition can be overcome by increasing the substrate concentration, which allows more substrate molecules to bind to the enzyme and outcompete the inhibitor. This ultimately restores the enzyme's normal activity.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275134,"front":"What is the role of non-competitive inhibitors in enzyme activity?","back":"Non-competitive inhibitors bind to the enzyme away from the active site, causing the active site to change shape. As a result, the substrate can no longer bind, regardless of how much substrate is added.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":0,"explanation":"Non-competitive inhibitors play a crucial role in regulating enzyme activity. Unlike competitive inhibitors, they do not compete with the substrate for the active site. Instead, they bind to a different site on the enzyme, causing a conformational change that affects the active site. This alteration prevents the substrate from binding effectively, reducing enzyme activity. Importantly, non-competitive inhibition is not influenced by substrate concentration, making it an effective mechanism for controlling enzyme function.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274957,"front":"Define the term 'active site' in the context of enzymes.","back":"The active site is a part of an enzyme that attaches to a substrate to catalyze a reaction. It is specific and unique in shape due to the specific folding and bonding in the tertiary structure of the protein.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":1,"explanation":"The active site of an enzyme is crucial for its function as it provides a specific location for substrate binding and catalysis. This specificity arises from the precise arrangement of amino acids in the enzyme's tertiary structure, allowing for efficient and selective chemical reactions to occur.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274959,"front":"Do enzymes attach to all substrates or only to those that are complementary in shape?","back":"Enzymes can only attach to substrates that are complementary in shape due to the specific active site.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":2,"explanation":"Enzymes can only attach to substrates that are complementary in shape due to the specific active site. This specificity allows for the formation of enzyme-substrate complexes, facilitating the catalysis of chemical reactions. The active site's shape and chemical properties are tailored to a specific substrate, ensuring efficient and selective binding.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274968,"front":"How do enzymes lower the activation energy needed for a reaction to occur?","back":"When enzymes attach to the substrate, they can lower the activation energy needed for the reaction to occur, and therefore speed up the reaction.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":3,"explanation":"Enzymes lower the activation energy needed for a reaction by providing an alternative pathway for the reaction to proceed. They do this by binding to the substrate and stabilizing the transition state, making it easier for the reaction to occur. This allows the reaction to happen more quickly and efficiently. Additionally, enzymes can also orient the substrate molecules in a way that promotes the formation of the transition state, further lowering the activation energy. Overall, enzymes act as catalysts by facilitating the reaction without being consumed in the process.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274974,"front":"Define the 'Lock & Key Model' of enzyme action.","back":"The Lock & Key Model suggests that the enzyme is like a lock and that the substrate is like a key that fits into it due to their complementarity in shape. This model suggests that the enzyme active site is a fixed shape and that due to random collision, the substrate can collide and attach to the enzyme.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":4,"explanation":"The Lock & Key Model of enzyme action proposes that enzymes and substrates have specific complementary shapes, akin to a lock and key. This model implies that the enzyme's active site is rigid and only fits specific substrates, highlighting the specificity of enzyme-substrate interactions.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274977,"front":"Are enzymes considered globular or fibrous proteins?","back":"Enzymes are considered globular proteins.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":5,"explanation":"Enzymes are considered globular proteins because they have a compact, spherical shape. This shape allows them to have a specific active site where they bind to substrates and catalyze chemical reactions. Globular proteins are typically soluble in water and have a wide range of functions in the body, including catalyzing biochemical reactions. In contrast, fibrous proteins have a long, extended shape and are often involved in structural roles, such as providing support and strength to tissues.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274982,"front":"What stage in protein development results in a unique 3D structure held in place by hydrogen, ionic, and disulfide bonds?","back":"The tertiary stage in protein development results in a unique 3D structure held in place by hydrogen, ionic, and disulfide bonds.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":6,"explanation":"The tertiary stage of protein development is crucial as it determines the final 3D structure. This structure is stabilized by various bonds, including hydrogen, ionic, and disulfide bonds. These interactions are essential for the protein's functionality and specificity.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274986,"front":"Describe the enzyme-substrate complex.","back":"The enzyme-substrate complex is formed when an enzyme binds to its substrate. The charged groups within the active site are thought to distort the substrate and therefore lower the activation energy. The products are then released, and the enzyme active site is empty and ready to be reused.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":7,"explanation":"The enzyme-substrate complex is a temporary association between an enzyme and its substrate. This complex is formed when the substrate binds to the active site of the enzyme. The active site contains charged groups that help in distorting the substrate, reducing the activation energy required for the reaction. Once the reaction is complete, the products are released, and the enzyme is free to bind to another substrate. This process allows the enzyme to catalyze multiple reactions efficiently.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1274994,"front":"Define the Induced Fit Model.","back":"The Induced Fit Model suggests that the enzyme active site is induced, or slightly changes shape, to mold around the substrate. When the enzyme-substrate complex occurs, due to the enzyme molding around the substrate, it puts strain on the bonds and therefore lowers the activation energy. The products are then removed, and the enzyme active site returns to its original shape.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":8,"explanation":"The Induced Fit Model proposes that the enzyme's active site adjusts its shape to accommodate the substrate, creating strain on the bonds and reducing activation energy. This allows for efficient catalysis before the enzyme returns to its original state.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275000,"front":"How does the Induced Fit Model differ from the Lock and Key Model?","back":"The Induced Fit Model suggests that the active site changes shape and then becomes complementary in shape, whereas the Lock and Key Model suggests enzymes are a fixed shape, and the active site does not change.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":9,"explanation":"The Induced Fit Model and Lock and Key Model differ in their views on enzyme and substrate interaction. The former proposes that the active site can change shape to accommodate the substrate, while the latter suggests a static, non-changing active site. This impacts our understanding of enzyme-substrate specificity and the dynamics of enzyme function.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275010,"front":"Do enzymes have a specific function?","back":"Yes, enzymes have a specific function. For example, Hexosaminidase is an enzyme present in blood that breaks down gangliosides, a type of lipid found on the cell surface of membranes of nerve cells. It does not break down other lipids.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":10,"explanation":"Yes, enzymes are highly specific in their function. Each enzyme is designed to catalyze a particular chemical reaction. This specificity is due to the unique shape of the enzyme's active site, which allows it to interact with specific substrates. For example, hexosaminidase specifically targets gangliosides and does not act on other types of lipids due to its specific structure and function.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}},{"id":1275033,"front":"Why does Hexosaminidase only break down gangliosides?","back":"Hexosaminidase only breaks down gangliosides because enzymes are highly specific. They have an active site that is complementary to a specific substrate, in this case, gangliosides. This specificity is due to the unique shape and structure of the enzyme, which allows it to bind only to a specific substrate and catalyze a specific reaction.","front_language":"English","back_language":"English","front_image":"","back_image":"","order":11,"explanation":"Enzyme specificity is crucial for biological processes. Hexosaminidase's unique structure fits gangliosides perfectly, enabling precise binding and catalysis. This specificity ensures targeted reactions, preventing unwanted breakdown of other molecules and maintaining cellular function.","deleted_at":null,"flashcard_deck_id":"uV615","original_id":null,"examMode":{"text":"","correct":"","incorrect":"","info":""}}]

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