Скачать с ютуб Enzyme Catalysis | Lock & Key, Induced Fit Model | Allosteric Enzymes | Urdu Hindi English | 2024 в хорошем качестве

Enzyme Catalysis | Lock & Key, Induced Fit Model | Allosteric Enzymes | Urdu Hindi English | 2024

Enzyme Action: Enzymes work by lowering the activation energy required for a chemical reaction to occur. They bind to substrates, positioning them for optimal reaction conditions, and facilitating the conversion of substrates to products. Lock and Key Model: The Lock and Key Model, proposed by Emil Fischer in 1894, describes the binding of substrates to enzymes. According to this model: Enzymes have a specific, rigid active site that perfectly complements the shape of the substrate. Substrates fit into the active site like a key into a lock, allowing the enzyme to catalyze the reaction. Induced Fit Model: The Induced Fit Model, proposed by Daniel Koshland in 1958, modifies the Lock and Key Model. According to this model: Enzymes have a flexible active site that changes shape upon substrate binding. The substrate induces a conformational change in the enzyme, allowing for optimal binding and catalysis. Allosteric Enzymes: Allosteric enzymes are enzymes that have multiple binding sites, called allosteric sites, in addition to the active site. These sites can bind regulatory molecules, which affect enzyme activity. Allosteric activation: Binding of an activator molecule increases enzyme activity. Allosteric inhibition: Binding of an inhibitor molecule decreases enzyme activity. Allosteric enzymes play crucial roles in metabolic pathways, allowing for fine-tuned regulation of enzyme activity in response to changing cellular conditions. Popular Hashtags for YouTube videos #biology #federalboard #enzymes #EnzymeAction #LockAndKeyModel #InducedFitModel #AllostericEnzymes #EnzymeRegulation #Biochemistry #Biology #Chemistry #Science #Education #LearnBiochemistry #BiochemistryLessons #BiologyTutorials #EnzymeMechanism #EnzymeKinetics #EnzymeInhibition #AllostericControl #MetabolicPathways