Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral intermediate collapses and product 2 released. -Aromatic R group of polypeptide substrate is positioned in hydrophobic pocket and the carbonyl of that residue is positioned in the oxyanion hole -His57 deprotonates Ser195 -Formation of acyl-enzyme intermediate -Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195. -Tetrahedra intermediate collapses and product 1 released -H2O enters active site of chumotrunsir -Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole -His57 deprotonates H20 -H20 does nucleophilic attack on carbonyl of substrate in oxyanion hole
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10.
-Tetrahedral intermediate collapses and product 2 released.
-
-His57 deprotonates Ser195
-Formation of acyl-enzyme intermediate
-Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195.
-Tetrahedra intermediate collapses and product 1 released
-H2O enters active site of chumotrunsir
-Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole
-His57 deprotonates H20
-H20 does nucleophilic attack on carbonyl of substrate in oxyanion hole
Step by step
Solved in 3 steps
