Govt. Exams
Entrance Exams
In non-competitive inhibition, both Km and Vmax are affected proportionally. On a Lineweaver-Burk plot (1/v vs 1/[S]), this results in lines with different slopes that intersect on the y-axis.
Ca²⁺ is required for enzymatic activity and is not consumed in the reaction, making it a cofactor. Many proteases require metal ions as structural or catalytic cofactors.
Tertiary structure requires secondary structure elements. Secondary structures (α-helix, β-sheet) fold into tertiary structure; one cannot exist without the other.
Apparent Km = Km(1 + [I]/Ki) = 2(1 + 1/0.5) = 2(1 + 2) = 6 mM. Competitive inhibition increases apparent Km without changing Vmax.
Serine proteases (like trypsin, chymotrypsin) form an acyl-enzyme intermediate through a nucleophilic attack by the active site serine residue.
GAA codes for Glutamic acid (Glu), GUA codes for Valine (Val). This is a non-conservative substitution of a charged to hydrophobic residue.
Cooperative binding (positive cooperativity) occurs when binding of one substrate molecule increases affinity for subsequent molecules, a classic example of allosteric regulation as seen in hemoglobin.