Govt Exams
Vitamin K-dependent carboxylation of glutamate residues in prothrombin and other clotting factors creates γ-carboxyglutamate residues that coordinate Ca2+ ions, essential for binding to phospholipid membranes and clotting cascade progression.
Turnover number (kcat = Vmax/[E]total) represents the number of substrate molecules converted to product per enzyme molecule per unit time at maximum velocity. It indicates catalytic efficiency when substrate is saturating.
Chymotrypsin is secreted as chymotrypsinogen. Trypsin (activated by enterokinase) cleaves a specific dipeptide from chymotrypsinogen to generate active chymotrypsin, which then undergoes autolytic cleavage for full activation.
GroEL/GroES in prokaryotes forms a barrel-like structure that creates an isolated environment for protein folding. GroEL binds unfolded proteins using ATP hydrolysis, providing conformational assistance distinct from Hsp70's role in preventing aggregation.
PP2A is a major serine/threonine phosphatase that plays crucial roles in reversing kinase-mediated phosphorylation. Its dysfunction is associated with various cancers, making it an important tumor suppressor enzyme.
Phenylalanine hydroxylase requires tetrahydrobiopterin (BH4) as a cofactor for the hydroxylation of phenylalanine to tyrosine. Mutations in this enzyme or BH4 synthesis lead to PKU, causing intellectual disability if untreated.
Allosteric enzymes like phosphofructokinase show cooperative binding where substrate binding at one subunit increases affinity at others. This produces an S-shaped curve rather than the hyperbolic Michaelis-Menten curve, allowing for better metabolic control.
Aminoacyl-tRNA synthetases achieve high fidelity through a two-step selection process: initial selection during aminoacylation and a second proofreading step (editing) that hydrolyzes incorrectly charged tRNA-amino acid complexes before they leave the enzyme.
Collagen has a characteristic Gly-X-Y tripeptide repeat pattern where glycine appears at every third position. This allows tight packing in the triple helix structure. Hydroxyproline (formed by post-translational modification of proline) stabilizes the helix.
Competitive inhibitors compete with substrate for the active site, increasing apparent Km while Vmax remains unchanged. Non-competitive inhibitors bind to a site other than the active site, decreasing Vmax without changing Km.