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Biochemistry Enzymes 33b4db2b

Serine proteases

A
Hydrolyze peptide bonds involving carboxyl groups of serine residues
B
Are characterized by having several active sites per molecule, each containing a serine residue
C
Are inactivated by reaching with one molecule of di-isopropyl-fluorophosphate per molecule of protein
D
Are exopeptidases
High-Yield Explanation
It is otherwise called alpha-anti-proteinase or protease inhibitor. It inhibits all serine proteases (proteolytic enzymes having a serine at their active center), such as plasmin, thrombin, trypsin, chymotrypsin, elastase, and cathepsin. Serine protease inhibitors are abbreted as Serpins. They are enzymes with a serine residue at the active site and most of the proteolytic enzymes belong to this group, e.g. trypsin, chymotrypsin, clotting factors Serine proteases examples-Trypsin, Chymotrypsin,Clotting factorsRef: DM Vasudevan, Page no: 44

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