<prompt> Pepsin is a type ofOxidoreductaseLigaseTransferaseHydrolase  <response>: D Hydrolase PEPSIN: Pepsin is produced by the serous cells of the stomach as pepsinogen, the inactive zymogen or proenzyme. Pepsin A is the most predominant gastric protease which preferentially cleaves peptide bonds formed by amino groups of phenylalanine or tyrosine or leucine. Protease or Peptidase or Proteinase: is any enzyme that performs proteolysis; protein catabolism by hydrolysis of peptide bonds. It break down the bonds by a process - hydrolysis and convert proteins into smaller chains - peptides or even smaller units - amino acids. Pepsinogen is converted to active pepsin either by autocatalysis, brought about by other pepsin molecules or by gastric HCI pH 2.HYDROLASESPhospholipids-PhospholipaseLysophospholipidsLecithin - LysolecithinEnzymes Acting on Peptide Bonds:Exopeptidases-CarboxypeptidaseAiminoacidsEndopeptidase-AminopeptidasessmallerpeptidesE.g.Pepsin Removal of a fragment of polypeptide chain 44 amino acids in case of pig enzyme makes the inactive enzyme active after attaining a proper conformation. Pepsin is an acid-stable endopeptidase optimally active at a very low pH 2.0. The active site of the enzyme contains two carboxyl groups, which are maintained at low pH. Pepsin digestion of proteins results in peptides and a few amino acids which act as stimulants for the release of the hormone cholecystokinin from the duodenum. 