Evolution of proteolytic enzymes.
Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D005075:Biological Evolution; D001777:Blood Coagulation; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D005796:Genes; D006801:Humans; D009154:Mutation; D010447:Peptide Hydrolases / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D011480:Protease Inhibitors / Q000032:analysis / Q000378:metabolism; D011487:Protein Conformation; D021382:Protein Sorting Signals; D013379:Substrate Specificity
D004792:Enzyme Precursors; D010455:Peptides; D011480:Protease Inhibitors; D021382:Protein Sorting Signals; D010447:Peptide Hydrolases