Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes.
Although primary structural homology between bacterial serine proteases and those from the mammalian pancreas is slight, two-thirds of the residues in the bacterial enzyme SGPB as seen at 2.8-A resolution, adopt a similar polypeptide chain conformation to that of the chymotrypsin family. The three major regions of difference show how this family of proteolytic enzymes has developed from the more primitive bacterial to the relatively sophisticated pancreatic enzymes.
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D005075:Biological Evolution; D002918:Chymotrypsin; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase; D010447:Peptide Hydrolases; D011487:Protein Conformation; D012694:Serine; D013329:Structure-Activity Relationship
D012694:Serine; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D010196:Pancreatic Elastase