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Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes
Nature
|October 30, 1975
Summary
Bacterial serine proteases share surprising structural similarities with mammalian pancreatic enzymes, despite limited primary homology. This suggests a common evolutionary path from simpler bacterial forms to complex mammalian proteases.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Bacterial serine proteases and mammalian pancreatic proteases are crucial enzyme families.
- Primary structural homology between these groups is generally considered slight.
Purpose of the Study:
- To investigate the structural similarities and differences between bacterial serine proteases and mammalian pancreatic enzymes.
- To understand the evolutionary relationship between these enzyme classes.
Main Methods:
- X-ray crystallography was used to determine the structure of the bacterial enzyme SGPB at 2.8-A resolution.
- Comparative structural analysis was performed against known structures of the chymotrypsin family.
Main Results:
- Two-thirds of the residues in SGPB adopt a similar polypeptide chain conformation to the chymotrypsin family.
- Three major regions of significant difference were identified between the bacterial and pancreatic enzymes.
Conclusions:
- Despite limited primary sequence homology, significant conformational similarities exist between bacterial serine proteases and mammalian pancreatic enzymes.
- The identified structural differences highlight the evolutionary divergence from primitive bacterial enzymes to sophisticated pancreatic proteases.
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