Analysis of an enzyme-substrate complex by X-ray crystallography and transferred nuclear Overhauser enhancement measurements: porcine pancreatic elastase and a hexapeptide

Biochemistry. 1988 Jan 26;27(2):725-30. doi: 10.1021/bi00402a035.


The hexapeptide substrate Thr-Pro-nVal-NMeLeu-Tyr-Thr reacts with porcine pancreatic elastase sufficiently slowly that accelerated crystallographic data collection procedures and two-dimensional transferred nuclear Overhauser enhancement measurements could be used to study the geometry of binding. Both studies report a time-averaged population of the Michaelis complex state, prior to proteolysis. This result provides an important data point along the reaction coordinate pathway for serine proteases. Crystallographic data to 1.80-A resolution were used in the structure analysis with refinement to an R-factor of 0.19.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Oligopeptides / metabolism*
  • Pancreas / enzymology*
  • Pancreatic Elastase / metabolism*
  • Protein Binding
  • Protein Conformation
  • Swine
  • X-Ray Diffraction / methods


  • Oligopeptides
  • Pancreatic Elastase