Comparative molecular modeling of the active subunit of human kininase I

Agents Actions Suppl. 1992:38 ( Pt 1):368-75. doi: 10.1007/978-3-0348-7321-5_46.

Abstract

The structure of the enzymatically active subunit of human plasma carboxypeptidase N was determined by computer aided model building by homology using the structural coordinates from carboxypeptidase A. The active site of carboxypeptidase N has been well conserved in comparison with carboxypeptidase A. Differences in substrate specificity can be explained by the comparison of energetically favorable binding sites for different atomic probe groups.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carboxypeptidases / chemistry
  • Carboxypeptidases / genetics
  • Carboxypeptidases / metabolism
  • Carboxypeptidases A
  • Humans
  • Lysine Carboxypeptidase / chemistry*
  • Lysine Carboxypeptidase / genetics
  • Lysine Carboxypeptidase / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Substrate Specificity
  • Thermodynamics

Substances

  • Carboxypeptidases
  • Carboxypeptidases A
  • Lysine Carboxypeptidase