Hendriks D, Vingron M, Vriend G, Wang W, Nalis D, Scharpé S
Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk, Belgium.
Agents Actions Suppl. 1992;38 ( Pt 1):368-75. doi: 10.1007/978-3-0348-7321-5_46.
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.
