Comparative molecular modeling of the active subunit of human kininase I.
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.
Hendriks
D
D
Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk, Belgium.
Vingron
M
M
Vriend
G
G
Wang
W
W
Nalis
D
D
Scharpé
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002268:Carboxypeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D043422:Carboxypeptidases A; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013379:Substrate Specificity; D013816:Thermodynamics
D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D001121:Lysine Carboxypeptidase