Title : Structural relationship between lipases and peptidases of the prolyl oligopeptidase family.

Pub. Date : 1992 Oct 26

PMID : 1397329






6 Functional Relationships(s)
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1 In prolyl oligopeptidase and its homologues, which constitute a new serine protease family, the order of the catalytic Ser and His residues in the amino acid sequence is the reverse of what is found in the trypsin and subtilisin families. Serine prolyl endopeptidase Homo sapiens
2 Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase. Serine prolyl endopeptidase Homo sapiens
3 Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase. Aspartic Acid prolyl endopeptidase Homo sapiens
4 Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase. Serine prolyl endopeptidase Homo sapiens
5 Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase. Histidine prolyl endopeptidase Homo sapiens
6 This comparison identifies the catalytic Asp residue in the prolyl oligopeptidase family. Aspartic Acid prolyl endopeptidase Homo sapiens