Prolyl endopeptidase and dipeptidyl peptidase IV are distantly related members of the same family of serine proteases.
Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined. We have compared the amino acid sequences, and this revealed a distant evolutionary relationship between the two enzymes. Conserved segments were found mainly in the C-terminal region which also contained the catalytic residues. It is concluded that the C-terminal region is a protease domain which is attached to some noncatalytic structures.
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
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Polgár
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Szabo
D000595:Amino Acid Sequence; D018819:Dipeptidyl Peptidase 4; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism*
D010455:Peptides; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D018819:Dipeptidyl Peptidase 4; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases