@article{0e76c61053f911dd8d9f000ea68e967b,
title = "Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV.",
abstract = "Dipeptidyl peptidases 8 and 9 have been identified as gene members of the S9b family of dipeptidyl peptidases. In the present paper, we report the characterization of recombinant dipeptidyl peptidases 8 and 9 using the baculovirus expression system. We have found that only the full-length variants of the two proteins can be expressed as active peptidases, which are 882 and 892 amino acids in length for dipeptidyl peptidase 8 and 9 respectively. We show further that the purified proteins are active dimers and that they show similar Michaelis-Menten kinetics and substrate specificity. Both cleave the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV. Inhibition of dipeptidyl peptidases IV, 8 and 9 using the well-known dipeptidyl peptidase IV inhibitor valine pyrrolidide resulted in similar K(i) values, indicating that this inhibitor is non-selective for any of the three dipeptidyl peptidases.",
author = "Bjelke, {Jais R} and Jesper Christensen and Nielsen, {Per F} and Sven Branner and Kanstrup, {Anders B} and Nicolai Wagtmann and Rasmussen, {Hanne B}",
note = "Keywords: Amino Acid Sequence; Antigens, CD26; Baculoviridae; Chromatography, Gel; Dipeptidases; Dipeptidyl Peptidases; Enzyme Activation; Enzyme Inhibitors; Humans; Kinetics; Molecular Sequence Data; Peptide Fragments; Protein Structure, Quaternary; Pyrroles; Recombinant Proteins; Sequence Alignment; Substrate Specificity; Valine",
year = "2006",
doi = "10.1042/BJ20060079",
language = "English",
volume = "396",
pages = "391--9",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "2",
}