The metal-binding motif of dipeptidyl peptidase III directly influences the enzyme activity in the copper derivative of dipeptidyl peptidase III.

@article{Hirose2004TheMM,
  title={The metal-binding motif of dipeptidyl peptidase III directly influences the enzyme activity in the copper derivative of dipeptidyl peptidase III.},
  author={Junzo Hirose and Hiroshi Kamigakiuchi and Hiroyuki Iwamoto and Hideaki Fujii and Masanori Nakai and Mituru Takenaka and Rieko Kataoka and Makoto Sugahara and Satoru Yamamoto and Kayoko M. Fukasawa},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={431 1},
  pages={1-8}
}
The zinc-binding motif (HELLGH) of dipeptidyl peptidase III (DPP III) is different from the common zinc-binding motif (HExxH) of metallopeptidases. To clarify the importance of the zinc-binding motif part of DPP III for enzymatic activity, we measured the recovery of the enzyme activity of apo-Leu(453)-deleted dipeptidyl peptidase III (apo-Leu(453)-del-DPP III), which has a motif (HELGH) like that of the common peptidase (HExxH), in the presence of various metal ions. The enzyme activity of apo… CONTINUE READING