2. Academic Validation
  3. Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion

Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion

  • Biochem Med Metab Biol. 1988 Dec;40(3):305-10. doi: 10.1016/0885-4505(88)90133-8.
Y Shimamori 1,  Y Watanabe,  Y Fujimoto
Affiliations

Affiliation

  • 1 Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
PMID: 3233187 DOI: 10.1016/0885-4505(88)90133-8
Abstract

The degradation of enkephalin and related Peptides by highly purified dipeptidyl Aminopeptidase III (EC 3.4.14.4) was studied. The Enzyme releases the N-terminal dipeptide units from substrates greater in length than the tetrapeptide. The Enzyme exhibits an optimum of pH 7.5, Km of 81 microM and Vmax of 0.043 mumole/min for Leu-enkephalin. Its activity was markedly stimulated by Co2+, with both the Km and Vmax being increased. Among the enkephalin-related Peptides examined, des-Tyr1-Leu-enkephalin was the most rapidly hydrolyzed with Co2+, but only slight stimulation was observed with Co2+.

Figures