EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.13.18 | Co2+ |
activates |
137174 |
| 3.4.13.18 | Co2+ |
best activator |
732459 |
| 3.4.13.18 | Co2+ |
complex pattern of inhibition or activation with different dipeptide substrates |
137182 |
| 3.4.13.18 | Co2+ |
enzyme contains two binding sites |
137173 |
| 3.4.13.18 | Co2+ |
hydrolysis of the relative poor substrates, Pro-Gly and Gly-Gly is activated, whereas that of Ala-Gly is inhibited |
137179 |
| 3.4.13.18 | Co2+ |
inhibits Ala-Gly hydrolysis, activates Leu-Gly hydrolysis |
137181 |
| 3.4.13.18 | Co2+ |
when substrates are cleaved rapidly by dipeptidase, addition of Co2+ inhibits the reaction. The more slowly a substrate is hydrolyzed in the absence of metals, the greater the activating effect, activation is not accompanied by change in Km |
137173 |
| 3.4.13.18 | Mg2+ |
favors the activity towards the substrates Leu-Gly and Ala-Gly |
137181 |
| 3.4.13.18 | Mn2+ |
0.1 mM, increases prolinase activity in normal erythrocytes against Pro-Gly, Pro-Glu, Pro-Leu, Pro-Ser and Pro-Phe |
664626 |
| 3.4.13.18 | Mn2+ |
about 35% of the activation with Co2+ |
732459 |
