EC Number   |
Protein Variants |
Reference |
|---|
   3.4.17.22 | E350Q |
critical active site residue in domain I, displays more than 50% activity from pH 5.0-7.5, similar to wild-type |
755155 |
| 3.4.17.22 | E350Q |
pH optimum of mutant enzyme is identical to wild-type enzyme, pH-range with 50% of maximal activity is pH 5.0-7.5 compared to pH 5.0-7.0 for wild-type enzyme |
755155 |
| 3.4.17.22 | E350Q/E762Q |
completely inactive towards all substrates and at all pH values tested |
755155 |
| 3.4.17.22 | E350Q/E762Q |
no detectable enzyme activity at any of the pH values examined |
755155 |
| 3.4.17.22 | E762Q |
critical active site residue in domain II, displays more than 50% activity from pH 6.5 to 7.5 |
755155 |
| 3.4.17.22 | E762Q |
pH optimum of mutant enzyme is pH 7.0, compared to pH 6.5 for wild-type enzyme. pH-range with 50% of maximal activity is pH 6.5-7.5 compared to pH 5.0-7.0 for wild-type enzyme |
755155 |
| 3.4.17.22 | more |
a noninfectious pre-S deletion mutant devoid of the binding region for carboxypeptidase D can be rendered infectious for primary duck hepatocytes by treatment with chymotrypsin |
688729 |
| 3.4.17.22 | more |
CPD mutant lacking the cytoplasmic trans-Golgi network-retrieval signal into primary duck hepatocytes, abolishes duck hepatitis B virus infection of transduced cells |
684108 |
| 3.4.17.22 | more |
duck CPD (dCPD) like all other CPDs identified, consists of three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each, one transmembrane domain and a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network. While two of the three luminal/extracellular domains bind Zn2+-ions and exhibit enzymatic carboxypeptidase activity towards yet unidentified cellular proteins that cross the secretory pathway, the membrane proximal C-domain of dCPD is enzymatically inactive and binds duck hepatitis B virus-preS polypeptide with very high affinity |
684108 |
| 3.4.17.22 | more |
enzyme with mutations in both domains I and II is completely inactive towards all substrates and at all pH values |
755155 |
