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Literature summary extracted from

  • Hu, Z.; Zhang, H.; Haley, B.; Macchi, F.; Yang, F.; Misaghi, S.; Elich, J.; Yang, R.; Tang, Y.; Joly, J.C.; Snedecor, B.R.; Shen, A.
    Carboxypeptidase D is the only enzyme responsible for antibody C-terminal lysine cleavage in Chinese hamster ovary (CHO) cells (2016), Biotechnol. Bioeng., 113, 2100-2106 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.17.22 medicine knocking out CpD gene expression provides one solution to eliminating C-terminal lysine heterogeneity for therapeutic antibody production Cricetulus griseus

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.6 Cricetulus griseus G3HR95
-
-
3.4.17.22 Cricetulus griseus G3HR95
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.16.6 CHO cell
-
 Cricetulus griseus
-
3.4.17.22 CHO cell
-
 Cricetulus griseus
-

Synonyms

EC Number Synonyms Comment Organism
3.4.16.6 CPD
-
 Cricetulus griseus

General Information

EC Number General Information Comment Organism
3.4.16.6 physiological function CpD is the only endogenous carboxypeptidase that cleaves antibody heavy chain C-terminal lysine in CHO cells. Knockdown of CpD by RNAi increases C-terminal lysine levels of antibodies, whereas there is no obvious change in C-terminal lysine levels when carboxypeptidase CpM, CpN, CpB, or CpE is knocked downIn a CpD knockout mutant, C-terminal lysine cleavage is completely abolished Cricetulus griseus
3.4.17.22 physiological function carboxypeptidase D is the only enzyme responsible for antibody C-terminal lysine cleavage in Chinese Hamster Ovary (CHO) cells Cricetulus griseus