EC Number   |
General Information |
Reference |
|---|
   3.4.17.22 | malfunction |
knockdown of endogenous CPD expression in Huh7 HCC cells by RNA interference reduces cell proliferation, blocks the cell cycle at G1 phase, and increases apoptosis |
731593 |
| 3.4.17.22 | malfunction |
to investigate the function of the various carboxypeptidase domains (1-3 active or inactive domains), transgenic flies are created expressing specific forms of CPD in the embryonic-lethal svrPG33 mutant. All constructs containing an active carboxypeptidase domain rescue the lethality with varying degrees, and full viability require inactive carboxypeptidase domain-3 |
708064 |
| 3.4.17.22 | more |
carboxypeptidase D is a host specific binding partner for full-length large envelope protein of duck hepatitis B virus. Carboxypeptidase D is important in productive DHBV infection, although it can not confer susceptibility to duck hepatitis B virus infection in any cell line |
753313 |
| 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 |
753046 |
| 3.4.17.22 | physiological function |
Svr regulates the memory formation via insulin pathway in neurosecretory cells outside the mushroom body of brain |
755289 |
| 3.4.17.22 | physiological function |
the carboxypeptidase D homolog silver regulates memory formation via insulin pathway in Drosophila |
755289 |
| 3.4.17.22 | physiological function |
together with the differences in pH optima, the different substrate specificities of CPD domains I and II allow the enzyme to perform distinct functions in the various locations within the cell |
755155 |
| 3.4.17.22 | physiological function |
transfected DCPD could confer duck hepatitis B virus binding to non-duck cell lines which is followed by rapid virus release from cells. Coexpression of furin leads to DCPD cleavage and increases virus retention |
709747 |
| 3.4.17.22 | physiological function |
transgenic flies overexpressing active carboxypeptidase domain-1 or -2 are similar to each other and to the viable svr mutants Overexpression of carboxypeptidase domain-1 or -2 reduce the levels of Lys/Arg-extended adipokinetic hormone intermediates. CPD domains-1 and -2 have largely redundant functions in the processing of growth factors, hormones, and neuropeptides |
708064 |
