Organism | UniProt | Comment | Textmining |
---|---|---|---|
Drosophila melanogaster | P42787 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + H2O | adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD | Drosophila melanogaster | pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly + Lys | - |
? | |
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys-Arg + H2O | adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD | Drosophila melanogaster | pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + Arg | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CPD | - |
Drosophila melanogaster |
svr | - |
Drosophila melanogaster |
General Information | Comment | Organism |
---|---|---|
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 | Drosophila melanogaster |
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 | Drosophila melanogaster |