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Literature summary for 3.4.17.22 extracted from

  • Sidyelyeva, G.; Wegener, C.; Schoenfeld, B.P.; Bell, A.J.; Baker, N.E.; McBride, S.M.; Fricker, L.D.
    Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior (2010), Cell. Mol. Life Sci., 67, 2991-3004.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster P42787
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Substrates and Products (Substrate)

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
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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
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Synonyms

Synonyms Comment Organism
CPD
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Drosophila melanogaster
svr
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Drosophila melanogaster

General Information

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