Gpr endopeptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.78 gpr endopeptidase
Pappalysin-1 is a 400-kDa disulfide-linked dimeric zinc metalloendopeptidase in peptidase family M43, circulating in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor. It cleaves the Met135-/-Lys bond in insulin-like growth factor binding protein (IGFBP)-4 and the Ser143-/-Lys bond in IGFBP-5; IGF increases hydrolysis of IGFBP-4 about 20-fold whereas IGFBP-5 hydrolysis is decreased about two-fold. In pregnancy it regulates IGF bioavailability and fetal growth. It features an M43-family zinc catalytic domain.
Pappalysin-1 is a 400-kDa disulfide-linked dimeric zinc metalloendopeptidase in peptidase family M43, circulating in human pregnancy mainly as a complex with the proform of eosinophil major basic protein, which acts as an inhibitor. It cleaves the Met135-/-Lys bond in insulin-like growth factor binding protein (IGFBP)-4 and the Ser143-/-Lys bond in IGFBP-5; IGF increases hydrolysis of IGFBP-4 about 20-fold whereas IGFBP-5 hydrolysis is decreased about two-fold. In pregnancy it regulates IGF bioavailability and fetal growth. It features an M43-family zinc catalytic domain.
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