Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.B27 extracted from

  • Nelsen, S.M.; Christian, J.L.
    Site-specific cleavage of BMP4 by furin, PC6, and PC7 (2009), J. Biol. Chem., 284, 27157-27166.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B27

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme displays resistance to alpha1-PDX Xenopus laevis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Xenopus laevis 16020
-

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Xenopus laevis
-
oocyte the cleaved form of PC7 is present in both embryos and oocytes, PC7-like activity is not detected in oocytes Xenopus laevis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the PC7 precursor protein undergoes efficient autocatalytic activation in both oocytes and embryos. PC7 requires a P2 basic residue to cleave a substrate Xenopus laevis ?
-
 ?
pro-bone morphogenetic protein 4 + H2O PC7, or a convertase with similar substrate specificity, functions to selectively cleave the S1 site of pro-BMP4 in a developmentally regulated fashion Xenopus laevis bone morphogenetic protein 4 + ?
-
 ?

Synonyms

Synonyms Comment Organism
PC7 also known as PC8, LPC, SPC7, or PCSK7 Xenopus laevis