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Literature summary for 3.4.21.75 extracted from

  • Bonod-Bidaud, C.; Beraud, M.; Vaganay, E.; Delacoux, F.; Font, B.; Hulmes, D.J.; Ruggiero, F.
    Enzymatic cleavage specificity of the proalpha1(V) chain processing analysed by site-directed mutagenesis (2007), Biochem. J., 405, 299-306.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
furin mutant and wild-type constructs transiently transfected into HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
R1584A/R1585A mutations efficiently protect the C-propeptide cleavage from furin activity. In absence of furin activity, bone morphogenetic protein-1 is capable of processing the C-propeptide even though less efficiently than furin Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
procollagen V + H2O proteolytic processing of the proalpha1(V) C-propeptide chain. Proteolytic C-propeptide removal by furin occurs between Arg1585 and Asn1586. Processing of the C-propeptide by furin is more efficient than processing by bone morphogenetic protein-1 Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Proprotein convertase
-
Homo sapiens