EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.21.B26 | endothelial lipase + H2O |
- |
Mus musculus |
? |
- |
? |
3.4.21.B26 | human immunodeficiency virus type 1 Vpr + H2O |
undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr |
Mus musculus |
? |
- |
? |
3.4.21.B26 | Lefty protein + H2O |
- |
Mus musculus |
? |
- |
? |
3.4.21.B26 | more |
no substrate: amyloid-beta precursor protein |
Mus musculus |
? |
- |
? |
3.4.21.B26 | more |
both isoforms can cleave a number of fluorogenic substrates of general formula Arg/Lys-(Xaa)n-(Arg)-, where n= 2, 4, or 6 |
Homo sapiens |
? |
- |
? |
3.4.21.B26 | more |
death at birth of the PC5/6-deficient embryos |
Mus musculus |
? |
- |
? |
3.4.21.B26 | more |
substrate cleavage analysis. Strong preference of Arg at position P1 and P4 |
Homo sapiens |
? |
- |
? |
3.4.21.B26 | more |
development of a high-throughput immunohistochemic assay for human proprotein convertase 5/6 for detecting uterine receptivity, method evaluation, overview |
Homo sapiens |
? |
- |
? |
3.4.21.B26 | osteopontin + H2O |
Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype |
Mus musculus |
? |
- |
? |
3.4.21.B26 | osteopontin + H2O |
the enzyme (PC5/6A) efficiently and completely cleaves human osteopontin into three distinct fragments migrating at about 50 kDa, about 18 kDa, and 16 kDa, with evidence for the predicted cleavage sites being at 168RSKSKKFR175-/- and 241KQSR244-/-. PC5/6 also partially cleaves mouse osteopontin to release fragments of about 30 kDa and 29 kDa |
Mus musculus |
? |
- |
? |