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A-disintegrin and metalloproteinase-like-1 + H2O
?
-
-
-
-
?
A-disintegrin and metalloproteinase-like-2 + H2O
?
-
-
-
-
?
A-disintegrin and metalloproteinase-like-3 + H2O
?
-
-
-
-
?
A-disintegrin and metalloproteinase-like-5 + H2O
?
-
-
-
-
?
acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin-7-amide + H2O
?
-
preferred substrate
-
?
acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
?
acetyl-KTKQLR-7-amido-4-methylcoumarin + H2O
acetyl-KTKQLR + 7-amino-4-methylcoumarin
-
most efficiently and selectively cleaved
-
-
?
acetyl-PAKSARSVRA + H2O
acetyl-PAKSAR + SVRA
-
sequence derived from pro-insulin growth factor
-
?
acetyl-PAKSERDVST + H2O
acetyl-PAKSER + DVST
-
sequence derived from pro-insulin growth factor
-
?
Boc-RERR-7-amido-4-trifluoromethyl coumarin + H2O
Boc-RERR + 7-amino-4-trifluoromethyl coumarin
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
Q6KW60
-
-
-
?
pERTKR-4-methyl coumaryl-7-amide + H2O
?
-
exhibits a gradual increase in cleavage with the amount of PC4 used
-
-
?
pro-insulin growth factor + H2O
?
-
-
-
?
pro-insulin growth factor-I + H2O
?
-
-
-
-
?
pro-insulin growth factor-II + H2O
?
-
-
-
-
?
pro-insulin growth factor-II + H2O
insulin growth factor-II
PC4 cleaves pro-insulin growth factor-II to generate the intermediate processed form insulin growth factor-II (1-102) and, subsequently, mature insulin-growth factor-II (1-67)
-
-
?
pro-pituitary adenylate cyclase-activating polypeptide + H2O
?
-
-
-
-
?
proform acrosin-binding protein + H2O
mature acrosin-binding protein + ?
proform IGF-2 + H2O
mature IGF-2 + ?
Q6KW60
-
-
-
?
propituitary adenylate cyclase-activating peptide + H2O
PACAP38 + PACAP27
-
PACAP peptides are produced during spermiogenesis, their receptors are found in Leydig cells and spermatids
-
?
REKR-4-methylcoumarin-7-amide + H2O
?
-
-
-
?
RSKR-4-methylcoumarin-7-amide + H2O
RSKR + 7-amino-4-methylcoumarin
-
-
-
?
RVRR-4-methylcoumarin-7-amide + H2O
?
-
-
-
?
t-butyloxycarbonyl-RVRR-4-methyl coumaryl-7-amide + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-RVRR-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
YQTLRRRVKRSLVVPTD + H2O
YQTLRRRVKR + SLVVPTD
-
preferred substrate
-
?
additional information
?
-
proform acrosin-binding protein + H2O
mature acrosin-binding protein + ?
a sperm fertilization molecule located in the acrosomal matrix, the enzyme activates the substrate by processing from a 58.5 kDa precursor to a 27.5 kDa mature form
-
-
?
proform acrosin-binding protein + H2O
mature acrosin-binding protein + ?
recombinant His-tagged substrate protein, the enzyme activates the substrate by processing from a 58.5 kDa precursor to a 27.5 kDa mature form. Two potential PCSK4 cleavage sites in the ACRBP sequence are KRVR-/-120-123 and KMSR-/-500-503
-
-
?
additional information
?
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
recombinant PCSK4 in vitro cleaves synthetic peptide substrates after an Arg in a basic sequence context, most often after paired basic residues, but it cleaves uniquely better after a single Arg preceded by a Lys at P4
-
-
?
additional information
?
-
-
recombinant PCSK4 in vitro cleaves synthetic peptide substrates after an Arg in a basic sequence context, most often after paired basic residues, but it cleaves uniquely better after a single Arg preceded by a Lys at P4
-
-
?
additional information
?
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
cleaves fluorogenic peptide substrates at pairs of basic residues
-
?
additional information
?
-
-
PC4 substrates are growth factors proIGF-1 and proIGF-2, hormonal polypeptides, proPACAP, and surface proteins of the ADAM family, e.g. ADAM1 or fertilin alpha, ADAM2 or fertilin beta, ADAM3 or cyritestin, and ADAM5
-
-
?
additional information
?
-
-
PC4 cleaves peptide bonds in the sequence R/K/H-X-X/R/K/-R, with X being any amino acid except cysteine, a preferred motif is KXKR
-
-
?
additional information
?
-
-
no substrate: amyloid-beta precursor protein
-
?
additional information
?
-
-
digestion of intramolecularly quenched fluorogenic peptides by PC4
-
-
?
additional information
?
-
PCSK4 appears to be a crucial enzyme for reproduction
-
-
?
additional information
?
-
-
PCSK4 appears to be a crucial enzyme for reproduction
-
-
?
additional information
?
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
recombinant PCSK4 in vitro cleaves synthetic peptide substrates after an Arg in a basic sequence context, most often after paired basic residues, but it cleaves uniquely better after a single Arg preceded by a Lys at P4
-
-
?
additional information
?
-
-
recombinant PCSK4 in vitro cleaves synthetic peptide substrates after an Arg in a basic sequence context, most often after paired basic residues, but it cleaves uniquely better after a single Arg preceded by a Lys at P4
-
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
cleaves fluorogenic peptide substrates at pairs of basic residues
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
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pro-insulin growth factor + H2O
?
-
-
-
?
proform acrosin-binding protein + H2O
mature acrosin-binding protein + ?
a sperm fertilization molecule located in the acrosomal matrix, the enzyme activates the substrate by processing from a 58.5 kDa precursor to a 27.5 kDa mature form
-
-
?
proform IGF-2 + H2O
mature IGF-2 + ?
Q6KW60
-
-
-
?
additional information
?
-
additional information
?
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
PC4 substrates are growth factors proIGF-1 and proIGF-2, hormonal polypeptides, proPACAP, and surface proteins of the ADAM family, e.g. ADAM1 or fertilin alpha, ADAM2 or fertilin beta, ADAM3 or cyritestin, and ADAM5
-
-
?
additional information
?
-
PCSK4 appears to be a crucial enzyme for reproduction
-
-
?
additional information
?
-
-
PCSK4 appears to be a crucial enzyme for reproduction
-
-
?
additional information
?
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
-
members of the ADAM family, in particular ADAM1 or fertilin alpha, ADAM2 or fertilin beta, and ADAM3 or cyritestin, are potential substrates for PCSK4. ADAMs are biosynthesized in male germ cells as type-1 transmembrane precursor proteins and undergo a cascade of testicular and post-testicular proteolytic cleavages to their acrosomebound forms
-
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
additional information
?
-
-
proprotein convertase subtilisin/kexin type 4 is associated with glucose-regulated protein78/immunoglobulin heavy-chain binding protein. The prozymogen cannot efficiently self-activate in somatic cells
-
-
?
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4-chloromercuribenzoate
-
strong inhibition
CDTA
-
complete inhibition at 1-10 mM
Co2+
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.25 mM
CRES peptides
-
development of PC4 inhibitors based onthe CRES reactive site loop, miniserpin inhibitors, sequences, overview
-
Cu2+
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.012 mM
cystatin related epididymal spermatogenic dimer
Q6KW60
i.e. CRES, an epididymal serpin, the recombinant protein inhibits the enzyme activity in vitro in a differential manner depending on its oligomeric state, overview
-
cystatin related epididymal spermatogenic monomer
Q6KW60
i.e. CRES, an epididymal serpin, the recombinant protein inhibits the enzyme activity in vitro in a differential manner depending on its oligomeric state, overview
-
decanoyl-RVRK-chloromethyl ketone
-
-
decanoyl-RVRR-chloromethyl ketone
-
-
EDTA
-
complete inhibition at 1-10 mM
EGTA
-
complete inhibition at 1-10 mM
Hg2+
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+
Ni2+
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+
PCSK4-Eda-1
peptidyl-(ene-diyne amino acid) derivative PAKSAR-(ene-diyne amino acid)-SVR
-
PCSK4-Eda-2
peptidyl-(ene-diyne amino acid) derivative PAKSER-(ene-diyne amino acid)-DVS
-
PCSK4-Eda-3
peptidyl-(ene-diyne amino acid) derivative RVKNKGRR-(ene-diyne amino acid)-IAY
-
PCSK4-Eda-4
peptidyl-(ene-diyne amino acid) derivative QRRVKR-(ene-diyne amino acid)-SVVVP
-
prodomain rPC4101-116 peptide
-
strong competitive inhibition
-
Zn2+
-
order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+
additional information
inhibition of PC4 by a PC4-specific inhibitor, developed from its own prodomain sequence near the primary activation site, blocks pro-insulin growth factor-II processing and reduces trophoblast cell migration, which can be partly restored by addition of mature insulin growth factor-II
-
additional information
-
inhibition of PC4 by a PC4-specific inhibitor, developed from its own prodomain sequence near the primary activation site, blocks pro-insulin growth factor-II processing and reduces trophoblast cell migration, which can be partly restored by addition of mature insulin growth factor-II
-
additional information
incorporation of enediyne functional moiety between P1 and P1' residues of a peptide substrate of a protease represents a novel and effective strategy for the design of small molecule peptidomimetic inhibitors of the cognate protease
-
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evolution
proprotein convertase 4 is a member of a family of proprotein convertases that convert inactive precursor proteins into their mature and active forms
evolution
the enzyme belongs to the 9-member superfamily of mammalian subtilases collectively called proprotein convertases or proprotein convertase subtilisin/kexins that convert inactive precursor proteins into their active mature forms by endoproteolytic cleavage
evolution
Q6KW60
the enzyme belongs to the 9-member superfamily of mammalian subtilases collectively called proprotein convertases or proprotein convertase subtilisin/kexins that convert inactive precursor proteins into their active mature forms by endoproteolytic cleavage
malfunction
inactivation of its gene in mouse does not alter spermatogenesis, but renders sperm incapable of fertilizing oocytes, resulting in part from sperm susceptibility to a premature acrosome reaction and from reduced ability to bind to the zona pellucida. In female mice, a lack of PCSK4 causes subfertility associated with impaired folliculogenesis
malfunction
PC4 knockout mice exhibit severely impaired male fertility due to premature sperm acrosome reaction
physiological function
-
PC4 activates everal protein precursors in the secretory pathway of mammalian reproduction system with a vital role in fertilization and sperm maturation
physiological function
the enzyme belongs to a family of endoproteinases involved in the proteolytic conversion of secretory precursor proteins to their active forms. PCSK4 appears to be a crucial enzyme for reproduction
physiological function
the enzyme belongs to a family of endoproteinases involved in the proteolytic conversion of secretory precursor proteins to their active forms. PCSK4 appears to be a crucial enzyme for reproduction. It stimulates the invasiveness of human placental trophoblasts in culture, suggesting that it may facilitate placentation in vivo
physiological function
the enzyme activity plays a crucial role in mammalian fertilization via activation of sperm surface proteins
physiological function
Q6KW60
the enzyme activity plays a crucial role in mammalian fertilization via activation of sperm surface proteins
physiological function
the enzyme is linked to mammalian fertilization and placenta growth
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?
x * about 58000, mature enzyme, SDS-PAGE
?
x * about 62000, mature enzyme, predicted from amino acid sequence
?
x * about 72000, pro-zymogen, SDS-PAGE
?
-
x * about 62000, mature enzyme, predicted from amino acid sequence
?
-
x * about 62000, mature enzyme, predicted from amino acid sequence
additional information
PCSKs are biosynthesized in the endoplasmic reticulum as multidomain preproproteins consisting of an N-terminal signal peptide followed by a pro domain, a conserved catalytic domain, a P domain, and a variable C-terminal domain. After cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates. Domain structure, overview
additional information
-
PCSKs are biosynthesized in the endoplasmic reticulum as multidomain preproproteins consisting of an N-terminal signal peptide followed by a pro domain, a conserved catalytic domain, a P domain, and a variable C-terminal domain. After cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates. Domain structure, overview
additional information
PCSKs are biosynthesized in the endoplasmic reticulum as multidomain preproproteins consisting of an N-terminal signal peptide followed by a pro domain, a conserved catalytic domain, a P domain, and a variable C-terminal domain. After cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates
additional information
-
PCSKs are biosynthesized in the endoplasmic reticulum as multidomain preproproteins consisting of an N-terminal signal peptide followed by a pro domain, a conserved catalytic domain, a P domain, and a variable C-terminal domain. After cotranslational removal of the signal peptide, the resulting proPCSK undergoes maturation by autocatalytic cleavage between the pro and the catalytic domains, within a cleavage motif that is also recognized by the fully activated enzyme in the primary sequence of its physiological substrates
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Seidah, N.G.; Chretien, M.
Pro-protein convertases of subtilisin/kexin family
Methods Enzymol.
244
175-188
1994
Mammalia, Rattus norvegicus
brenda
Basak, A.; Toure, B.B.; Lazure, C.; Mbikay, M.; Chretien, M.; Seidah, N.G.
Enzymic characterization in vitro of recombinant proprotein convertase PC4
Biochem. J.
343
29-37
1999
Rattus norvegicus
brenda
De Strooper, B.; Creemers, J.W.; Moechars, D.; Huylebroeck, D.; Van De Ven, W.J.; Van Leuven, F.; Van den Berghe, H.
Amyloid precursor protein is not processed by furin, PACE 4, PC1/3, PC2, PC4 and PC5/6 of the furin family of proprotein processing enzymes
Biochim. Biophys. Acta
1246
185-188
1995
Mus musculus
brenda
Basak, S.; Chretien, M.; Mbikay, M.; Basak, A.
In vitro elucidation of substrate specificity and bioassay of proprotein convertase 4 using intramolecularly quenched fluorogenic peptides
Biochem. J.
380
505-514
2004
Mus musculus, Rattus norvegicus
brenda
Bassi, D.E.; Fu, J.; Lopez de Cicco, R.; Klein-Szanto, A.J.
Proprotein convertases: "master switches" in the regulation of tumor growth and progression
Mol. Carcinog.
44
151-161
2005
Homo sapiens
brenda
Qiu, Q.; Basak, A.; Mbikay, M.; Tsang, B.K.; Gruslin, A.
Role of pro-IGF-II processing by proprotein convertase 4 in human placental development
Proc. Natl. Acad. Sci. USA
102
11047-11052
2005
Homo sapiens (Q6UW60), Homo sapiens
brenda
Gyamera-Acheampong, C.; Tantibhedhyangkul, J.; Weerachatyanukul, W.; Tadros, H.; Xu, H.; van de Loo, J.; Pelletier, R.; Tanphaichitr, N.; Mbikay, M.
Sperm from mice genetically deficient for the PCSK4 proteinase exhibit accelerated capacitation, precocious acrosome reaction, reduced binding to egg zona pellucida, and impaired fertilizing ability
Biol. Reprod.
74
666-673
2006
Mus musculus (P29121), Mus musculus
brenda
Freyer, C.; Kilpatrick, L.M.; Salamonsen, L.A.; Nie, G.
Pro-protein convertases (PCs) other than PC6 are not tightly regulated for implantation in the human endometrium
Reproduction
133
1189-1197
2007
Homo sapiens (Q6UW60)
brenda
Gyamera-Acheampong, C.; Mbikay, M.
Proprotein convertase subtilisin/kexin type 4 in mammalian fertility: a review.
Hum. Reprod. Update
15
237-247
2009
Mus musculus (P29121), Mus musculus, Homo sapiens (Q6UW60), Homo sapiens
brenda
Basak, A.; Shervani, N.J.; Mbikay, M.; Kolajova, M.
Recombinant proprotein convertase 4 (PC4) from Leishmania tarentolae expression system: purification, biochemical study and inhibitor design
Protein Expr. Purif.
60
117-126
2008
Rattus norvegicus
brenda
Basak, A.; Shervani, N.; Kolajova, M.; Cherla, S.; Basak, S.
Novel reactive site loop derived mini-serpin inhibitors of recombinant proprotein convertase 4
Adv. Exp. Med. Biol.
611
105-106
2009
Mammalia
brenda
Gyamera-Acheampong, C.; Sirois, F.; Denis, N.J.; Mishra, P.; Figeys, D.; Basak, A.; Mbikay, M.
The precursor to the germ cell-specific PCSK4 proteinase is inefficiently activated in transfected somatic cells: evidence of interaction with the BiP chaperone
Mol. Cell. Biochem.
348
43-52
2011
Mus musculus, Rattus norvegicus, Homo sapiens (Q6UW60), Homo sapiens
brenda
Mishra, P.; Qiu, Q.; Gruslin, A.; Hidaka, Y.; Mbikay, M.; Basak, A.
In vitro regulatory effect of epididymal serpin CRES on protease activity of proprotein convertase PC4/PCSK4
Curr. Mol. Med.
12
1050-1067
2012
Mus musculus (P29121), Homo sapiens (Q6KW60), Homo sapiens
brenda
Tardif, S.; Guyonnet, B.; Cormier, N.; Cornwall, G.A.
Alteration in the processing of the ACRBP/sp32 protein and sperm head/acrosome malformations in proprotein convertase 4 (PCSK4) null mice
Mol. Hum. Reprod.
18
298-307
2012
Mus musculus (P29121)
brenda
Basak, A.; Goswami, M.; Rajkumar, A.; Mitra, T.; Majumdar, S.; OReilly, P.; Bdour, H.M.; Trudeau, V.L.; Basak, A.
Enediynyl peptides and iso-coumarinyl methyl sulfones as inhibitors of proprotein convertases PCSK8/SKI-1/S1P and PCSK4/PC4 Design, synthesis and biological evaluations
Bioorg. Med. Chem. Lett.
25
2225-2237
2015
Rattus norvegicus (Q78EH2)
brenda