Information on EC 3.4.21.75 - Furin

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.4.21.75
-
RECOMMENDED NAME
GeneOntology No.
Furin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-/- bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors
show the reaction diagram
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys, releases albumin, complement component C3 and von Willebrand factor from their respective precursors, the term -+- depicts the point of cleavage
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
141760-45-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
-
Manually annotated by BRENDA team
overview
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-
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57/BL6 mice
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Wistar
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-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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alpha1-PDX blocks cleavage of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase, probably PC7, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
show the reaction diagram
-
-
-
-
2-amino benzoyl-AEQDRNTREVFAQ-T(3-nitro-tyrosine)-A + H2O
2-amino benzoyl-AEQDRNTR + EVFAQ-T(3-nitro-tyrosine)-A
show the reaction diagram
-
furin-mediated cleavage of a fluorogenic peptide derived from hSARS-CoV spike protein
-
-
?
2-aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
show the reaction diagram
-
-
-
-
-
Abz-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIRRKRSVSHQ-EDDnp + H2O
Abz-GIRRKR + SVSHQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GIRRKR + SVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Rous sarcoma viral envelope glycoprotein
-
-
?
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GRRTRR + EAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Zaire viral envelope glycoprotein
-
-
?
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HHRQRR + SVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human A disintegrin and metalloproteinase with thrombospondin ADAM-TS 6
-
-
?
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HKREKR + QAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human bone morphogenetic protein hBMP-2
-
-
?
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRREKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 2 viral envelope glycoprotein
-
-
?
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRRQKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 3 viral envelope glycoprotein
-
-
?
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-KIRRRR + DVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-6A viral envelope glycoprotein
-
-
?
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-LKRRRR + DTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Borna disease viral envelope glycoprotein
-
-
?
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-NLRRRR + DLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-6B viral envelope glycoprotein
-
-
?
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RERRRKKR + GLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RKRSRR + QVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Sudan viral envelope glycoprotein
-
-
?
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRAKR + SPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human bone morphogenetic protein hBMP-4
-
-
?
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRDKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 4 viral envelope glycoprotein
-
-
?
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLfGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + SLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RVKRGLAY(NO2)D-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-SGRSRRAIDLQEDDnp + H2O
Abz-SGRSRR + AIDLQEDDnp
show the reaction diagram
-
-
-
-
?
Abz-SKRSRRSVSVQ-EDDnp + H2O
Abz-SKRSRR + SVSVQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SKRSRR + SVSVQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Japan beta-encephalitis viral envelope glycoprotein
-
-
?
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRHKR + FAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from measle virus Fo viral envelope glycoprotein
-
-
?
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + DVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Ivory Coast viral envelope glycoprotein
-
-
?
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + SASTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-8 viral envelope glycoprotein
-
-
?
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SSRHRR + ALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human transforming growth factor TGF-beta3
-
-
?
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-TRRFRR + SITEQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from infectious bronchitis viral envelope glycoprotein
-
-
?
Ac-AAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AAKYKR
show the reaction diagram
-
-
-
?
Ac-AARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AARYKR
show the reaction diagram
-
-
-
?
Ac-Arg-Val-Arg-Arg-4-nitroanilide + H2O
Ac-Arg-Val-Arg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Ac-KARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-KARYKR
show the reaction diagram
-
-
-
?
Ac-RA-norvaline-YKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RA-norvaline-YKR
show the reaction diagram
-
-
-
?
Ac-RAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RAKYKR
show the reaction diagram
-
-
-
?
Ac-RARYAR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYAR
show the reaction diagram
-
-
-
?
Ac-RARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYKR
show the reaction diagram
-
-
-
?
Ac-RARYRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYRR
show the reaction diagram
-
-
-
?
Ac-RYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRR
show the reaction diagram
-
-
-
?
Ac-RYRFKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRFKR
show the reaction diagram
-
-
-
?
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
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Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
-
-
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
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Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
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-
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
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-
Acetyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
show the reaction diagram
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
show the reaction diagram
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
AcRARYKK-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + AcRARYKK
show the reaction diagram
-
-
-
?
ADAMTS9 propeptide + H2O
?
show the reaction diagram
alpha-Subunit of the rat endopeptidase-24.18 + H2O
?
show the reaction diagram
-
-
-
-
-
anthrax protective antigen + H2O
?
show the reaction diagram
synthetic construct
-
-
-
-
?
anthrax protective antigen precursor + H2O
?
show the reaction diagram
-
-
-
-
?
anthrax protective antigen-83 + H2O
?
show the reaction diagram
-
-
-
-
?
anthrax protective antigen-83 + H2O
anthrax protective antigen-63 + ?
show the reaction diagram
-
-
-
-
?
avian influenza virus A hemagglutinin + H2O
?
show the reaction diagram
Boc-RVRR-4-methylcoumarin 7-amide + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-RVRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Boc-RVRR
show the reaction diagram
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
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?
Carboxybenzyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
-
-
chimeric transforming growth factor-beta1/beta2 + H2O
?
show the reaction diagram
CPA95 + H2O
?
show the reaction diagram
-
-
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
show the reaction diagram
duck carboxypeptidase D + H2O
?
show the reaction diagram
-
i.e. DCPD, duck carboxypeptidase D acts as species-specific docking receptor for the duck hepatitis B virus. No cleavage of recombinant DCPD expressed in LMH cells
-
-
?
duck hepatitis B virus large envelope pre-S protein + H2O
?
show the reaction diagram
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the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus
-
-
?
epithelial Na+ channel + H2O
?
show the reaction diagram
extracellular superoxide dismutase + H2O
?
show the reaction diagram
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
show the reaction diagram
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
show the reaction diagram
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
show the reaction diagram
G-protein-coupled receptor GPR107 + H2O
?
show the reaction diagram
glycoprotein 160 + H2O
?
show the reaction diagram
-
from HIV-1, low activity
-
-
?
gp40/15 + H2O
gp40 + gp15
show the reaction diagram
gp40/15 subtype 1e + H2O
gp40 + gp15
show the reaction diagram
hBMP-2 precursor protein + H2O
?
show the reaction diagram
-
cleavage sites are HKREKR-/-QAKH and HVRISR-/-SLHQ
-
-
?
hBMP-4 precursor protein + H2O
?
show the reaction diagram
-
cleavage sites are RRRAKR-/-SPKH and HVRISR-/-SLPQ
-
-
?
hemagglutinin + H2O
?
show the reaction diagram
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O
?
show the reaction diagram
-
hemagglutinin loop of high pathogenic avian influenza virus subtype H5 binds much more tightly into the catalytic site of furin than the hemagglutinin low pathogenic avian influenza virus subtype H3 and hemagglutinin low pathogenic avian influenza virus subtype H5 systems. The -RRRKK- insertion in the hemagglutinin high pathogenic avian influenza virus subtype H5 in particular two arginines at S4 and S6 positions helps directly to hold the hemagglutinins cleavage loop in place by forming many strong hydrogen bonds between residues of hemagglutinin and furin
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-
?
hemagglutinin low pathogenic avian influenza virus subtype H3 + H2O
?
show the reaction diagram
-
-
-
-
?
hemagglutinin low pathogenic avian influenza virus subtype H5 + H2O
?
show the reaction diagram
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-
-
-
?
heparan sulfate 6-O-endosufatase Sulf2 + H2O
?
show the reaction diagram
-
cleavage at arginine 570, located in the consensus sequence for the cleavage by furin-type proprotein convertases. The consensus sequence of the cleavage by furin and PCs is R/K-X-R/K-X-R/K-R-/-X. R, K, X, and denote arginine, lysine, any amino acid. Proteolytic processing of SulfFP2 protein by furin and furin-like proprotein convertases, and activity with Sulf2 truncation and exchange mutants, overview
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-
?
hepatitis B e antigen precursor + H2O
?
show the reaction diagram
high pathogenic H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
furin can only cleave the high pathogenic hemagglutinin. It generates most of its selectivity through interactions with subsites P1, P4, and P6, with interactions at P2 being less important and little preference at P3, P5, P7, and P8. The S1, S4, and S6 pockets are specifically designed to accommodate arginine, with lysine substitution fitting less well in different degrees
-
-
?
highly pathogenic Queretaro H5N2 hemagglutinin + H2O
?
show the reaction diagram
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only processed in the presence of heparin
-
-
?
histonin + H2O
?
show the reaction diagram
-
furin releases intact histonin monomers from F4-multimeric histonin (12-mer). Histonin has an RLKR motif at the C-terminus after which furin cleaves specifically
-
-
?
HIV-1 gp160 + H2O
?
show the reaction diagram
-
13mer and 19mer peptides digested equally well by furin at site1, showing complete processing at 5 h. 41mer and 51mer peptides are either barely or unprocessed, respectively. Product inhibition does not explain inability of furin to process the 41mer and 51mer peptides. Extended sequences require heparin for optimal processing
-
-
?
HIV-1 Tat protein + H2O
?
show the reaction diagram
human semaphorin 3F + H2O
?
show the reaction diagram
IBV spike protein + H2O
?
show the reaction diagram
-
-
-
-
?
inactive pro-MT1-MMP + H2O
active MT1-MMP + ?
show the reaction diagram
-
-
-
-
?
influenza deltaK-Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
76% processed
-
-
?
influenza Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
70% processed
-
-
?
influenza variant Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
mutations at the furin-processing site of the hemagglutinin, is less cleaved (38%) by furin as compared to the parent Fujian-like strain derived peptides
-
-
?
insulin-like growth factor-1 receptor + H2O
?
show the reaction diagram
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
lethal factor inhibitor 2 + H2O
?
show the reaction diagram
-
-
-
-
?
membrane type-1 matrix metalloproteinase + H2O
?
show the reaction diagram
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
show the reaction diagram
membrane-bound collagen XXIII + H2O
shed collagen XXIII
show the reaction diagram
-
furin is the major protease to process collagen XXIII. Processing occurs after the downstream recognition motif 94KIRTVR99, releasing the ectodomain
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
show the reaction diagram
membrane-type 1-matrix metalloproteinase + H2O
?
show the reaction diagram
-
-
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
show the reaction diagram
mouse pro-growth hormone-releasing hormone + H2O
?
show the reaction diagram
N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
nodal + H2O
?
show the reaction diagram
-
cripto interacts with the nodal pro segment and mature domain and presents uncleaved precursor to extracellular furin that is recruited through its P-domain
-
-
?
p-Glu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
PA83 + H2O
PA63
show the reaction diagram
-
-
-
-
?
parathyroid hormone-related peptide + H2O
?
show the reaction diagram
-
-
-
-
?
PC1/3 C-terminal peptide + H2O
?
show the reaction diagram
-
cleavage by furin into a peptide with an apparent molecular mass of 12.5 kDa. Cleavage of the C-terminal to the pair of Args occupying positions 627 and 628
-
-
?
PC2-S383A
?
show the reaction diagram
-
furin fully processes the PC2 mutant at the secondary site in AtT-20 cells, site is accessible to in trans cleavage
-
-
-
PCSK9 + H2O
?
show the reaction diagram
-
cleavage by furin at Arg218. Mutations R218S, F216L, and D374Y of PCSK9 associated with hypercholesterolemia result in total or partial loss of furin/PC5/6A processing at the motif RFHR21, mutant A443T shows enhanced susceptibility to furin cleavage
-
-
?
PE2 glycoprotein precursor + H2O
?
show the reaction diagram
enzyme is involved in maturation of PE2 glycoprotein of alphaviruses. Enzyme cleaves efficiently PE2 glycoprotein mutants with residues arginine, serine, phenylalanine, histidine, asparagine, or aspartic acid at the +1 position
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peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
show the reaction diagram
pERKTR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
?
show the reaction diagram
-
-
-
-
-
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methycoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methycoumarin
show the reaction diagram
-
-
-
?
POMC prohormone precursor + H2O
ACTH + alpha-MSH + beta-endorphin
show the reaction diagram
-
human pituitary may utilize the cathepsin L and prohormone convertase pathways for producing POMC-derived peptide hormones
-
-
?
precursor of transforming growth factor beta + H2O
?
show the reaction diagram
pro-ADAMTS4 + H2O
?
show the reaction diagram
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
show the reaction diagram
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
show the reaction diagram
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
show the reaction diagram
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
show the reaction diagram
-
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
show the reaction diagram
pro-hADAM-15 protein + H2O
?
show the reaction diagram
-
cleavage site is HIRRRR-/-DVVT
-
-
?
pro-hADAM-TS 4 protein + H2O
?
show the reaction diagram
-
cleavage site is RPRRAKR-/-FASL
-
-
?
pro-hADAM-TS 6 protein + H2O
?
show the reaction diagram
-
cleavage site is HHRQRR-/-SVSI
-
-
?
pro-hADAMTS-17 protein + H2O
?
show the reaction diagram
-
cleavage site is HVRKRR-/-ADPD
-
-
?
pro-hADAMTS-23 protein + H2O
?
show the reaction diagram
-
cleavage site is LKRRKR-/-AVNP
-
-
?
pro-hepcidin + H2O
active mature hepcidin
show the reaction diagram
pro-hTGF-beta1 protein + H2O
?
show the reaction diagram
-
cleavage site is NRRKKR-/-ALDA
-
-
?
pro-hTGF-beta2 protein + H2O
?
show the reaction diagram
-
cleavage site is GQRKKR-/-ALDT
-
-
?
pro-hTGF-beta3 protein + H2O
?
show the reaction diagram
-
cleavage site is SSRHRR-/-ALDT
-
-
?
pro-hTGF-beta4 protein + H2O
?
show the reaction diagram
-
cleavage site is RSRGRR-/-FSQS
-
-
?
pro-MT-MMP 1 protein + H2O
?
show the reaction diagram
-
cleavage site is NVRRKR-/-YALT
-
-
?
pro-MT-MMP 11 protein + H2O
?
show the reaction diagram
-
cleavage site is RHRQKR-/-FVLS
-
-
?
pro-MT-MMP 3 protein + H2O
?
show the reaction diagram
-
cleavage site is RNRQKR-/-FVLS
-
-
?
pro-MT-MMP 4 protein + H2O
?
show the reaction diagram
-
cleavage site is QSRRRR-/-QTPP
-
-
?
pro-MT-MMP 6 protein + H2O
?
show the reaction diagram
-
cleavage site is VRRRRR-/-YALS
-
-
?
pro-von Willebrand factor + H2O
?
show the reaction diagram
-
-
-
-
?
proaerolysin + H2O
?
show the reaction diagram
-
cleavage site is KVRRAR-/-SVDG
-
-
?
procollagen V + H2O
?
show the reaction diagram
-
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
-
-
?
proPDGF-A + H2O
PDGF-A + PGDF-A propeptide
show the reaction diagram
-
a growth factor proform
-
-
?
proPDGF-B + H2O
PDGF-B + PGDF-B propeptide
show the reaction diagram
-
a growth factor proform of 31 kDa
mature form of 17 kDa
-
?
proprotein convertase PCSK9 + H2O
?
show the reaction diagram
-
-
PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form, PCSK9 is inactivated by furin by cleavage at residue R218
-
?
Prorenin + H2O
?
show the reaction diagram
-
-
-
-
-
Protective antigen component of anthrax toxin + H2O
?
show the reaction diagram
-
cleavage at the sequence Arg-Lys-Lys-Arg
-
-
-
Protein precursor + H2O
?
show the reaction diagram
proVEGF-C + H2O
VEGF-C + VEGF-C propeptide
show the reaction diagram
-
a growth factor proform
-
-
?
Pseudomonas aeruginosa exotoxin A + H2O
?
show the reaction diagram
-
-
-
?
Pseudomonas exotoxin A + H2O
?
show the reaction diagram
Pseudomonas toxin + H2O
?
show the reaction diagram
-
cleavage site is RHRQPR-/-GWEQ
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pyr-Arg-Thr-Lys-Arg
show the reaction diagram
-
pERTKR-MCA
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamic acid-RTKR-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-RTKR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
RPTPkappa + H2O
?
show the reaction diagram
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + Arg-Thr-Lys-Arg
show the reaction diagram
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
show the reaction diagram
-
-
?
SARS coronavirus spike glycoprotein + H2O
?
show the reaction diagram
-
introduction of a prototypic furin recognition motif at R667 allows for efficient cleavage of the mutant glycoprotein
-
-
?
Shiga toxin + H2O
?
show the reaction diagram
Synthetic peptides + H2O
?
show the reaction diagram
-
based on the N-terminal sequence of human proalbumin
-
-
-
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
TACE/ADAM17 + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-RVRR-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
TGFbeta1 + H2O
?
show the reaction diagram
-
-
-
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
viral precursor protein E3E2
?
show the reaction diagram
synthetic construct
-
processes E3E2 from African Chikungunya virus strain at the HRQRR642ST site, whereas a Chikungunya virus strain of Asian origin is cleaved at site RRQRR642SI
-
-
?
Viral spike glycoproteins + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADAMTS9 propeptide + H2O
?
show the reaction diagram
-
the intact zymogen is secreted to the cell surface and is subsequently processed by furin before release into thge medium. ADAMTS9 processing is exclusively extracellular and occurs at the cell surface in cells that express high levels of furin
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
show the reaction diagram
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
show the reaction diagram
-
-
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
show the reaction diagram
G-protein-coupled receptor GPR107 + H2O
?
show the reaction diagram
-
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
HIV-1 Tat protein + H2O
?
show the reaction diagram
-
furin processing is a likely mechanism for inactivating extracellular HIV-1 Tat protein. Furin cleavage reduces the transactivation activity of tat without preventing Tat uptake and entry into the nucleus
-
-
?
human semaphorin 3F + H2O
?
show the reaction diagram
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
IBV spike protein + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor-1 receptor + H2O
?
show the reaction diagram
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
show the reaction diagram
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
show the reaction diagram
-
furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP at the surface of cancer cells. Furin and related PCs are the essential components of the specialized cellular machinery that controls the levels of the functionally active, mature, MT1-MMP enzyme on the cell surface to continually support the potency of pericellular proteolysis
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
show the reaction diagram
-
production of mature growth hormone-releasing hormone from pro-growth hormone-releasing hormone is a stepwise process mediated predomionantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus
-
-
?
precursor of transforming growth factor beta + H2O
?
show the reaction diagram
pro-ADAMTS4 + H2O
?
show the reaction diagram
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
show the reaction diagram
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
show the reaction diagram
-
pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4
-
-
?
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
show the reaction diagram
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
show the reaction diagram
-
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
show the reaction diagram
-
CD109 is produced as a 205 kDa glycoprotein, which is then processed in the Golgi apparatus into 180 kDa and 25 kDa proteins by furin
-
-
?
proprotein convertase PCSK9 + H2O
?
show the reaction diagram
-
-
PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CoCl2
-
partially restores activity after EDTA treatment
Mg2+
-
selective activation of furin by Mg2+ ions as a result of cooperativity between furin subsites. Furin hydrolysis of peptides from measles virus fusion protein Fo and from Asian avian influenza A, H5N1, is activated between 60- and 80-fold by MgCl2. Both the pH profile of furin and its intrinsic fluorescence are modified by Mg2+ ions, which bind to furin with a Kd value of 1.1 mM
MnCl2
-
partially restores activity after EDTA treatment
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
synthetic construct
-
-
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
synthetic construct
-
-
(D-Arg)6 amide
-
IC50: 0.3 mM
(D-Arg)9 amide
-
IC50: 0.01 mM
(D-Arg)9-amide
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
-
competitive inhibitor
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
-
competitive inhibitor
1,10-phenanthroline
-
-
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(azeno)-4,10-benzodiazacyclopentadecine
-
12% inhibition at 0.1 mM
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
10% inhibition at 0.1 mM
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
synthetic construct
-
-
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
synthetic construct
-
-
11-amino-undecanoyl-RARRRKKRT
-
-
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
noncompetitive inhibitor
2-Bromopalmitate
-
inhibits nodal processing by Flag-tagged furin
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
-
-
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
-
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
-
competitive inhibitor
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
-
competitive inhibitor
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
-
4,6-bis(4-guanidinylphenoxy)-1-guanidinyl-3-(4-guanidinylphenylamino)cyclohexane
-
-
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
-
-
4-(2-aminoethyl)benzenesulphonyl fluoride
-
-
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
-
4-Hydroxycoumarin
-
-
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
-
-
8,11,22,25-tetrabenzyl-5,6,13,14,19,20,27,28-octadehydro-7,8,9,10,11,12,21,22,23,24,25,26-dodecahydrodibenzo[h,t][1,4,13,16]tetraazacyclotetracosine
-
-
8-amino-octanoyl-RARRRKKRT
-
-
a1-PDX
-
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
-
Ac-HHKRRR-NH2
-
-
Ac-HRKRRR-NH2
-
-
Ac-KHKRRR-NH2
-
-
Ac-KRKRRR-NH2
-
-
Ac-LLRVKR
-
-
Ac-LLRVKR-NH2
-
-
Ac-MHKRRR-NH2
-
-
Ac-MRKRRR-NH2
-
-
Ac-RHKRRR-NH2
-
-
Ac-RRKRRR-NH2
-
-
acetyl-RARRRKKRT
-
-
acetyl-Val-Arg-4-amidinobenzylamide
-
-
AEBSF
-
partially inhibits ectodomain shedding by 45%
alpha1-Antichymotrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antichymotrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
Alpha1-antitrypsin
alpha1-antitrypsin M352R
-
i.e. alpha1-PDX. Engineering of alpha1-antitrypsin variants, containing Arg at the P1 site within the reactive site loop, with improved specificity for the proprotein convertase furin using site-directed random mutagenesis, screening, overview. The engineered a1-antitrypsin variant carrying the RXXR consensus motif for furin within its reactive site loop. Furin-mediated maturation of bone morphogenetic protein-4 is completely inhibited by ectopic expression of the AVNR variant
-
alpha1-antitrypsin Portland variant
alpha1-AT
-
a naturally occurring serpin and a potent inhibitor of furin
-
alpha1-PDX
alpha1-PDX inhibitor
-
-
-
antipain
antithrombin
antithrombin/heparin
-
not: antithrombin alone
-
Arg-oxime
beta-Ala-TPRARRRKKRT-amide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
-
brefeldin A
Chloroquine
synthetic construct
-
weakly affects proprotein convertase activity and E3E2 processing. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
cholyl-RARRRKKRT
-
-
chymostatin
Cu(2,2':6,2''-terpyridine)Cl2
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.005 mM
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(di-[2-picolyl]amine)Cl2
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
D-poly-Arg-NH2
-
-
D-Tyr-Ala-Lys-Arg-CH2Cl
-
-
Dec-RVKR-CMK
-
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
decanoyl-RVKR-chloromethyl ketone
decanoyl-RVKR-chloromethylketone
-
the furin inhibitor reduces DHBV infection of primary duck hepatocytes
decanoyl-RVRR-chloromethyl ketone
-
-
diisopropyl fluorophosphate
dithiothreitol
-
-
DYYHFWHRGVKRSLSPHRPRHSR
-
i.e. profurin 39-62
E-64
-
minimal inhibition of ectodomain shedding
Eglin c
eglin c Arg replaced with Asp at P3
-
-
-
eglin c mutant D42R
-
-
-
eglin c mutant L45R
-
-
-
eglin variant M1 RVTR
-
-
-
eglin variant M2 RVKR
-
-
-
eglin variant M3 RVTRDERY
-
-
-
eglin variant M4 RVTRDRRY
-
-
-
eglin variant M5 RVTRDLDY
-
-
-
eglin variant M6 RVTRDLRR
-
-
-
eglin variant M7 RVTRDLRE
-
-
-
eglin variant M8 RVTRDARY
-
-
-
furin inhibitor I
-
-
-
furin-Eda peptide acyclic
-
synthesis, overview. Designed a potent furin inhibitor that contains a highly reactive beta-turn inducing and radical generating enediynyl amino acid moiety, which is inserted between P1 and P19 residues of hfurin98-112 peptide, derived from the primary cleavage site of furin's own prodomain. The inhibitor displays a predominantly beta-turn structure. The inhibitor protects furin protein from self degradation
furin-Eda peptide cyclic
-
synthesis, overview
Glu-Gly-Arg-chloromethylketone
-
poor inhibitor
hepta-L-arginine
-
-
hexa-D-arginine
hexa-L-arginine
-
-
hfurin25-107
-
i.e. furin prodomain protein, competitive inhibitor, blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview. Secondary structure of furin prodomain protein, overview
-
histone H1
-
efficiently blocks furin-dependent pro-von Willebrand factor processing in a dose-dependent manner, interaction between histone H1 and furin mainly takes place on the cell surface. H1 may be involved in extracellular and/or intracellular furin regulation
-
human proteinase inhibitor 8
-
-
-
inter-alpha-inhibitor protein IalphaIp
-
blocks furin activity in vitro and provides significant protection against cytotoxocity for murine peritoneal macrophages exposed to up to 500 ng/ml anthrax lethal toxin
-
iodoacetamide
L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
-
lethal factor inhibitor 2
-
IC50: 0.002 mM
-
Leupeptin
LLRVKR
-
-
LLRVKR-NH2
-
-
Lys-Arg chloromethyl ketone
m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
-
a competitive, noncovalent inhibitor, binding structure, overview
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
noncompetitive inhibitor
MnCl2
-
-
monensin
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
competitive inhibitor
N-(benzo[d][1,3]dioxol-5-yl)-1,2,3,4-tetrahydroacridin-9-amine
-
competitive inhibitor
N-(thiazol-2-yl)-4-(5-((2,4,6-trioxotetrahydropyrimidin-5(6H)-ylidene)methyl)furan-2-yl)benzenesulfonamide
-
competitive inhibitor
N-tosyl-L-lysine chloromethyl ketone
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
-
N-[5-guanidino-2,4-bis-(4-guanidino-phenoxy)-cyclohexyl]-guanidine
-
-
N-[5-guanidino-2,4-bis-(5-guanidino-pyridin-2-yloxy)-cyclohexyl]-guanidine
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
-
NEM
-
moderately
nona-L-arginine
-
most potent inhibitor
octa-L-arginine
-
-
Octapeptidyl chloromethane inhibitor
-
potent irreversible inhibitor
-
p-chloromercuribenzenesulfonic acid
-
-
p-hydroxymercuribenzoate
PenLen (rSAAS-(221-2546))
-
neuroendocrine protein proSAAS-derived peptide
penta-L-arginine
-
-
Peptidyl chloroalkyl ketones
Phe-Pro-Arg-chloromethylketone
-
poor inhibitor
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
-
a competitive, noncovalent inhibitor, binding structure, overview
phenylmethanesulfonyl fluoride
phenylmethylsulfonyl fluoride
-
-
Pro-Gly-Lys-Arg-CH2Cl
-
-
pro-hepcidin
-
hydrolytic activity of membrane furin against the fluorescent substrate Boc-RVRR-7-amino-4-methyl-coumarin is reduced by approximately 50% in presence of 2 micromol pro-hepcidin and completely abolished in presence of 5 micromol pro-hepcidin
-
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
-
profurin 48-62 VTKRSLSPHRPRHSR
-
peptide derived from proprotein convertase 1/3
profurin 54-62 SPHRPRHSR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62 NHYLFKHKSHPRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-62 RRSRR SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
peptide derived from proprotein convertase 1/3
-
proPC1/3 55-62 SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62/A SALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 74-83 QQYEKERSKR
-
peptide derived from proprotein convertase 1/3
RARRRKKRT
-
-
SAAS-(235-244)
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P1'A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P2'A
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P3A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P3AP5A
-
neuroendocrine protein proSAAS-derived peptide
tetra-L-arginine
-
-
tosyl-Lys chloromethyl ketone
TPQRARRRKKRF
-
-
TPQRARRRKKRT
-
-
TPQRARRRKKRW
-
-
TPQRARRRKKRY
-
-
TPRARRRKKRG
-
-
TPRARRRKKRI
-
-
TPRARRRKKRT
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
[Cu(2,2':6,2''-terpyridine)Cl2] (OCl4)
-
IC50: 0.0069 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
parasite expresses a Ca2+ dependent, furin-like protease activity
heparin
-
optimizies furin processing of substrates containing multibasic residues at strategic P-positions within the cleavage site. Incubation of Fujian-like peptides with heparin results in ca. 2- to 3fold enhancement of processing. Heparin at a concentration of 0.02 mM dramatically enhances processing of the basic highly pathogenic Queretaro H5N2 peptide, albeit at neutral pH. It has no effect on processing of low pathogenic Mexico H5N2 peptide
Tumor necrosis factor alpha
-
-
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
0.0038
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
-
-
0.00039 - 0.00042
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00021 - 0.0012
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0003 - 0.0032
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00038 - 0.0027
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0002 - 0.00022
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00028 - 0.00037
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00005 - 0.0001
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00028 - 0.0052
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00033 - 0.0014
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.0002 - 0.0065
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0012 - 0.0122
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00039 - 0.00041
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00041 - 0.00049
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00015 - 0.00045
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00014 - 0.005
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00086 - 0.00416
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.0123
Ac-Arg-Val-Arg-Arg-4-nitroanilide
-
-
0.001
Ac-norleucineYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.016
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.008
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.345
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
-
-
0.0015
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.005
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.106
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.028
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00194
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37C
0.0071
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0009
AcRARYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.0008
AcRYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.0006
AcRYRFKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.019
Boc-RVRR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.01
Boc-RVRR-7-amido-4-methyl-coumarin
-
-
0.029
Boc-RVRR-7-amido-4-methylcoumarin
-
0.035
DSSARIRRNAKG
-
pH 7.0, 37C
0.0059
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate
-
-
0.00007 - 0.0013
hBMP-2 precursor protein
0.0014 - 0.0015
hBMP-4 precursor protein
0.00124
pERKTR-7-amido-4-methylcoumarin
-
0.005
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
-
0.0002
pro-hADAM-15 protein
-
pH 7.0, 37C
-
0.00055
pro-hADAM-TS 4 protein
-
pH 7.0, 37C
-
0.0004
pro-hADAM-TS 6 protein
-
pH 7.0, 37C
-
0.0091
pro-hADAMTS-17 protein
-
pH 7.0, 37C
-
0.0067
pro-hADAMTS-23 protein
-
pH 7.0, 37C
-
0.0001
pro-hTGF-best1 protein, pro-hTGF-beta2 protein
-
pH 7.0, 37C
-
0.00014
pro-hTGF-beta3 protein
-
pH 7.0, 37C
-
0.0022
pro-hTGF-beta4 protein
-
pH 7.0, 37C
-
0.00015
pro-MT-MMP 1 protein
-
pH 7.0, 37C
-
0.00011
pro-MT-MMP 11 protein, pro-MT-MMP 3 protein
-
pH 7.0, 37C
-
0.00045
pro-MT-MMP 4 protein
-
pH 7.0, 37C
-
0.00037
pro-MT-MMP 6 protein
-
pH 7.0, 37C
-
0.00064
proaerolysin
-
pH 7.0, 37C
-
0.002
protective antigen
-
(-Arg-Lys-Lys-Arg-Ser-Thr-Ser-Ala-Gly-)
-
0.0118
Pseudomonas toxin
-
pH 7.0, 37C
-
0.0032
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
pH 7.5, 37C
0.0026
Shiga toxin
-
pH 7.0, 37C
-
0.01517
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.0156
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
-
-
0.000036 - 0.000122
viral precursor protein E3E2
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.3
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
Mammalia
-
-
29.6 - 30.3
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
3.6 - 4.2
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
28.9 - 39.5
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
6.3 - 6.9
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
7.6 - 12.2
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
9.2 - 14.9
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
0.6 - 3.1
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
0.61 - 6.7
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
2 - 3.5
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
2.6 - 12.3
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
8.4 - 11.3
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
5.3 - 8.7
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
12.2 - 14.6
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
5
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
2.4 - 6.7
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
1 - 7.6
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
10.5 - 18.3
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
0.21 - 2.4
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
9.2 - 9.9
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
10 - 11.1
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
5.6 - 7.1
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
16.4 - 19.8
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
50
Ac-norleucineYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
0.000934
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.02
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.0507
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00111
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.0403
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00159
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00088
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.7
acetyl-RVRR-4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.0, 37C
0.00135
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-4-methylcoumarin 7-amide
Homo sapiens
-
-
250
AcRARYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
193
AcRYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
200
AcRYRFKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
21
Boc-RVRR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
0.003
Boc-RVRR-7-amido-4-methylcoumarin
Trichoplusia ni
Q5DNW1
-
3 - 3.6
hBMP-2 precursor protein
3.6 - 5.6
hBMP-4 precursor protein
0.008
pERKTR-7-amido-4-methylcoumarin
Trichoplusia ni
Q5DNW1
-
5.5
pro-hADAM-15 protein
Homo sapiens
-
pH 7.0, 37C
-
4.5
pro-hADAM-TS 4 protein
Homo sapiens
-
pH 7.0, 37C
-
40
pro-hADAM-TS 6 protein
Homo sapiens
-
pH 7.0, 37C
-
1
pro-hADAMTS-17 protein, pro-hADAMTS-23 protein
Homo sapiens
-
pH 7.0, 37C
-
1.5
pro-hTGF-beta1 protein
Homo sapiens
-
pH 7.0, 37C
-
3.4
pro-hTGF-beta2 protein
Homo sapiens
-
pH 7.0, 37C
-
8.4
pro-hTGF-beta3 protein
Homo sapiens
-
pH 7.0, 37C
-
1.2
pro-hTGF-beta4 protein
Homo sapiens
-
pH 7.0, 37C
-
2.4
pro-MT-MMP 1 protein
Homo sapiens
-
pH 7.0, 37C
-
1.3
pro-MT-MMP 11 protein
Homo sapiens
-
pH 7.0, 37C