Information on EC 3.4.21.75 - Furin and Organism(s) Homo sapiens

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Homo sapiens


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The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.75
-
RECOMMENDED NAME
GeneOntology No.
Furin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
141760-45-4
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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cellular furin content might be a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection
physiological function
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
-
-
-
-
?
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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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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Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
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Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
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Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
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
-
-
-
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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
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
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
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
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 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
-
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
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
-
-
-
?
CPA95 + H2O
?
show the reaction diagram
-
-
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
show the reaction diagram
epithelial Na+ channel + H2O
?
show the reaction diagram
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
extracellular superoxide dismutase + H2O
?
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
-
cleaves recombinant Cryptosporidium parvum and Cryptosporidium hominis gp40/15. Putative furin cleavage site RSRR
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
show the reaction diagram
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
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
hepatitis B e antigen precursor + H2O
?
show the reaction diagram
-
-
-
-
?
highly pathogenic Queretaro H5N2 hemagglutinin + H2O
?
show the reaction diagram
-
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
-
-
?
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
-
-
?
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-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
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
-
-
-
-
?
p-Glu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
PA83 + H2O
PA63
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
-
-
?
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-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-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
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
-
-
?
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-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
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
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
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
-
?
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 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-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
-
-
-
-
?
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
-
furin is required for S1 processing of RPTPkappa in the secretory pathway. Purified furin cleaves RPTPkappa within the membrane-proximal fibronectin type III domain at the sequence RTKR
-
-
?
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
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
-
-
-
-
?
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
-
-
-
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
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
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
show the reaction diagram
-
i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
-
?
G-protein-coupled receptor GPR107 + H2O
?
show the reaction diagram
-
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
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
-
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
1,2,12,13-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
11-amino-undecanoyl-RARRRKKRT
-
-
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
noncompetitive inhibitor
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-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
-
-
-
acetyl-RARRRKKRT
-
-
alpha1-Aantichymotrypsin
-
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
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-PDX
-
-
-
alpha1-PDX inhibitor
-
-
-
antipain
-
-
Arg-oxime
-
-
beta-Ala-TPRARRRKKRT-amide
-
-
brefeldin A
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
CDTA
-
-
cholyl-RARRRKKRT
-
-
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
Cu2+
-
IC50: 0.014 mM
D-poly-Arg-NH2
-
-
Dec-RVKR-CMK
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
decanoyl-RVKR-chloromethyl ketone
decanoyl-RVRR-chloromethyl ketone
-
-
diisopropyl fluorophosphate
-
-
dithiothreitol
-
-
Eglin c
-
engineered variants
EGTA
-
-
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
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
-
Hg2+
-
-
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
-
-
leupeptin
-
moderately
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-[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
-
-
NaCl
-
600 mM
Octapeptidyl chloromethane inhibitor
-
potent irreversible inhibitor
-
p-hydroxymercuribenzoate
-
-
PenLen (rSAAS-(221-2546))
-
neuroendocrine protein proSAAS-derived peptide
Peptidyl chloroalkyl ketones
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
-
a competitive, noncovalent inhibitor, binding structure, overview
phenylmethanesulfonyl fluoride
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
siRNA
-
-
-
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
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
-
-
0.00039 - 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
0.035
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
-
0.005
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
-
0.0118
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
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
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
-
pH 7.0, 37C
0.000934
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.02
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0507
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
-
-
0.00111
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0403
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00159
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00088
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.7
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37C
0.00135
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-4-methylcoumarin 7-amide
-
-
250
AcRARYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
193
AcRYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
200
AcRYRFKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
21
Boc-RVRR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
3 - 3.6
hBMP-2 precursor protein
-
3.6 - 5.6
hBMP-4 precursor protein
-
5.5
pro-hADAM-15 protein
-
pH 7.0, 37C
-
4.5
pro-hADAM-TS 4 protein
-
pH 7.0, 37C
-
40
pro-hADAM-TS 6 protein
-
pH 7.0, 37C
-
1
pro-hADAMTS-17 protein, pro-hADAMTS-23 protein
-
pH 7.0, 37C
-
1.5
pro-hTGF-beta1 protein
-
pH 7.0, 37C
-
3.4
pro-hTGF-beta2 protein
-
pH 7.0, 37C
-
8.4
pro-hTGF-beta3 protein
-
pH 7.0, 37C
-
1.2
pro-hTGF-beta4 protein
-
pH 7.0, 37C
-
2.4
pro-MT-MMP 1 protein
-
pH 7.0, 37C
-
1.3
pro-MT-MMP 11 protein
-
pH 7.0, 37C
-
0.5
pro-MT-MMP 3 protein
-
pH 7.0, 37C
-
5.5
pro-MT-MMP 4 protein
-
pH 7.0, 37C
-
0.84
pro-MT-MMP 6 protein
-
pH 7.0, 37C
-
12.2
proaerolysin
-
pH 7.0, 37C
-
0.54
Pseudomonas toxin
-
pH 7.0, 37C
-
16
Shiga toxin
-
pH 7.0, 37C
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70550 - 77100
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
3085 - 20190
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
9031 - 116100
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
2354 - 17730
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
38300 - 55640
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
32430 - 40270
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
6000 - 53450
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
1303 - 2184
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
1470 - 10610
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
1555 - 123000
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
1291 - 56300
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
710 - 4383
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
29660 - 37510
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
322
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
797 - 30500
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
606 - 33040
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
25360 - 37350
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
559 - 33860
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
20470 - 66000
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
1992 - 76230
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
1707 - 6488
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
28360 - 37360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
361
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37C
2331 - 50710
hBMP-2 precursor protein
-
2649 - 3700
hBMP-4 precursor protein
-
27600
pro-hADAM-15 protein
-
pH 7.0, 37C
-
8127
pro-hADAM-TS 4 protein
-
pH 7.0, 37C
-
100000
pro-hADAM-TS 6 protein
-
pH 7.0, 37C
-
109
pro-hADAMTS-17 protein
-
pH 7.0, 37C
-
143
pro-hADAMTS-23 protein
-
pH 7.0, 37C
-
14700
pro-hTGF-beta1 protein
-
pH 7.0, 37C
-
34200
pro-hTGF-beta2 protein
-
pH 7.0, 37C
-
60140
pro-hTGF-beta3 protein
-
pH 7.0, 37C
-
534
pro-hTGF-beta4 protein
-
pH 7.0, 37C
-
15800
pro-MT-MMP 1 protein
-
pH 7.0, 37C
-
11450
pro-MT-MMP 11 protein
-
pH 7.0, 37C
-
4545
pro-MT-MMP 3 protein
-
pH 7.0, 37C
-
12670
pro-MT-MMP 4 protein
-
pH 7.0, 37C
-
2240
pro-MT-MMP 6 protein
-
pH 7.0, 37C
-
20670
proaerolysin
-
pH 7.0, 37C
-
45
Pseudomonas toxin
-
pH 7.0, 37C
-
6134
Shiga toxin
-
pH 7.0, 37C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000013
(D-Arg)9-amide
-
-
0.0000089
11-amino-undecanoyl-RARRRKKRT
-
pH 7.5, 37C
0.012
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
with CPA95 as substrate/with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.0033
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.00104
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.1851
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0783
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.022
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0208
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00605
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0188
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
2
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
1.3
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
7.3
4-Hydroxycoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0000083
8-amino-octanoyl-RARRRKKRT
-
pH 7.5, 37C
0.0000065
acetyl-RARRRKKRT
-
pH 7.5, 37C
0.0000152
cholyl-RARRRKKRT
-
pH 7.5, 37C
0.000156
hfurin25-107
-
pH 7.4, 37C, versus N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide
-
0.0000000538
human proteinase inhibitor 8
-
pH 7.5, 37C
-
0.1452
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0118
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00058
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
-
pH 7.0,22C
0.00046
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
pH 7.0,22C
0.00104
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
pH 7.0,22C
0.00113
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
-
pH 7.0,22C
0.00302
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000063
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00749
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000078
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00000081
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000553
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00107
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00971
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000053
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00132
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00273
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000627
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00143
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000001
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000016
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000033
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
pH 7.0, temperature not specified in the publication
0.0193
PenLen (rSAAS-(221-246))
-
pH 7.4, 37C
-
0.0009
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
pH 7.0, 25C
0.0028
profurin 48-62 VTKRSLSPHRPRHSR
-
pH 7.0, 25C
0.023
profurin 54-62 SPHRPRHSR
-
pH 7.0, 25C
0.0007 - 0.0154
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
0.0012
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
pH 7.0, 25C
0.0023
proPC1/3 50-62 RRSRR SALHITKR
-
pH 7.0, 25C
0.0048
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
pH 7.0, 25C
-
0.0316
proPC1/3 55-62 SALHITKR
-
pH 7.0, 25C
0.013
proPC1/3 55-62/A SALAITKR
-
pH 7.0, 25C
0.0475
proPC1/3 74-83 QQYEKERSKR
-
pH 7.0, 25C, competitive inhibition
0.000008
RARRRKKRT
-
pH 7.5, 37C
0.000261
SAAS-(235-244)
-
pH 7.4, 37C
0.0394
SAAS-(235-246)
-
pH 7.4, 37C
-
0.00128
SAAS-(235-246)P1'A
-
pH 7.4, 37
0.0044
SAAS-(235-246)P2'A
-
pH 7.4, 37C
-
0.092
SAAS-(235-246)P3A
-
pH 7.4, 37C
0.000038
TPQRARRRKKRF
-
-
0.000033
TPQRARRRKKRT
-
-
0.000034
TPQRARRRKKRW
-
-
0.000047
TPQRARRRKKRY
-
-
0.000057
TPRARRRKKRG
-
-
0.00003
TPRARRRKKRI
-
-
0.000023
TPRARRRKKRT
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
(D-Arg)9-amide
Homo sapiens;
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
0.102
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.084
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.007
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
Homo sapiens;
-
with CPA95 as substrate/with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.025
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
Homo sapiens;
-
with CPA95 as substrate
0.055
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
Homo sapiens;
-
with CPA95 as substrate
0.004
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
Homo sapiens;
-
with CPA95 as substrate
0.02
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
Homo sapiens;
-
with CPA95 as substrate
0.051
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.137
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.0000142
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
Homo sapiens;
-
-
0.0000105
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
Homo sapiens;
-
-
0.028
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.00016 - 0.000192
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
0.000023
beta-Ala-TPRARRRKKRT-amide
Homo sapiens;
-
pH 7.5, 37C
0.0077
Cu(2,2':6,2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0072
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0051
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.014
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.038
Cu(di-[2-picolyl]amine)Cl2
Homo sapiens;
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.014
Cu2+
Homo sapiens;
-
IC50: 0.014 mM
0.00004 - 0.000193
furin-Eda peptide acyclic
0.000193
furin-Eda peptide cyclic
Homo sapiens;
-
versus substrate fluorogenic peptide derived from hSARS-CoV spike protein
0.159
N-(benzo[d][1,3]dioxol-5-yl)-1,2,3,4-tetrahydroacridin-9-amine
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.011
N-(thiazol-2-yl)-4-(5-((2,4,6-trioxotetrahydropyrimidin-5(6H)-ylidene)methyl)furan-2-yl)benzenesulfonamide
Homo sapiens;
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.009
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.009
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens;
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.021
Zn2+
Homo sapiens;
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0069
[Cu(2,2':6,2''-terpyridine)Cl2] (OCl4)
Homo sapiens;
-
IC50: 0.0069 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
-
purified recombinant enzyme, pH 7.0, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
acetyl-Arg-Ser-Lys-Arg-4-methylcoumaryl 7-amide
7 - 7.5
-
-
7.4
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
-
5: about 35% of activity maximum, 6.5: about 15% of activity maximum, mouse, acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
6 - 7.5
-
influenza deltaK-Fujian-like H5N1 peptide is the best furin substrate between pH 6-7.5. At pH 6, all Fujian-like peptides are cleaved with lower kinetics as compared to pH 7.5. Low pathogenic Mexico H5N2 peptide and highly pathogenic Queretaro H5N2 peptide are not processed by furin at either pH 7.5 or 6
6 - 8
-
pH 6.0: about 70% of maximal activity, pH 8.0: about 65% of maximal activity
6 - 8.5
-
more than 50% of activity maximum at pH 6.0 and 8.5
additional information
-
pH-profiles of furin activity in the presence and absence of salts, e.g. KCl. The pK1 values for the pH-profiles of hydrolysis of all four substrates in the presence of KCl are lower than those in its absence
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
extravillous cells
Manually annotated by BRENDA team
-
expresses PC1/3 and PC2
Manually annotated by BRENDA team
-
proprotein convertase furin is highly expressed in syncytial trophoblast in the first trimester human placentas, and expression of furin in the syncytiotrophoblast is significantly lower in the placentas from pre-eclamptic patients as compared with their gestational age-matched control placentas
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
furin-propeptide complex is restricted to the endoplasmic reticulum by a PACS-2- and COPI-dependent mechanism. His69 is a pH sensor that allows enzyme activation following transport of the furin-propeptide complex from the endoplasmic reticulum to the mildly acidic TGN/endosomal system
Manually annotated by BRENDA team
-
cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
x * 55000, soluble furin, SDS-PAGE
additional information
-
x * 60000-65000, Western blot analysis, PC1/3 and PC2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 55000, soluble furin, SDS-PAGE
additional information
-
secondary structure of furin prodomain protein, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with inhibitors m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine or phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, mixing of 7.5 mg/ml enzyme with 0.290 mM m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine and 3 mM phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, respectively, and 50 mM Tris, pH 8.5, 2.8 M sodium formate and 0.015 mM Cymal-7, at 30C, displacement of the highly potent inhibitor m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine by competitive soaking with excessive amounts of the less potent phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a positively-charged Lys residue replacing His43 in the 16-49 fragment imparts stability to the super-secondary structure of the furin prodomain at both acidic and neutral pH
678743
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 26% loss of activity of furin mutant hFUR713t, 21% loss of activity of soluble furin after 3 weeks, optimal conditions of conservation are at 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by metal-chelating chromatography
-
by Ni2+ affinity chromatography
-
partially, recombinant hfurin
-
recombinant enzyme 300fold from HEK-293 cells by metal affinity chromatography, inhibitor based affinity chromatography, and gel filtration
-
recombinant enzyme mutant R466G/K468G from HEK-293T cells
-
recombinant furin from the stably transfected Sf9 insect cells
-
recombinant Her2-antigen e23sFv-TD-tBID from Escherichia coli strain M15
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BSC40 cells infected with soluble furin
-
CHO cell lines stably expressing Tac-furin chimeric protein (extracellular/transmembrane domain of the interleukin-2 receptor alpha-chain (Tac) and the cytoplasmic domain of furin)
-
expressed in CHO cells
-
expressed in Sf9 cells using baculovirus expression system
-
expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
expression of Her2-antigen e23sFv-TD-tBID in Escherichia coli strain M15
-
full-length epitope-tagged furin constructs or mutants expressed in A7 cells or BSC-40 cells
-
full-length furin prodomain overexpressed in Escherichia coli strain BL21 (DE3)
-
furin and pro-von Willebrand factor co-expressed in BHK21 cells. cDNA of furin subcloned into the pcDNA3/VSV expression vector between the EcoRI and XbaI sites. HeLa cells transiently transfected with pCMV-furin, pCDNA3-furin-VSV or pSVHVWF1.1
-
furin expression in CHO cells, COS-7 cells, furin-deficient FD11 cells, and furin-overexpressing cells
-
furin mutant and wild-type constructs transiently transfected into HEK-293 cells
-
furin overexpressed from vaccinia virus
-
furin precursor cDNA transferred to pcDNA3.1-. Co-expression of furin-site-containing spike glycoprotein with furin cDNA in FD11 cells or CHO cells
-
HEK-293 cells transiently cotransfected with cDNA encoding V5-tagged wild-type PCSK9 and furin
-
HepG2 cells transiently transfected with furin luciferase reporter constructs pGL2-P1, pGL2-P1A and pGL2-P1B
-
human furin cDNA transfected to Huh-7 cells, HepG-2 cells and HEK-293 cells
-
LoVo cells stably expressing furin. Furin cleavage-site mutant (LNTR) transfected into COS-7 cells
-
LoVo cells transfected with vector pSVLFur encoding furin
-
MDA-MB-231 breast cancer cells stably transfected with a vector containing furin prosegment
-
mutants expressed in Sf9 cells. Mutant constructs transiently transfected in LoVo cells
-
plasmid pEFGRAPfurin expressed in CHO cells
-
recombinant expression in HEK-293 cells
-
recombinant expression of enzyme mutant R466G/K468G in HEK-293T cells
-
recombinant furin prepared in the S2 Drosophila expression system
-
recombinant hfurin from the sectreted culture media of somatomammotroph GH4C1 cells following infection with respective cDNA encoding vaccinia viruses
-
recombinant soluble C-terminus truncated furin expressed in Sf9 insect cells
-
transient expression of the enzyme in HEK-293 cells, co-expression of inhibitor mutant alpha1-antitrypsin M352R
-
vector pcDNA3-furin expressed in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cytokine transforming growth factor TGF-beta stimulates furin mRNA expression in HepG2 cells
-
forskolin induces the enzyme expression in choriocarcinoma cells
-
furin expression is detected in all rhabdomyosarcoma cell lines tested at high levels, while myoblasts and fibroblasts show low levels of furin transcripts
-
in heaptitis C virus-infected cells, furin expression is upregulated about 3fold
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D153A
-
inactive furin mutant, fails to up-regulate interferon gamma protein
D153N
-
is catalytically inert, is efficiently synthesized but inefficiently processed and secreted and therefore is difficult to be purified. Is incapable of self-activation, is less active than the wild-type
D4K
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G5
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G6
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H6
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H66L
-
profurin mutant, shows no measurable effect on propeptide excision relative to the control (65% mature furin). No effect on the pH-triggered activation and propeptide release or on the trypsin-mediated unmasking of furin
H69K
-
profurin mutant, 80% reduced efficiency of propeptide excision, fails to be activated by acidic pH or trypsinolysis
H69L
-
profurin mutant, 70% reduced efficiency of propeptide excision. Completely blocked ability of acid pH to trigger furin activation and propeptide cleavage but shows no effect on the trypsin-mediated activation step. Propeptide fails to dissociate from mature furin
K117P
-
mutation does not affect the efficiency of autocatalytic processing and the resulting secretory mutants are capable of prodomain processing at the primary cleavage site Arg-Thr-Lys-Arg107-Asp108. Is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
K74G/R75G
-
secondary cleavage sites are inactivated, is incapable of self-activation
K74G/R75G/R107G
-
is incapable of self-activation
K74G/R75G/R89G
-
is incapable of self-activation
K74G/R75G/R89G/R107G
-
is incapable of self-activation
R107G
-
primary cleavage sites are inactivated, is incapable of self-activation
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
R75A
-
profurin mutant, substitution at the P1 position of the internal cleavage site, which blocks profurin activation but not propeptide excision or endoplasmic reticulum export of the furin-propeptide complex. No effect on the folding of the catalytic domain but blocked sensitivity of the furin-propeptide complex to acid pH
R89G
-
efficiency of self-activation of the mutant in which the tertiary cleavage site (Arg-Leu-Gln-Arg89Q-Glu90) is inactivated, is significantly reduced compared to that of wild-type furin
R89G/R107G
-
is incapable of self-activation
additional information