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Information on EC 3.4.21.75 - Furin
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3.4.21.75 FurinSpecify your search results
Word Map
- 3.4.21.75
- proproteins
- sars-cov-2
- covid-19
- metalloproteinase
- ectodomain
- spike
- endoprotease
- coronavirus
- viruses
-
trans-golgi
-
disintegrin
- adam17
- ace2
- pandemic
- tmprss2
- neuropeptides
- endosomes
-
neuroendocrine
-
endoproteolytic
- propeptide
- proinsulin
- zymogen
- prodomain
- mt1-mmp
- virion
- anthrax
- subtilisins
- proglucagon
- proopiomelanocortin
-
exotoxin
-
uncleaved
- alpha1-antitrypsin
- prorenin
-
baffs
- portland
- betacoronavirus
- prostasin
-
secretogranin
-
alpha-amidating
-
juxtamembrane
- pharmacology
-
sds-stable
- medicine
-
corticotrophs
-
polybasic
- prosegment
-
monobasic
- drug development
- industry
- mers-cov
- pcsk9
- paramyxoviruses
-
membrane-type
-
subtilase
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
furin, sheddase, prohormone convertase, furin a, furin protease, proconvertase, subtilisin-like proprotein convertase, furin-like protease, furin convertase, kpc-1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dibasic processing enzyme
-
-
-
-
furin
furin-like protease
PACE
Paired basic amino acid cleaving enzyme
-
-
-
-
Paired basic amino acid converting enzyme
-
-
-
-
Paired basic amino acid residue cleaving enzyme
-
-
-
-
PC1
PCSK3
prohormone convertase
prohormone convertase 1
Proprotein convertase
Serine proteinase PACE
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-
-
-
SPC3
-
-
-
-
subtilisin-like protein convertase
Trans golgi network protease furin
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-
-
-
additional information
PACE
-
-
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PC1
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-
-
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prohormone convertase
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-
-
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Proprotein convertase
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-
-
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Proprotein convertase
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Proprotein convertase
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additional information
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at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
furin belongs to the family of proprotein convertase subtilisin/kexin type proteases
additional information
-
also cf. EC 3.4.21.93. Prohormone convertases are calcium-dependent serine endoproteases of the subtilisin family
additional information
-
furin is a crucial member of secretory mammalian subtilase, the proprotein convertase or proprotein convertase subtilisin/kexin, PCSK, superfamily
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
furin belongs to the subtilisin/Kex2p-like proprotein convertases
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
141760-45-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
2-amino benzoyl-AEQDRNTREVFAQ-T(3-nitro-tyrosine)-A + H2O
2-amino benzoyl-AEQDRNTR + EVFAQ-T(3-nitro-tyrosine)-A
-
furin-mediated cleavage of a fluorogenic peptide derived from hSARS-CoV spike protein
-
-
?
5-carboxyfluorescein-Gln-Arg-Val-Arg-Arg-Ala-Val-Gly-Ile-Asp-Lys(5-carboxytetramethylrhodamine)-OH + H2O
?
-
-
-
?
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GIRRKR + SVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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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
-
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
-
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
-
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
-
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
-
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
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SKRSRR + SVSVQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
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
-
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
-
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
-
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
-
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
-
FRET-peptide derived from infectious bronchitis viral envelope glycoprotein
-
-
?
Ac-AAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AAKYKR
-
-
-
?
Ac-AARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AARYKR
-
-
-
?
Ac-Arg-Val-Arg-Arg-4-nitroanilide + H2O
Ac-Arg-Val-Arg-Arg + 4-nitroaniline
-
-
-
-
?
Ac-KARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-KARYKR
-
-
-
?
Ac-norleucine-YKR-4-methylcoumarin-7-amide
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-RA-norvaline-YKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RA-norvaline-YKR
-
-
-
?
Ac-RAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RAKYKR
-
-
-
?
Ac-RARYAR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYAR
-
-
-
?
Ac-RARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYKR
-
-
-
?
Ac-RARYRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYRR
-
-
-
?
Ac-RYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRR
-
-
-
?
Ac-RYRFKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRFKR
-
-
-
?
acetyl-norleucine-YKR-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-7-amido-4-methylcoumarin + H2O
acetyl-Tyr-Glu-Lys-Glu-Arg + Ser-Lys-7-amido-4-methylcoumarin
-
-
-
-
?
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
AcRARYKK-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + AcRARYKK
-
-
-
?
Boc-RVRR-4-methylcoumarin 7-amide + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-RVRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Boc-RVRR
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
duck carboxypeptidase D + H2O
?
-
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
?
-
the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
Glu-Arg-Thr-Lys-Arg + (7-methylcoumarin-4-yl)acetate
-
-
-
-
?
hBMP-2 precursor protein + H2O
?
-
cleavage sites are HKREKR-/-QAKH and HVRISR-/-SLHQ
-
-
?
hBMP-4 precursor protein + H2O
?
-
cleavage sites are RRRAKR-/-SPKH and HVRISR-/-SLPQ
-
-
?
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O
?
-
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
-
-
?
heparan sulfate 6-O-endosufatase Sulf2 + H2O
?
-
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
-
-
?
high pathogenic H5N1 hemagglutinin + H2O
?
-
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
?
-
only processed in the presence of heparin
-
-
?
histonin + H2O
?
-
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
?
-
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
-
-
?
influenza variant Fujian-like H5N1 hemagglutinin + H2O
?
-
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
?
-
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
membrane-bound collagen XXIII + H2O
shed collagen XXIII
-
furin is the major protease to process collagen XXIII. Processing occurs after the downstream recognition motif 94KIRTVR99, releasing the ectodomain
-
-
?
N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
nodal + H2O
?
-
cripto interacts with the nodal pro segment and mature domain and presents uncleaved precursor to extracellular furin that is recruited through its P-domain
-
-
?
PC1/3 C-terminal peptide + H2O
?
-
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
?
-
furin fully processes the PC2 mutant at the secondary site in AtT-20 cells, site is accessible to in trans cleavage
-
-
?
PCSK9 + H2O
?
-
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
?
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
-
-
?
pGlu-Arg-Thr-Lys-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
phenylacetyl-Arg-Val-Arg-7-amido-4-methylcoumarin + H2O
phenylacetyl-Arg-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
POMC prohormone precursor + H2O
ACTH + alpha-MSH + beta-endorphin
-
human pituitary may utilize the cathepsin L and prohormone convertase pathways for producing POMC-derived peptide hormones
-
-
?
pro-ADAMTS4 + H2O
?
-
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
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
-
-
-
?
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + propeptide
-
-
-
?
procollagen V + H2O
?
-
proteolytic processing of the proalpha1(V) C-propeptide chain. Proteolytic C-propeptide removal by furin occurs between Arg1585 and Asn1586. Processing of the C-propeptide by furin is more efficient than processing by bone morphogenetic protein-1
-
-
?
proPDGF-B + H2O
PDGF-B + PGDF-B propeptide
-
a growth factor proform of 31 kDa
mature form of 17 kDa
-
?
proprotein convertase PCSK9 + H2O
?
-
-
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
-
?
Protective antigen component of anthrax toxin + H2O
?
-
cleavage at the sequence Arg-Lys-Lys-Arg
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pyr-Arg-Thr-Lys-Arg
-
pERTKR-MCA
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
pyroglutamic acid-RTKR-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-RTKR + 7-amino-4-methylcoumarin
-
-
-
-
?
SARS coronavirus spike glycoprotein + H2O
?
-
introduction of a prototypic furin recognition motif at R667 allows for efficient cleavage of the mutant glycoprotein
-
-
?
Sema3B + H2O
?
cleavage at the furin recognition site is critical for the function of this tumor suppressor
-
-
?
Sema3C + H2O
?
cleavage at the furin recognition site 742RNRR745. The point mutation R745A at the basic domain at the hypothetical furin recognition site 742RNRR745 disables the processing of Sema3C at this specific location. The C-terminal arginine of the putative furin cleavage site at the basic domain of Sema3C protein is critical for its functions in angiogenesis process
-
-
?
Synthetic peptides + H2O
?
-
based on the N-terminal sequence of human proalbumin
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
viral precursor protein E3E2
?
-
processes E3E2 from African Chikungunya virus strain at the HRQRR642ST site, whereas a Chikungunya virus strain of Asian origin is cleaved at site RRQRR642SI
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
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-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
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
-
-
-
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
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-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
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
-
-
?
ADAMTS9 propeptide + H2O
?
-
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
-
-
?
ADAMTS9 propeptide + H2O
?
-
ADAMTS is a disintegrin and metalloprotease domain with thrombospondin type 1 repeats
-
-
?
avian influenza virus A hemagglutinin + H2O
?
-
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
avian influenza virus A hemagglutinin + H2O
?
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
consists of the transforming growth factor-beta1 LAP region, the transforming growth factor-beta2 cleavage site and the transforming growth factor-beta2 mature peptide
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
efficiently cleaved
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide-derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
epithelial Na+ channel + H2O
?
-
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
-
-
?
epithelial Na+ channel + H2O
?
-
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
-
-
?
epithelial Na+ channel + H2O
?
-
furin cleavage of epithelial Na+ channel subunits activates the channels by relieving Na+ self-inhibition. Activation requires that the alpha-subunit is cleaved twice
-
-
?
epithelial Na+ channel + H2O
?
-
epithelial Na+ channel activation during preferential assembly requires furin-dependent and furin-independent processing. Furin consensus site on the alpha subunit is required for epithelial Na+ channel activation upon assembly into alphabetagamma complexes, beta subunit may play a distinct furin-independent role in activation. No causal relationship between gamma cleavage and epithelial Na+ channel activation upon preferential assembly
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
the furin consensus site RRRR-/-D is located between the feline foamy virus Env residues 127 and 128
-
-
?
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
G-protein-coupled receptor GPR107 + H2O
?
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
G-protein-coupled receptor GPR107 + H2O
?
recombinant HA-tagged substrate expressed in HeLa cells. GPR107 contains an extended furin recognition site that includes KSKR, a variant of the classical furin cleavage motif (Arg-Xaa-(Lys/Arg)-Arg), although not common among furin substrates, in GPR107 the Lys residue replaces the first conserved Arg
-
-
?
gp40/15 + H2O
gp40 + gp15
-
cleaves recombinant Cryptosporidium parvum and Cryptosporidium hominis gp40/15. Putative furin cleavage site RSRR
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
hepatitis B e antigen precursor + H2O
?
-
furin can cleave the RRDR, RRGR, and RSPR motifs
-
-
?
HIV-1 Tat protein + H2O
?
-
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
-
-
?
HIV-1 Tat protein + H2O
?
-
furin cleaves full-length Tat protein between amino acid 56 and 57, irrespective of seuence differences at amino acid 57
-
-
?
human semaphorin 3F + H2O
?
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
human semaphorin 3F + H2O
?
-
the substrate is produced as a C-terminal or an N-terminal human growth hormone fusion from the pLexM vector. Cleavage at the RXRR furin recognition site in the C-terminus, which is essential for the interaction of the C-terminus of Sema3F with the b1 domain of neuropilin
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
-
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
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
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
there are two furin cleavage motifs, R89-R-P-R-C93 and R108-R-K-R-Y112
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
furin cleaves the Env precursor into the surface and transmembrane subunits in the cell and then the viral protease cleaves the R-peptide from TM in newvirus. Structure analysis of the open cage-like structure like that of the R-peptide precursor and of the mature protein, overview. Furin cleavage not only separates the subunits and liberates the fusion peptide at the end of TM but also allows the C-terminal domain to relocate into a peripheral position. This conformational change might explain how the C-terminal domain of surface subunit gains the potential to undergo disulfide isomerization, an event that facilitates membrane fusion
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
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
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
furin is the most efficient convertase in cleaving the N-terminal RXXR/RXRR site
-
-
?
PA83 + H2O
PA63 + PA20
the protective antigen substrate is from Bacillus anthracis, commercial plant-produced deglycosylated PA83 (dPA83). Cleavage of the substrate generates two protein fragments with distinctly different molecular masses of 63 kDa (PA63) and 20 kDa (PA20). Plant-produced PA83 protein is almost fully cleaved by commercial furin, while plant-produced truncated enzymatically active furin displays about 75% relative activity compared to commercial human furin in vitro
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
cleavage sequence is Arg73-Ala-Pro-Arg76-/-Ser77
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
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-BMP4 + H2O
BMP4 + propeptide of BMP4
-
i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
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
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
CD109 is a glycosylphosphatidylinositol-anchored glycoprotein, cleavage motif comprises amino acids 1270-RRRR-1273
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
the term -+- depicts the point of cleavage, e.g. stromelysin 3
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
rapid cleavage of the-Arg-Arg-Asp-site, no significant cleavage of natural unprocessed variants with cleavage site sequences of-Arg-Arg-Val-, His-Arg-Asp- or Cys-Arg-Asp
-
-
?
Protein precursor + H2O
?
-
circulating human proalbumin variants with a mutation at either of the basic amino acids adjacent to the cleavage site are not cleaved
-
-
?
Protein precursor + H2O
?
-
cleavage following the prosequence Arg-Gly-Val-Phe-Arg-Arg
-
-
?
Protein precursor + H2O
?
-
also cleaves chicken proalbumin after a single arginine residue following the Arg-Asn-Leu-Gln-Arg-Phe-Ala-Arg prosequence
-
-
?
RPTPkappa + H2O
?
-
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
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
-
Borna disease virus glycoprotein is synthesized as a precursor that is cleaved by cellular furin to produce the mature glycoproteins GP1 and GP2
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
intracellular processing by furin-like prohormone convertases is required for secretion of cysteine-rich FGF receptor
-
-
?
additional information
?
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
-
-
?
additional information
?
-
-
no processing of: human lactase-phlorizin hydrolase
-
-
?
additional information
?
-
-
Preference for Arg-Glu-Lys-Arg-+-Ala vs. Lys-Ala-Lys-Arg-+-Arg
-
-
?
additional information
?
-
-
peptides patterned on the sequence 307-330 of the specific viral strains of the gp120 V3 loop
-
-
?
additional information
?
-
-
study of the specificity of human prohormone convertase PC1 and human furin
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
probably involved in the proteolysis resulting in secretion of rat endopeptidase 24.18 alpha-subunit
-
-
?
additional information
?
-
-
possible role in processing essential cellular factors
-
-
?
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
?
additional information
?
-
-
proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
-
?
additional information
?
-
-
low pathogenic Mexico H5N2 hemagglutinin is not processed by furin
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
-
a three-step autocatalytic processing including the cleavage of the prodomain at the Arg-Leu-Gln-Arg89Q-Glu90 site, is required for the efficient activation of furin
-
-
?
additional information
?
-
-
furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase, recombinantly expressed as GFP-tagged enzyme in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
-
-
?
additional information
?
-
-
furin cleavage sequence is RXXR-/-X, X is not Cys
-
-
?
additional information
?
-
-
furin is a proprotein convertase that requires the cleavage sequence R-X-K/R-R, clear interdependence of furin subsites, substrate specificity with synthetic peptide substrates, overview
-
-
?
additional information
?
-
-
furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
-
-
?
additional information
?
-
-
furin performs autocleaqvage to its soluble form
-
-
?
additional information
?
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
high substrate selectivity and enzymatic activity of furin
-
-
?
additional information
?
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
survey of furin substrate specificity using substrate phage display
-
-
?
additional information
?
-
-
synthetic tripeptide substrates containing only pairs of basic amino acids are not well cleaved
-
-
?
additional information
?
-
-
the term -+- depicts the point of cleavage, the enzyme prefers substrates with an arginine 4-amino acid amino-terminal to the cleavage site
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
no cleavage of the low pathogenic H1N1 H1 hemagglutinin
-
-
?
additional information
?
-
-
soluble hemojuvelin originates from a furin cleavage at position 332-335. Soluble hemojuvelin is increased in cells overexpressing exogenous furin
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
?
additional information
?
-
-
3D structural environment of the furin binding pocket surrounding the core region P6-P2' of furin substrates, comparison to other protein convertases, to allow the rational design of novel specific molecular inhibitors targeting specific members of the mammalian proprotein convertase family, overview. The furin autocleavage site is RGVTKR75 -/-
-
-
?
additional information
?
-
-
furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
-
-
?
additional information
?
-
-
probably plays a role in proprotein maturation
-
-
?
additional information
?
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
plays an important role in posttranslatioal protein processing
-
?
additional information
?
-
-
plays an important role in posttranslatioal protein processing
-
?
additional information
?
-
-
regular (short) form of transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin
-
-
?
additional information
?
-
-
transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin. Transforming growth factor-beta2 is only inefficiently cleaved as a consequence of the isoform specific characteristics of its latency-associated peptide region structures
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADAMTS9 propeptide + H2O
?
-
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
-
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
-
-
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
G-protein-coupled receptor GPR107 + H2O
?
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
HIV-1 Tat protein + H2O
?
-
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
?
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
insulin-like growth factor-1 receptor + H2O
?
-
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
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
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
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
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
-
-
?
pro-ADAMTS4 + H2O
?
-
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
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
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 + ?
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
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
-
-
?
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + propeptide
-
-
-
?
proprotein convertase PCSK9 + H2O
?
-
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
additional information
?
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
probably involved in the proteolysis resulting in secretion of rat endopeptidase 24.18 alpha-subunit
-
-
?
additional information
?
-
-
possible role in processing essential cellular factors
-
-
?
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
?
additional information
?
-
-
proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
-
?
additional information
?
-
-
furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase, recombinantly expressed as GFP-tagged enzyme in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
-
-
?
additional information
?
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
-
activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
-
-
?
additional information
?
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
?
additional information
?
-
-
probably plays a role in proprotein maturation
-
-
?
additional information
?
-
plays an important role in posttranslatioal protein processing
-
?
additional information
?
-
-
plays an important role in posttranslatioal protein processing
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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
Ca2+
strict Ca2+ dependence, calcium-dependent activity regulation of furin
Ca2+
optimal concentration of mutant furin is 0.5 mM, activity gradually reduced with increasing Ca2+ concentrations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
-
-
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
-
-
(1S,14S,17S,20S,23S,26S,33r)-26-amino-N-(4-carbamimidoylbenzyl)-20,23-bis(3-guanidinopropyl)-17-neopentyl-4,8,16,19,22,25,32-heptaoxo-3,9,15,18,21,24,31-heptaazabicyclo[31.2.2]heptatriacontane-14-carboxamide
-
(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
1,1'-((1R,3S,4S,6R)-4,6-bis(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
meso compound
1,1'-((1R,3S,4S,6R)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
racemate, blocks the S2 pocket
1,1'-((1S,3R,4R,6S)-4-((4-guanidinonaphthalen-1-yl)oxy)-6-(4-guanidinophenoxy)cyclohexane-1,3-diyl)diguanidine
blocks the S2 pocket
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
-
-
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
-
-
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
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-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(4-amidomethyl)-benzamidine
MI-52, a substrate-analogous, noncovalent inhibitor. The furin-MI-52 complex is highly stable
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
-
-
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
-
-
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 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
-
Chloroquine
-
weakly affects proprotein convertase activity and E3E2 processing. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
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(4,4''-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
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
-
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
-
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
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
-
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
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 4-[4-(2-amino-2-oxoethyl)piperazin-1-yl]butanamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]butanediamide bridged)
-
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]pentanediamide bridged)
-
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
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,N'-[[(1R,3S,4S,6R)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
racemate, interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine
interferes directly with the catalytic competent conformation of the catalytic triad. Inhibition mechanism, overview
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
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-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-carbamimidamidopentyl)-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
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
a competitive, noncovalent inhibitor, binding structure, overview
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
-
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 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
peptide derived from proprotein convertase 1/3
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
alpha1-antitrypsin
-
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-antitrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
alpha1-antitrypsin
-
in cells overexpressing alpha1-antitrypsin, mRNA level of furin is reduced
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-PDX
-
a furin- and PC6-selective inhibitor, blocks cleavage of furin minimal consensus motifs, and of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase
-
brefeldin A
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
efficiently inhibits ectodomain shedding by 95%
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
20 micromol results in a decrease in processed sol-membrane type-1 matrix metalloproteinase, significant decrease in motility compared to control cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
most inhibitory, inhibits Cryptosporidium parvum infection of HCT-8 cells in a dose-dependent manner, with ca. 50% inhibition occurring at a concentration of 0.01 mM
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin protease inhibitor, significantly diminishes secretion of S-tag-containing cysteine-rich FGF receptor products
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
significantly blocks the processing of ADAMTS4 in HEK-293 cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks cleavage of the first and second motifs in human hepatoma cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
fully blocks the substrate cleavage by the wild-type enzyme
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks furin activity, 99% inhibition of parathyroid hormone-related peptide maturation
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor, pro-hepcidin activity is abolished
decanoyl-RVKR-chloromethyl ketone
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
decanoyl-RVKR-chloromethyl ketone
-
furin inhibitor, inhibits E3E2 cleavage. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
decanoyl-RVKR-chloromethylketone
-
the furin inhibitor reduces DHBV infection of primary duck hepatocytes
hexa-D-arginine
-
blocks furin activity, 85% inhibition of parathyroid hormone-related peptide maturation
Zn2+
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
cell-permeable, small-molecule compound, which inhibits at 15 micromol furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in an almost complete inhibition of matrix metalloprotease-2-related cell motility in CHO cells
-
additional information
-
aprotinin has no effect on furin-like protease activity
-
additional information
-
a potent inhibitor containing a ketomethylene arginyl pseudopeptide bond; contains Cys near the active site His
-
additional information
-
Boc-RVRR-4-methylcoumarin-7-amide does not show any signs of substrate inhibition
-
additional information
-
the prodomain exhibits inhibitory action toward furin
-
additional information
-
siRNA-mediated depletion of endogenous c-Jun NH2-terminal kinase-interacting leucine zipper protein (JLP) or phosphoinositide kinase for position 5 containing a five finger domain (PIKfyve), profoundly delays microtubule-based transport of chimeric furin (Tac-furin) from endosomes to the trans-Golgi network in a CHO cell line, which is rescued upon ectopic expression of siRNA-resistant JLP or PIKfyve constructs
-
additional information
-
cell-permeable, small-molecule compound, which inhibits furin-mediated cleavage of pro-membrane type-1 matrix metalloproteinase, resulting in a 50% decrease in the invasiveness of the HT1080 cell
-
additional information
-
expression of furin in HaCaT cells declines with respect to time in response to UV radiation irrespective of the type or the dose used
-
additional information
-
O-glycosylation of substrate proBNP in the cleavage site region at Thr71 reduces furin cleaving activity, overview
-
additional information
-
EC values of furin inhibitors, overview. Inhibition of cell-surface PA83 processing in cell-based assays, overview
-
additional information
-
synthetic aromatic enediyne derivatives and their effects on protease activity of proprotein convertases furin, overview
-
additional information
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
-
peptidomimetic compounds based on a phenylacetyl-Arg-Val-Arg-4-(amidomethyl)benzamidine core structure belong to the strongest noncovalent enzyme inhibitors. Upon variation of the P5 position, dramatic changes of the Ki values are observed that cannot be explained by the known recognition motive. The Ki improves by approximately 2 orders of magnitude after addition of basic substituents, e.g., by modification of the Phac-moiety at P5 by a m- or p-guanidinomethyl group. Structure-guided drug design, overview
-
additional information
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
-
active site distortions of human furin by a small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, analysis of binding structures of noncovalent 2,5-dideoxystreptamine-derived furin inhibitors, overview
-
additional information
analysis of the interactions of P4-P6 of furin with substrate-like peptide inhibitors using X-ray crystallography, substrate specificity is mediated at these binding sites, docking study, detailed overview
-
additional information
inhibitor constructuion, synthesis, and structure-function analysis, overview. Evaluation of inhibition of alphavirus propagation and inhibition of diphtheria toxin action
-
additional information
development of specific inhibitors of furin, synthesis of several truncated analogues of the bicyclic sunflower trypsin inhibitor (SFTI-1), or of compounds by various head-to-tail, head-to-side chain, and side-chain-to-tail cyclizations within multibasic octapeptides, or of several cationic cyclized peptides with cell-penetrating properties, overview. Inhibitory potency of these compounds is determined in enzyme kinetic assays with furin. Inhibitor docking study, crystal structure determination, and structure-function analysis. Modeling of furin in complex with inhibitors N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide, diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate, diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate, and diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate. Inhibition of respiratory syncytial virus propagation in A549 cells
-
additional information
no inhibition of human furin by DFP, 4-(2-aminoethyl)benzensulfonylfluorid (AEBSF), and PMSF
-
additional information
-
soluble hemojuvelin is reduced in cells treated with a furin inhibitor
-
additional information
-
pepstatin A, 1,10-ortho-phenanthroline, EDTA, or TAPI-0 do not inhibit ectodomain shedding
-
additional information
-
design of specific small molecule inhibitors targeting furi, overview
-
additional information
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
largely unaffected by aprotinin, leupeptin, pepstatin A, [4-amidino-phenyl]-methansulfonylfluoride, (4-[2-aminoethyl]-benzolsulfonylfluoride), phosphoramidon, bestatin, phenylmethylsulfonylfluoride, and antipain
-
additional information
-
compounds 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(2-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(3-guanidinopyridin-4-yloxy)cyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-2,4-bis(2-amino-1H-benzo[d]imidazol-6-yloxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide, 2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(pyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide and (1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(2-guanidinophenylcarbamate) do not inhibit
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
additional information
-
heparin-peptide interaction may better expose site1, and hence allow more effective furin cleavage. Extended sequences require heparin for optimal processing by furin
-
additional information
-
His69 controls the pH-sensitive furin propeptide cleavage and enzyme activation in vitro. Protonated His69 disrupts the propeptide to expose the internal cleavage site and increases the efficiency of cleavage at Arg75 to yield the active enzyme
-
additional information
-
in the presence of trifluoroethanol, the N-terminal half of the prodomain is better structured and more compactly folded than the C-terminal half of the prodomain. N-terminal residues 1-46 of the prodomain in 50% trifluoroethanol populates backbone conformations containing a short helix, a beta-strand and a helix-loop-helix supersecondary structure with elements of tertiary interactions. The intervening segment (residues 47-65) is predominately unstructured with a long and highly flexible region surrounding the protease activation loop followed by a partially helical segment in the C-terminal end. A peptide fragment derived from residues Pro16-Arg49 can form the helix-loop-helix structure in aqueous solution in the absence of trifluoroethanol
-
additional information
-
L-Sox5 and Sox-6 act as negative regulators of Sox9-induced furin expression
-
additional information
-
expression of furin in irradiated Colo-16 cells remains constant for 48 h following exposure of the cells to either low dose UVA and/or UVB radiation, and high-dose UVA radiation. In cells irradiated with high-dose UVB radiation, significant increase in furin expression commencing at 12 h, which peaks at 24 h (5fold). Correlation between expression of pp38 and furin in Colo-16 cells, but not HaCaT cells, following UV exposure
-
additional information
structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism, complex activation mechanism, overview
-
additional information
-
furin is up-regulated by iron deficiency and hypoxia in association with the stabilization of HIF-1alpha
-
additional information
-
relationship between Sox-9 dependent expression of furin and the maturation/bioactivation of substrates involved in chondrogenesis. Peak expression of both furin mRNA and furin parathyroid hormone-related peptide maturation in ATDC5 cells during chondrocyte nodule formation stage
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
0.01517
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.00039
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00042
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00021
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0012
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0003
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0032
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00038
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0027
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0002
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00022
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00028
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00037
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00005
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0001
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00028
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0052
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00033
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0014
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0002
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0065
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0012
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0122
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00039
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00041
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00041
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00049
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00015
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00045
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00014
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.005
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00086
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00416
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.000036
viral precursor protein E3E2
-
R64A mutant peptide of E3E2 from Asian Chikungunya virus strain
-
0.000122
viral precursor protein E3E2
-
wild-type E3E2 from Asian Chikungunya virus strain
-
additional information
additional information
-
upon increase of the pH from 6.0 to 9.0, KM-decreases linearly up to pH 7.5 and then remains constant
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
29.6
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
30.3
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.6
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
4.2
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
28.9
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
39.5
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.3
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6.9
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.6
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
12.2
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
9.2
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
14.9
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.6
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.1
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.61
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.7
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3.5
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2.6
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
12.3
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
8.4
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
11.3
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
5.3
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
8.7
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
12.2
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
14.6
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2.4
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
6.7
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.6
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
10.5
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
18.3
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
0.21
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2.4
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
9.2
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
9.9
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
10
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
11.1
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
5.6
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
7.1
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
16.4
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
19.8
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
additional information
additional information
-
over the pH intercal 6.0 to 9.0 kcat occurs as a bell-shaped form with a maximum at pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
322
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
70550
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
77100
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
3085
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
20190
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
9031
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
116100
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
2354
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
17730
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
38300
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
55640
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
32430
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
40270
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6000
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
53450
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1303
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
2184
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
1470
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
10610
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1555
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
123000
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1291
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
56300
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
710
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
4383
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
29660
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
37510
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
797
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
30500
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
606
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
33040
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
25360
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
37350
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
559
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
33860
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
20470
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
66000
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1992
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
76230
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
1707
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
6488
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
28360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, absence of Mg2+
37360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37°C, presence of Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001768
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
-
-
0.000812
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
-
-
0.00000099
(1S,14S,17S,20S,23S,26S,33r)-26-amino-N-(4-carbamimidoylbenzyl)-20,23-bis(3-guanidinopropyl)-17-neopentyl-4,8,16,19,22,25,32-heptaoxo-3,9,15,18,21,24,31-heptaazabicyclo[31.2.2]heptatriacontane-14-carboxamide
pH and temperature not specified in the publication
0.000046
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
-
-
0.000423
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
-
-
0.000169
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
-
-
0.000404
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000089
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000022
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000069
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000012
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000042
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
-
-
0.000006
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
-
-
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
2
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0000025
3-guanidinomethylphenylacetyl-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000000224
4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
1.3
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.000019
Ac-Ac-RQIKIWFQNRRMKWKKRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000228
Ac-AGYLLGKINLKALAALAKKILRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000107
Ac-RRRRRRRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000011
Ac-YGRKKRRQRRRVR 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0024
acetyl-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.0000094
Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.000006
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.0000093
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
pH and temperature not specified in the publication
0.0000000337
Arg-Arg-Arg-Val-Arg-4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000000000337
Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.0000574
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.000009
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000151
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000383
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0042
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000278
cyclo[(Arg)10]
pH and temperature not specified in the publication
0.0001104
cyclo[(Arg)6]
pH and temperature not specified in the publication
0.0000227
cyclo[(Arg)8]
pH and temperature not specified in the publication
0.00000068
cyclo[glutaryl-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000504
cyclo[glutaryl-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.00000105
cyclo[glutaryl-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000146
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000154
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.0000000538
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000136
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000378
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Arg 4-amidinobenzylamide
pH and temperature not specified in the publication
0.000000618
cyclo[succinyl-Phe-2-Nal-Arg-Arg-Arg-Lys]-Lys 4-amidinobenzylamide
pH and temperature not specified in the publication
0.00000011
D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000378
D-Arg-D-Arg-D-Arg-D-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000078
eglin c mutant Arg replaced with Asp at P3
-
pH 7.5, 37°C
-
0.000023
eglin c mutant D42R, eglin c mutant L45R, eglin variant M1 RVTR
-
pH 7.5, 37°C
-
0.000156
hfurin25-107
-
pH 7.4, 37°C, versus N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide
-
0.000000491
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 4-[4-(2-amino-2-oxoethyl)piperazin-1-yl]butanamide bridged)
pH and temperature not specified in the publication
0.00000504
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]butanediamide bridged)
pH and temperature not specified in the publication
0.00000117
Lys-Arg-Arg-Tle-Lys 4-amidinobenzylamide (Lys1-Lys5 N1-[[4-(2-amino-2-oxoethyl)phenyl]methyl]pentanediamide bridged)
pH and temperature not specified in the publication
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 7.0,22°C
0.00046
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
pH 7.0,22°C
0.00104
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
pH 7.0,22°C
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 7.0,22°C
0.000000193
N2(carbamidoyl)Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000449
N2(carbamidoyl)Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0002693
N2-(3-aminomethyl-phenylacetyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000459
N2-(5-(guanidino)valeroyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000267
N2-(5-guanidinopentanoly)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
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
0.0000000786
N2-acetyl-D-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
pH 7.0, 22°C
0.000001
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000164
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000482
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Tle-Lys 4-amidinobenzylamide
pH 7.0, 22°C
0.0000378
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.000000164
N2-acetyl-Leu-Leu-Leu-Leu-Arg-Val-Lys 4-amidinobenzylamide
pH 7.0, 22°C
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
0.000000051
N2-phenylacetyl-Ala-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000283
N2-phenylacetyl-Arg-Ala-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000337
N2-phenylacetyl-Arg-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000491
N2-phenylacetyl-Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000563
N2-phenylacetyl-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000000138
Nalpha(carbamidoyl)Arg-Arg-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.00000081
phenylacetyl-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.000238
phenylacetyl-Cit-Arg-Val-Arg-4-aminomethyl-benzamidine
pH and temperature not specified in the publication
0.00000126
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
0.0000385
N2-(5-aminopentanoyl)-Val-Arg 4-amidinobenzylamide
pH 7.0, 22°C
additional information
additional information
-
Ki-values of alpha1-antitrypsin and alpha1-antichymotrypsin mutants obtained by incorporation of furin recognition sequences within the reactive site loop of the molecule and modifying the P7-P1 region of the reactive site loop
-
additional information
additional information
Ki values of the inhibitors with inhibition constants above 0.1 nM are determined by fitting of the data to the equation for classical reversible competitive inhibition
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
0.051
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
0.0077
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
0.000193
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
0.00016
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
Homo sapiens
-
-
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
Homo sapiens
-
-
0.00004
furin-Eda peptide acyclic
Homo sapiens
-
versus substrate N-benzyloxy-RVRR-4-methylcoumarin 7-amide
0.00004
furin-Eda peptide acyclic
Homo sapiens
-
versus substrate N-benzyloxy-RVRR-4-methylcoumarin 7-amide, pH not specified in the publication, temperature not specified in the publication
0.000193
furin-Eda peptide acyclic
Homo sapiens
-
versus substrate fluorogenic peptide derived from hSARS-CoV spike protein, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
7.5
additional information
additional information
between pH 7-9, mutant has a broad pH optimum shifted toward alkalinity
additional information
-
between pH 7-9, mutant has a broad pH optimum shifted toward alkalinity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
6 - 11
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
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
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
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
at least 3 related enzymes are recognized in mammals: PC2
-
-
brenda
at least 3 related enzymes are recognized in mammals: PC3 (identical with PC1)
-
-
brenda
-
29686, 29688, 29692, 29693, 29694, 29695, 29696, 29697, 29699, 29701, 668923, 669214, 669255, 669258, 669442, 670247, 670828, 677290, 677460, 677786, 677957, 677962, 678063, 678743, 678910, 679039, 679142, 679776, 679871, 680137, 680654, 680696, 680791, 680878, 681510, 681918, 682808, 682972, 693230, 697621, 698960, 699309, 699910, 700401, 700627, 700898, 707275, 707527, 707598, 708162, 708168, 708242, 708682, 708753, 709465, 710165, 710258, 710381, 717306, 717362, 717827, 717903, 717927, 718256, 718447
-
-
brenda
-
731038, 731605, 732149, 732423, 732499, 732774, 732833, 732859, 732972, 752361, 752405, 752785, 753128, 753199, 753279, 753282, 754359, 755027, 755183, 755251
SwissProt
brenda
rat somatomammotroph cell line, GH4C1 infected with vaccinia virus recombinants of human PC1
-
-
brenda
-
29699, 29700, 667392, 669253, 670247, 677460, 677511, 677962, 678739, 678910, 678922, 680811, 680878, 697609, 699309, 701154, 707598, 708682, 708758, 717230, 717317, 717857, 718256, 731605
-
-
brenda
expression in Chinese hamster ovary cells
-
-
brenda
rat somatomammotroph cell line, GH4C1 infected with vaccinia virus recombinants of murine PC1
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in the digestive gland the PC1 activity of pre-breeding stage is 1.17fold and 1.55fold as that of the during-breeding and the post-breeding stages, respectively
brenda
-
PCSK3 is primarily expressed in the duodenum and the jejunum. PCSK3 is detectable in 75% of glucose-dependent insulinotropic polypeptide positive cells and 60% of substance P positive cells
brenda
additional information
-
chief cells, coordinated decrease of pepsinogen, furin, and transforming growth factor beta
brenda
-
chief cells, coordinated decrease of pepsinogen, furin, and transforming growth factor beta
-
brenda
-
relative activity of PC1 in gonad is 10% of that in the digestive gland. In male, the PC1 activity in digestive gland is slightly lower than in female
brenda
-
expression and regulation of furin in ovarian tissue, injection of equine and human chorionic gondotropin, overview
brenda
-
furin is highly expressed in placental villi during early pregnancy, specifically in trophoblast column and trophoblast shell, regions where highly invasive cytotrophoblast cells invade the maternal decidua during human placentation
brenda
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
brenda
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
brenda
additional information
no PCSK3 in head, ovary, and small intestine, expression in the adult, not embryo stage
brenda
additional information
-
no PCSK3 in head, ovary, and small intestine, expression in the adult, not embryo stage
brenda
additional information
-
preferentially expressed in T helper 1 cells in a Stat4-dependent manner
brenda
additional information
-
present in glucagon cells, absent from insulin cells, somatostatin cells and pancreatic polypeptide cells
brenda
additional information
-
colorectal carcinoma LoVo cell line is devoid of furin activity
brenda
additional information
cellular furin abundance in five human cell lines is shown to be strongly correlated with productive infectious bronchitis virus, IBV, infection, cells expressing furin, overview
brenda
additional information
-
cellular furin abundance in five human cell lines is shown to be strongly correlated with productive infectious bronchitis virus, IBV, infection, cells expressing furin, overview
brenda
additional information
the enzyme is constitutively expressed in all cell lines. No enzyme activity in LoVo colorectal carcinoma cells
brenda
additional information
ubiquitous expression, although furin is expressed universally, expression levels vary and can be quite low depending on tissue types
brenda
additional information
-
ubiquitous expression, although furin is expressed universally, expression levels vary and can be quite low depending on tissue types
brenda
additional information
-
furin mRNA and protein highly expressed in T helper 1 cells compared with T helper 2 cells. Stat4 binding sites in the putative promoter region (2000 bp upstream of exon 1). Also present in CD4+ T cells
brenda
additional information
-
furin is highly expressed in granulosa cells and oocytes of the ovary with very limited expression in other ovarian cells such as the epithelial, stromal or theca cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
brenda
the enzyme contains a signal peptide (amino acids 1-25) and is secreted
-
brenda
additional information
-
hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
brenda
-
furin localizes to endosomes when Mint3 expression is knocked down
brenda
-
hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
brenda
-
furin is primarily located in the Golgi and trans-Golgi network, and it can also circulate between the cell surface and the trans-Golgi network
brenda
-
interaction between the phosphotyrosine-binding domain of Mint3 and the acidic peptide signal in the cytoplasmic domain of furin regulates the specific localization of furin in the trans-Golgi network. The phosphotyrosine-binding domain of Mint3 is essential for furin-Mint3 interaction
brenda
-
the membrane-bound enzyme undergoes post-translational processing to produce a soluble form of the enzyme that can be secreted
brenda
-
cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
-
brenda
-
cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
-
brenda
-
human, mainly, the enzyme can translocate between the cell surface and the trans-Golgi network
-
brenda
-
knockdown of Mint3 increases the distribution of furin at the membrane
brenda
additional information
-
furin is present both in the intracellular secretory pathway and at the cell surface
-
brenda
additional information
furin is a protease localized in the trans-Golgi network and in late endocytic compartments
-
brenda
additional information
-
furin is a protease localized in the trans-Golgi network and in late endocytic compartments
-
brenda
additional information
complementary subcellular distribution of bioactive furin and proprotein convertase PC7. Furin activity in endosomes is 10fold less inhibited by decanoyl-RVKR-chloromethylketone and enriched over 3fold in endosomes compared to the trans-Golgi network. Development of targeted compartment-specific biosensors. Endogenous PC7, which resists the inhibitor, is active in distinct vesicles. The distribution of proprotein convertase activities at the tissue level are monitored by introduction of biosensor CLIP (cell-linked indicator of proteolysis). CLIP v.3 is suitable for ratiometric imaging without interference by FRET and can estimate PC activity in exocytic compartments, whereas CLIP v.4 can be used as a FRET-based biosensor to quantify PC activities in specific intracellular vesicles. Fusion to the cytosolic tail of PC7 directs CLIP v.4 to compartments that harbor furin activity, but not full-length PC7
-
brenda
additional information
-
localization of furin predominantly outside lipid rafts
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
molecular evolution of enzyme function in the proprotein convertase family, overview
evolution
-
PC members are paralogous genes derived from a common ancestor, which represents independent lineages by gene replication in evolution. Abalone PC1 is located in PC1 clade which is orthologous genes in different species. The potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
evolution
furin is a member of the pro-hormone/pro-protein convertase family of subtilisin-like endoproteinases
evolution
-
furin is a member of the subtilisin-like proteases and belongs to the proprotein convertase subtilisin/kexin-like proteases, subgroup PCSK3
evolution
-
phylogenetic analysis and sequence comparisons. Differences may exist between furin proteases present in fruit bats compared to furins in other mammalian species, and these differences may impact protease usage for viral glycoprotein processing. Subtle differences in cellular distribution and localization of furin or trafficking through trans-Golgi network may exist between different mammalian species
evolution
the enzyme belongs to the proprotein convertase family of proteases
evolution
the enzyme is a member of the subtilisin-like proprotein convertase family
evolution
four of nine conserved proprotein convertases (PCs), including furin, Pace4, PC5A/B, and PC7, cleave substrates after the minimal dibasic recognition motif (K/R)-(X)n-(K/R)Y, where n is 0, 2, 4, or 6 and X can be any amino acid. In 152 PC sequences examined across species, the catalytic sites are 95% identical
evolution
furin belongs to the family of Ca2+-dependent proprotein convertases (PCs), all of which contain a subtilisin-like serine protease domain. Furin and the other six basic PCs, i.e. PC1, PC2, PC4, PACE4, PC5, and PC7, cleave their substrates at multibasic sequences mainly after arginine, whereas the nonbasic PC site-1 protease (S1P) cleaves preferentially after leucine, valine, or isoleucine
evolution
furin belongs to the proprotein convertase subtilisin/kexin (PCSK) family of enzymes play a crucial role in processing and trafficking of a wide variety of precursor proteins such as hormones, receptors, and enzymes
malfunction
-
blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview
malfunction
-
furin inhibition leads to a 38% reduction of oocyte release from ovaries, overview
malfunction
-
furin is involved in many physiological and pathological processes
malfunction
-
furin is linked to cancer, tumorgenesis, and viral and bacterial pathogenesis
malfunction
-
furin or a furin-like proprotein convertase facilitates duck hepatitis B virus, DHBV, infection by cleaving both the docking receptor and the viral large envelope protein
malfunction
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
malfunction
ablation of productive infectious bronchitis virus, IBV, infection by knockdown of furin expression in H1299 cells
malfunction
-
furin inhibition reduces brain-derived neurotrophic factor maturation and secretion
malfunction
-
furin siRNA significantly increases apoptosis of the granulosa cells from large antral/preovulatory follicles, in part via downregulation of the anti-apoptotic proteins, XIAP and p-AKT. On the contrary, furin siRNA markedly decreases proliferation of granulosa cells based on the downregulation of proliferation cell nuclear antigen
malfunction
furin siRNAs upregulate HIF-1alpha protein under normoxic condition to a level similar to that obtained by cobalt chloride treatment, eventually leading to activation of VEGF-A synthesis in two human head and neck squamous cell carcinoma cell lines. HIF-1alpha induction of the enzyme siRNAs and either cobalt chloride or the 26S ribosome inhibitor, MG-132, suggesting a post-transcriptional enzyme-mediated regulation, the induction by siRNAs is inhibited by a specific IGF-1R signaling inhibitor
malfunction
furin-specific siRNAs or inhibitors inhibit cell fusion in choriocarcinoma BeWo cells, as well as trophoblast syncytialization in human placental explants
malfunction
knockdown of the enzyme expression in C8161.9, MelJuSo, and HeLa cells by shRNA leads to reduced or complete loss of KISS1 processing
malfunction
-
placenta-specific knockdown of furin in the mouse leads to severe defects in syncytialization and embryonic lethality, phenotype, overview
malfunction
an unbalanced activity of proprotein convertases is connected to pathologies like cancer, atherosclerosis, hypercholesterolaemia, and infectious diseases
malfunction
dysregulation of furin is implicated in numerous disease states, including cancer and fibrosis
malfunction
interleukin-2 is increased initially in furin-deficient mouse CD4+ T cells, but the T-cell receptor-induced interleukin-2 mRNA expression is not sustained in the absence of furin. Conditional deletion of FURIN in CD4+ T-cells leads to hyperactive T-cells and the overproduction of Th1 and Th2 cytokines and systemic autoimmunity as a result of the loss of Treg-mediated immunologic tolerance
malfunction
plant-produced human furin treated with PNGase F and Endo H does not exhibit cleavage activity. Similarly, when commercial human furin (NEB) is treated with commercial Endo H or PNGase F, no cleavage is observed for the substrate PA83
malfunction
Sema3B acts as a tumor suppressor in lung cancer and inhibits the formation of endothelial cells tubes in an in vitro angiogenesis. This function is abrogated upon mutation at the furin cleavage site. The C-terminal arginine of the putative furin cleavage site at the basic domain of Sema3C protein is critical for its functions in angiogenesis process
malfunction
the inhibition of furin in human Jurkat T cell lines also results in a decrease in interleukin-2 production, whereas the overexpression of wild-type furin is associated with elevated interleukin-2 levels
malfunction
the PLC motif in the cytosolic tail of proprotein convertase 7 (PC7) is dispensable for endosomal activity, but it is specifically required for trans-Golgi network (TGN) recycling and to rescue proactivin-A cleavage in furin-depleted B16-F1 melanoma cells. PC7 complements furin in cleaving Notch1 independently of PLC-mediated TGN access
malfunction
-
furin inhibition reduces brain-derived neurotrophic factor maturation and secretion
-
metabolism
cellular furin content might be a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection
metabolism
-
the enzyme activates large numbers of proprotein substrates and is ubiquitously expressed and implicated in many physiological and pathological processes
metabolism
all proprotein convertase (PC) activity detected in the trans-Golgi network/endosomal system of B16-F1 cells is mediated by furin, but not by endogenous PC7
metabolism
furin promotes the activation of T cell receptor-induced transcription factors
metabolism
furin-dependent transactivators in different mouse CD4+ T-cell subsets, overview
physiological function
-
bone morphogenetic proteins, BMPs, require proteolytic activation by members of the proprotein convertase family
physiological function
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furin activation of the C-terminus of Sema3F produces a species that potently inhibits the binding of VEGF to neuropilin, the C-terminal neuropilin binding region of human Sema3F comprises residues 605-785. Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, mechanism, overview
physiological function
-
furin and related proprotein convertases cleave the multibasic motifs R-X-R/K/X-R in the precursor proteins and, as a result, transform the latent proproteins into biologically active proteins and peptides
physiological function
-
furin cleavage of CD109 is necessary for its biological activity, CD109 negatively regulates transforming growth factor-beta signaling in keratinocytes by directly modulating receptor activity. Processing of CD109 into 180 kDa and 25kDa proteins by furin, followed by complex formation with the type I TGF-beta receptor is required for the regulation of TGF-beta signaling in cancer cells and keratinocytes
physiological function
-
furin is involved in many physiological and pathological processes, it plays a role in human trophoblast invasion and migration
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
proprotein convertase FurinA plays a role in zebrafish fin development and cell surface shedding of Fras1 and Frem2, large basement membrane proteins, thereby allowing proper localization of the proteins within the basement membrane of forming fins, mechanisms of basement membrane anchorage, overview
physiological function
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 30fold
physiological function
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 7fold
physiological function
-
the enzyme plays a key role in the posttranslational processing of precursors for bioactive peptides
physiological function
expression of Dfurin1 enhances Sindbis virus titers in RPE.40 cells by a factor of 100-1000, and this increase correlates with efficient cleavage of PE2 glycoprotein
physiological function
-
furin is involved in processing of bone morphogenetic protein BMP10. Processing occurs mostly intracellularly, but also at the cell surface
physiological function
-
furin serves as an intermolecular chaperone for matrix metalloprotease MMP-28 secretion by interacting with the propeptide domain of MMP-28. cleavage of MMP-28 at the furin consensus sequence does not occur and proteolytic inactive furin is equally effective in enhancing MMP-28 secretion
physiological function
-
hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells. Exposing these cells back to normoxic conditions reverses furin redistribution, suggesting that the tumor microenvironment modulates furin trafficking in a highly regulated manner. Both Rab4GTPase-dependent recycling and interaction of furin with the cytoskeletal anchoring protein, filami A, are essential for the cell surface relocalization of furin. Interference with the association of furin with filamin A, prevents cell surface relocalization of furin and abolishes the ability of cancer cells to migrate in response to hypoxia
physiological function
-
in mice lacking furin in hepatocytes, the PCSK9-inactivated form is strongly reduced. Full-length, membrane-bound, but not soluble, furin is the cognate convertase which inactivates PCSK9 by cleavage at R218
physiological function
-
fruit bat cells have homologues of cathepsin and furin proteases capable of cleaving and activating both the cathepsin-dependent Hendra virus F and the furin-dependent parainfluenza virus 5 F proteins, involvement of a furin protease in the cleavage of the PIV5 fusion protein, overview
physiological function
furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure, overview
physiological function
furin is involved in the secretory pathway. It is the major proprotein convertase required for KISS1-to-kisspeptin processing. KISS1 is a broadly functional secreted proprotein that is then processed into small peptides, termed kisspeptins
physiological function
furin is the major processing protease of the secretory pathway. GPR107 localizes to the trans-Golgi network and is essential for retrograde transport. It is cleaved by the endoprotease furin
physiological function
-
furin is upregulated and cleaves certain substrates during hypoxia in cancer cells, the enzyme mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation. Maturation of brain-derived neurotrophic factor in astrocytes requires furin-mediated endoproteolytic processing of the precursor protein pro-brain-derived neurotrophic factor to brain-derived neurotrophic factor
physiological function
-
furin may play an important role in regulating apoptosis and proliferation of granulosa cells, role of furin in the development of granulosa cells during folliculogenesis, overview
physiological function
furin mediates maturation of bone morphogenetic protein-4
physiological function
regulation of HIF-1 alpha, a major transcription factor involved in tumorigenesis by sensing intratumoral hypoxia, by the proprotein convertases furin and PC7 in human squamous carcinoma cells, overview. Furin is one of the numerous target genes regulated by HIF-1alpha transactivation and its distribution into endosomal compartments and onto the cell surface can be triggered by hypoxia via HIF-1alpha, overview
physiological function
the enzyme is necessary to promote the formation of higher order dendritic branches in PVD mechanosensory neurons and to ensure self-avoidance of sister branches, but is likely not required during maintenance of dendritic arbors. The enzyme also regulates the development of other neurons in all major neuronal classes in Caenorhabditis elegans, including aspects of branching and extension of neurites as well as cell positioning. The enzyme functions in a pathway with MNR-1/menorin, SAX-7/L1CAM and DMA-1 to control dendritic branch formation and extension of PVD neurons. The enzyme acts in concert with the menorin pathway to control branching and growth of somatosensory dendrites in PVD
physiological function
the furin expression level is directly proportional to the efficiency of hemagglutinin cleavage, with implications for viral spread in the host, activation mechanism of avian influenza virus H9N2 by furin, overview
physiological function
-
the multinucleated syncytial trophoblast, which forms the outermost layer of the placenta and serves multiple functions, is differentiated from and maintained by cytotrophoblast cell fusion. Cytotrophoblast cell fusion and syncytialization are accompanied by furin expression. Processing of type 1 IGF receptor by furin is an essential mechanism for syncytialization. Furin function is required for the development of syncytiotrophoblast structure in the labyrinth layer, as well as for normal embryonic development
physiological function
the multinucleated syncytial trophoblast, which forms the outermost layer of the placenta and serves multiple functions, is differentiated from and maintained by cytotrophoblast cell fusion. Cytotrophoblast cell fusion and syncytialization are accompanied by furin expression. Processing of type 1 IGF receptor by furin is an essential mechanism for syncytialization. Furin function is required for the development of syncytiotrophoblast structure in the labyrinth layer, as well as for normal embryonic development
physiological function
activation of viral glycoproteins or bacterial toxins, furin and other PCs contribute to the propagation of certain pathogenic viruses and to the toxicity of some bacteria
physiological function
CRISPR editing reveals that both furin and PC7 are functional in B16-F1 cells and able to substitute for each other during Notch1 and ADAM10 precursor processing
physiological function
furin is a calcium-dependent serine endoprotease that processes a wide variety of proproteins involved in cell function and homeostasis
physiological function
furin is a ubiquitous proprotein convertase that is involved in the processing (activation) of a wide variety of precursor proteins, including blood coagulation factors, cell surface receptors, hormones and growth factors, viral envelope glycoproteins, etc. and plays a critical regulatory role in a wide variety of cellular events
physiological function
morula compaction and inner cell mass formation depend on PC7 and the related proteases Furin and Pace4. These proteases jointly regulate cell-cell adhesion mediated by E-cadherin processing during blastocyst formation
physiological function
proprotein convertase furin is a highly specific serine protease modifying and thereby activating proteins in the secretory pathway by proteolytic cleavage. Its substrates are involved in many diseases, including cancer and infections caused by bacteria and viruses
physiological function
proprotein convertase substilisin/kexin-type (PCSK) enzymes regulate proprotein maturation by catalyzing the proteolytic cleavage of their substrates. The prototype PCSK furin is induced upon T cell receptor (TCR) activation, and its expression in T cells is critical for the maintenance of peripheral immune tolerance. Proprotein convertase furin regulates T cell receptor-induced transactivation. TGF-beta1 and NOTCH1 are synthesized initially as inactive precursors and are proteolytically activated during T cell activation. In Jurkat cells, furin is dispensable for immediate T cell receptor (TCR) signaling steps, such as ERK, ZAP70, or LAT phosphorylation. Furin regulates the expression of interleukin-2 in human Jurkat T cell lines, specific TGF-beta1-independent role for furin in interleukin-2 regulation. Furin activates specifically and nonredundantly the anti-inflammatory cytokine pro-TGF-beta1 and thus, directly modulates the activity of CD4+ and CD8+ T cells. Importantly, Furin regulates its own activity by autocleavage, and its mRNA and protein levels are modulated dynamically during alterations in T cell physiology. Furin does not affect TCR-induced immediate phosphorylation events in Jurkat T cells
physiological function
proprotein convertase substilisin/kexin-type (PCSK) enzymes regulate proprotein maturation by catalyzing the proteolytic cleavage of their substrates. The prototype PCSK furin is induced upon T-cell receptor (TCR) activation, and its expression in T cells is critical for the maintenance of peripheral immune tolerance. Proprotein convertase furin regulates T cell receptor-induced transactivation. TGF-beta1 and NOTCH1 are synthesized initially as inactive precursors and are proteolytically activated during T-cell activation. In Jurkat cells, furin is dispensable for immediate T-cell receptor (TCR) signaling steps, such as ERK, ZAP70, or LAT phosphorylation. Furin regulates the expression of interleukin-2 in human Jurkat T-cell lines, specific TGF-beta1-independent role for furin in interleukin-2 regulation. Furin activates specifically and nonredundantly the anti-inflammatory cytokine pro-TGF-beta1 and thus, directly modulates the activity of CD4+ and CD8+ T-cells. Importantly, Furin regulates its own activity by autocleavage, and its mRNA and protein levels are modulated dynamically during alterations in T-cell physiology
physiological function
proprotein convertases (PCs) are highly specific proteases required for the proteolytic modification of many secreted proteins. Calcium-dependent activity regulation of furin
physiological function
transforming growth factor beta (TGF-beta) is a signalling molecule that plays a key role in developmental and immunological processes in mammals. Pro-TGF-beta forms homodimers and is further processed in the trans-Golgi by a furin protease. Proteolytic cleavage by furin separates mature TGF-beta from latency-associated peptide (LAP). This dimeric complex is called the small latency complex (SLC) and keeps mature TGF-beta in an inactive form. Furin requires multiple processing steps and correct localization within the secretory pathway to become active
physiological function
-
furin is upregulated and cleaves certain substrates during hypoxia in cancer cells, the enzyme mediates brain-derived neurotrophic factor upregulation in cultured rat astrocytes exposed to oxygen-glucose deprivation. Maturation of brain-derived neurotrophic factor in astrocytes requires furin-mediated endoproteolytic processing of the precursor protein pro-brain-derived neurotrophic factor to brain-derived neurotrophic factor
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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
additional information
enzyme modeling by molecular dynamics calculations. Furin shows a complex activation mechanism and exists in at least four defined states: (i) the off state, incompatible with substrate binding as seen in the unliganded enzyme; (ii) the active on state seen in inhibitor-bound furin; and the respective (iii) calcium-free and (iv) calcium-bound forms. The transition from the off to the on state is triggered by ligand binding at subsites S1 to S4 and appears to underlie the preferential recognition of the four-residue sequence motif of furin. Ligation by calcium at the PC-specific binding site II influences the active-site geometry and determines the rotamer state of the oxyanion hole-forming Asn295, and adds a second level of the activity modulation of furin. Analysis of substrate induced structural rearrangements of furin, the spatial restrictions at and around the catalytic serine residue 368 of furin are structurally reminiscent of typical trypsin-like proteases, overview. Hotspots of conformational changes include the catalytic residues His194, Ser368, Asn295 of the oxyanion hole, the sodium binding site (Thr309 and Ser316), and residues in direct contact with the inhibitor peptide (e.g. the region Ser253-Pro256, the alignment template). Mapping of the Calpha displacement to the surface of the structure induced by inhibitor binding reveals a concerted local rearrangement at the substrate-binding cleft
additional information
X-ray structures of the proprotein convertase furin bound with substrate analogue inhibitors reveal substrate specificity determinants beyond the S4 pocket, overview. Substrate specificity is mediated at the P4-P6 binding sites of furin
Show AA Sequence and Transmembrane Helices (214 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
96000
additional information
additional information
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3 different forms, MW 81000, 83000 and 96000, may be produced by differential processing of a furin molecule and mature furin may be autocatalytically produced
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
2 * 53446, recombinant prodomain-processed, nonglycosylated aa108-574-TEV-FLAG-His6 N387D/N440D mutant, mass spectrometry
additional information
additional information
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secondary structure of furin prodomain protein, overview
additional information
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3 MW forms: MW 64000, 75000 and 86000, SDS-PAGE, COOH-terminal truncation is responsible for the different molecular mass forms
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
after autocleavage, proprotein convertases (PCs) exit the endoplasmatic reticulum. They remain bound to their inhibitory cleaved prosegments in latent form until arrival at the cell surface or, in the case of furin, in acidic endosomes, probably to avoid precocious activation or degradation of their substrates. Activated furin can then recycle from endosomes to the trans-Golgi network by binding to specific adaptors in the cytosol
glycoprotein
N-glycosylation is necessary for the proper folding and catalytic activity of plant produced or commercial human furin (NEB). Plant-produced human furin treated with PNGase F and Endo H does not exhibit cleavage activity. Similarly, when commercial human furin (NEB) is treated with commercial Endo H or PNGase F, no cleavage is observed for the substrate PA83
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme furin in complexes with inhibitors N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde, N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide, N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide, N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide, diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate, diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate, and diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate, vapor diffusion method, 9.0 mg/ml glycosylated human furin in 10 mm HEPES, pH 7.5, 100 mm NaCl, and 2 mm CaCl2 is mixed with an equal volume of crystallization solution containing 100 mm MES, 200 mm K/NaH2PO4, pH 5.5-6.0, and 2m NaCl, and equilibrated against reservoir solution with 3.0-3.6m NaCl, at 20°C, crystals are soaked for 16 h in soaking solution containing 3.13 M NaCl, 100 mM Mes/NaOH, pH 5.5, 200 mM NaH2PO4, 1 mM CaCl2, and 20% DMSO supplemented with inhibitor N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde (5 mM), N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide (5 mM), N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide (5 mM), N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide (5 mM), diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate (5 mM), diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate (1 mM), or diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate (1 mM), X-ray diffraction structure determination and analysis
purified furin in complex with a non-substrate-like small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, hexagonal crystals of unliganded furin are soaked in a 5 mM solution of inhibitor in 100 mM MES, pH 5.5, 200 mM K/NaH2PO4, 1 mM CaCl2, 10% DMSO, and 3.4 mM NaCl for 16 h, X-ray diffraction structure determination and analysis at 1.9 A resolution
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 30°C, 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
purified recombinant furin mutant N387D/N440D in nonglycosylated apo-form, vapor diffusion method, 400 nl of 6 mg/ml of apo-furin (aa108-574-TEV-FLAG-His6 N387D/N440D) in 10 mM HEPES, pH 7.5, 150 mM NaCl, and 5 mM CaCl2, is mixed with 400 nl of crystallization solution containing 11-13% PEG 8000, 0.11-0.16 M potassium dihydrogen phosphate, and 0.1 M HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 1.89 A resolution. The nonglycosylated furin protein reliably forms extremely durable apo crystals that diffract to high resolution, crystals are stable at 4°C for over one year. Digestion with TEV protease for the removal of the His6 and FLAG tags is not necessary for crystallization
purified recombinant His-tagged enzyme in complexes with three peptide-derived inhibitors, vapor diffusion method, mixing of 9 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, and 2 mM CaCl2, with an equal volume of crystallization solution containing 100 mM MES, 200 mM K/NaH2PO4, pH 5.5-6.0, 3-4 M NaCl, and 3% dimethyl sulfoxide, and equilibration against reservoir solution containing 3-4 M NaCl, 20°C, crystals are soaked for about 16 h in a soaking solution conatining 3.16 M NaCl, 100 mM MES/NaOH, pH 5.5, 200 mM Na/KH2PO4, and 1 mM CaCl2 and supplemented with 2 mM Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine, or 1 mM phenylacetyl-Cit-Val-Arg-4-aminomethyl-benzamidine, or 1 mM 4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
purified unliganded furin in different functional states, different Ca2+- and inhibitor (3-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(4-amidomethyl)-benzamidine)-bound forms of the enzyme, crystals of human furin are grown in sitting drops mixing equal volumes of 9 mg/ml protein solution and crystallization solution containing 100 mM MES, 200 mM K/NaH2PO4, pH 5.5-6.0, 3-4 M NaCl, and 3% v/v DMSO, the reservoir contains 3-4 M NaCl, for inhibitor binding studies the crystals are soaked with inhibitor and for calcium-studies the crystals are soaked with EDTA and Ca2+, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution
crystal structure of furin with bound decanoyl-Arg-Val-Lys-Arg-chloromethylketone inhibitor
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triclinic crystals, space group P1, unit cell dimensions a = 93.3 A, b = 135.4 A, c = 137.8 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H6
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H66L
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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
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profurin mutant, 80% reduced efficiency of propeptide excision, fails to be activated by acidic pH or trypsinolysis
H69L
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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
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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
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secondary cleavage sites are inactivated, is incapable of self-activation
R1584A/R1585A
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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
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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
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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
DELTA759-780
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furin mutant lacking both the YKGL motif and the acidic cluster, shows low-affinity interactions with Mint3
DELTA769-780
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furin mutant with a deleted acidic cluster, shows low-affinity interactions with Mint3
R138A
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mutation of the furin cleavage site in the gamma subunit, gamma furin site mutation interfers with protein synthesis and/or degradation
R205A/R231A
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mutation of the furin cleavage site in the alpha subunit, eliminates the appearance of the 65-kDa cleavage product at the cell surface
additional information
additional information
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in furin-deficient DF11 cells, release of Borna disease virus particles induced by the treatment of Borna disease virus-infected cells with hypertonic buffer is not significantly affected, while virion infectivity is dramatically impaired, correlating with the decreased incorporation of Borna disease virus glycoprotein species into viral particles
additional information
loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
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loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
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the zebrafish craniofacial mutant sturgeon in the proprotein convertase FurinA displays mild blisters in the median fin folds
additional information
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FD11 cell line, deficient in furin protease, processing of furin-site-containing glycoproteins is abrogated
additional information
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furin cleavage-site mutant, neither trifluoperazine-induced nor basal shedding causes P-stalk accumulation
additional information
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point mutations of sites A, B and C of furin P1A promoter. Mutations of site A and more importantly site B decreases Sox9-induced promoter activity, while mutations of both A and B sites result in only slight but nonsignificant additional inhibition. Mutation of site C does not reduce Sox9 activity
additional information
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construction of an immunoproapoptotic molecule with antitumor activity: Her2-antigen e23sFv-TD-tBID with a 10-amino acid residue furin cleavage sequence. Purified e23sFv-TD-tBID protein recognized breast cancer cells from patients and preserved the ability to kill HER2-positive tumor cells after incubation in human serum
additional information
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furin-deficient LoVo cells are uncapable to process pro-B-type natriuretic peptide, coexpression of human wild-type furin compensates and results in effective pro-B-type natriuretic peptide cleavage. Suppression of furin in HEK-293 cells by siRNA leads to the same result, overview
additional information
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knockdown of furin expression by siRNA significantly inhibits invasion and migration of HTR8/SVneo cells, with corresponding decrease of matrix metalloproteinase-9, MMP-9, activities. In contrast, overexpression of furin markedly increases cell invasion and migration, accompanied by significant increase of MMP-9 activities. Furthermore, furin siRNA significantly increases the levels of both tissue inhibitors of MMPs, TIMP-1 and -2, overview. Proliferation of HTR8/SVneo cells is inhibited by furin siRNA
additional information
enhancement of productive IBV infection by knockin of furin in A-549 cells
additional information
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enhancement of productive IBV infection by knockin of furin in A-549 cells
additional information
furin siRNA efficiently inhibits furin expression, expression of enzyme-specific siRNA in choriocarcinoma cells inhibits cell fusion
additional information
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furin siRNA efficiently inhibits furin expression, expression of enzyme-specific siRNA in choriocarcinoma cells inhibits cell fusion
additional information
knockdown of the enzyme expression in C8161.9, MelJuSo, and HeLa cells by shRNA
additional information
engineering of the human furin gene for expression in plants, the production of a functional active recombinant truncated human furin in Nicotiana benthamiana plants. The signal peptide (amino acids 1-25) is removed from the furin sequence, and Nicotiana tabacum PR-1a signal peptide (MGFVLFSQLPSFLLVSTLLLFLVISHSCRA) is added to the N-terminus. The KDEL sequence (the endoplasmic reticulum retention signal) and the His6 tag (the affinity purification tag) are added to the C-terminus. A truncated form of furin (amino acids 26-595) is expressed with a PR-1a signal peptide at N-terminus and His6-KDEL at C-terminus
additional information
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engineering of the human furin gene for expression in plants, the production of a functional active recombinant truncated human furin in Nicotiana benthamiana plants. The signal peptide (amino acids 1-25) is removed from the furin sequence, and Nicotiana tabacum PR-1a signal peptide (MGFVLFSQLPSFLLVSTLLLFLVISHSCRA) is added to the N-terminus. The KDEL sequence (the endoplasmic reticulum retention signal) and the His6 tag (the affinity purification tag) are added to the C-terminus. A truncated form of furin (amino acids 26-595) is expressed with a PR-1a signal peptide at N-terminus and His6-KDEL at C-terminus
additional information
expression and purification of nonglycosylated human furin using the BacMam technology and site-directed mutagenesis of the glycosylation sites. Recombinant nonglycosylated furin produced using this system retains full proteolytic activity indistinguishable from that of the glycosylated protein
additional information
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expression and purification of nonglycosylated human furin using the BacMam technology and site-directed mutagenesis of the glycosylation sites. Recombinant nonglycosylated furin produced using this system retains full proteolytic activity indistinguishable from that of the glycosylated protein
additional information
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LoVo/neo cells lacking functional furin are unable to activate both wild type Shiga toxin and mutant Shiga-2D toxin
additional information
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deletion of the cysteine-rich domain and the cytoplasmic tail of furin does not abolish binding to cripto
additional information
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production of lentiviruses carrying shRNA for furin and infection of blastocyststage embryos with the viruses, along with lentiviruses expressing EGFP
additional information
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the binding efficiency of the furin mutants LI/AN Y/A and LI/AN F/N Y/A to Mint3 decrease
additional information
truncated mutant, lacking Cys-rich repeated segments
additional information
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truncated mutant, lacking Cys-rich repeated segments
additional information
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furin antisense expression leading to furin depletionin oocytes is accompanied by a corresponding decrease in the levels of both the fully cleaved prodomain and mature BMP4
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 mg/ml bovine serum albumin, less than 5% loss of activity after 2 months
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-70°C, 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
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4°C, 5 mg/ml bovine serum albumin, 0.02% NaN3, less than 5% loss of activity after 2 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification protocol combining the heterologous expression of furin from CHO cells with an affinity step that efficiently extracts only active furin from the conditioned medium by using furin-specific inhibitor moieties as bait. The best affinity tag used, biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-4-amidinobenzylamide coupled to streptavidin-Sepharose beads, is used in a three-step chromatographic protocol and routinely results in a high yield of a homogeneous furin preparation with a specific activity of about 60 units/mg protein
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recombinant enzyme 300fold from HEK-293 cells by metal affinity chromatography, inhibitor based affinity chromatography, and gel filtration
recombinant FLAG/His6-tagged furin ectodomain from CHO cells or Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, ultrafiltration, and gel filtration, to homogeneity
recombinant glycosylated His-tagged furin from HEK-293S cells by nickel affinity and inhibitor affinity chromatography, followed by gel filtration
recombinant His6-tagged enzyme from Nicotiana benthamiana leaves by nickel affinity chromatography, co-purification of the coexpressed proteins
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned into vector pAdTrack-CMV, followed by recombination in Escherichia coli cells with the adenovirus backbone pAdEasy-1, recombinant DNA transfected to HEK-293 cells. Introduction by adenovirus vector in LoVo cells
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cDNA sequenced, cloned from a cDNA library of Sf9 cells, overexpressed from a baculovirus vector in Sf9 cells
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)
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DNA and amino acid sequence determination of neuropeptides and expression profiling, overview
expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
full-length epitope-tagged furin constructs or mutants expressed in A7 cells or BSC-40 cells
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full-length furin prodomain overexpressed in Escherichia coli strain BL21 (DE3)
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functional recombinant expression of His6-tagged human furin lacking its signal peptide in Nicotiana benthamiana plants. Plant-produced human furin is highly active both in vivo and in vitro and specifically cleaves the tested target proteins, factor IX (FIX) and protective antigen (PA83). Plants lack some of the important posttranslational modifications, including furin processing, but both, enzymatic deglycosylation and proteolytic processing of target proteins, can be achieved in vivo by coexpression of deglycosylating and furin cleavage enzymes in a single cell to produce deglycosylated and furin processed target proteins. Recombinant coexpression of engineered enzyme and substrate using the Agrobacterium tumefaciens strain AGL1 transfection method, expression in leaves. Coexpression of human furin with PA83 of Bacillus anthracis and deglycosylation enzymes Endo H or PNGase F in Nicotiana benthamiana. Deglycosylation efficiency of plant produced Endo H is greater than that of plant produced PNGase F. When full length furin is coexpressed with the PA83 protein in Nicotiana benthamina plants, there is little or no cleavage of PA83. Plant-produced human furin treated with PNGase F and Endo H does not exhibit cleavage activity
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
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furin cDNA ligated into a modified pCEP-Pu vector carrying a 5'-SPARC/BM40 signal peptide and a 3'-FLAG tag. HEK 293-EBNA cells cotransfected with full-length alpha1(XXIII) or furin cDNA and phosphatidylinositol-linked placental alkaline phosphatase or human transferrin receptor cDNA, respectively
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furin expression in CHO cells, COS-7 cells, furin-deficient FD11 cells, and furin-overexpressing cells
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furin mutant and wild-type constructs transiently transfected into HEK-293 cells
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furin precursor cDNA transferred to pcDNA3.1-. Co-expression of furin-site-containing spike glycoprotein with furin cDNA in FD11 cells or CHO cells
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gene FURIN, quantitative RT-PCR expression analysis
gene FURIN, recombinant expression of glycosylated aa108-574-TEV-FLAG-His6-furin and nonglycosylated aa108-574-TEV-FLAG-His6 N387D/N440D furin mutant (ectodomains with a TEV cleavage site) from plasmid termed furin aa1-574 in CHO cells and in Spodoptera frugiperda Sf9 cells via BacMam virus transfection, typically producing a highly glycosylated, heterogeneous protein
HEK-293 cells transiently cotransfected with cDNA encoding V5-tagged wild-type PCSK9 and furin
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HepG2 cells transiently transfected with furin luciferase reporter constructs pGL2-P1, pGL2-P1A and pGL2-P1B
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LoVo cells stably expressing furin. Furin cleavage-site mutant (LNTR) transfected into COS-7 cells
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MDA-MB-231 breast cancer cells stably transfected with a vector containing furin prosegment
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mutants expressed in Sf9 cells. Mutant constructs transiently transfected in LoVo cells
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PC1, DNA and amino acid sequence determination and analysis, phylogenetic tree
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PCR product of the truncated mutant inserted between the EcoR1 and Not1 sites of the pFastBac1H vector, expression in Tn5 cells
plasmid pCMV-furin expressed in HeLa cells. Catalytic domain, P domain and cytoplasmic domain of furin subcloned from full-length pCMV-furin and ligated in-frame to the C-terminus of GST using the PGEX-6P system
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recombinant hfurin from the sectreted culture media of somatomammotroph GH4C1 cells following infection with respective cDNA encoding vaccinia viruses
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soluble ectodomain of furin is expressed in dihydrofolate reductase-amplified CHO cells
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stably transfected LoVo cells expressing either furin (LoVo/fur) or the vector alone (LoVo/neo)
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the distribution of proprotein convertase activities at the tissue level are monitored by introduction of biosensor CLIP (cell-linked indicator of proteolysis). CLIP v.3 is suitable for ratiometric imaging without interference by FRET, whereas CLIP v.4 can be used as a FRET-based biosensor to quantify PC activities in specific intracellular vesicles, enzyme and CLIP expression in HEK-293T cells. Fusion to the cytosolic tail of PC7 directs CLIP v.4 to compartments that harbor furin activity, but not full-length proprotein convertase 7 (PC7)
transient co-expression of human furin and human TGF-beta1 in the presence of the latency-associated peptide (LAP) in Nicotiana benthamiana leaves processing of the latent complex by a furin-like protease does not occur in planta. The use of a chitinase signal peptide enhances the expression and secretion of LAP-TGF-beta1, and co-expression of human furin enables the proteolytic processing of latent TGF-beta1 into a biologically active protein. Mature TGF-beta1 can be expressed without LAP, but results in necrosis (due to improper signal peptide cleavage). The Fc portion of immunoglobulin alpha 1 (Fcalpha), a natural dimer, is used as a fusion partner allowing dimerization of TGF-beta1. Furin requires multiple processing steps and correct localization within the secretory pathway to become active. Biological activity of Fcalpha-TGF-beta1 in crude plant extracts is assessed in a cell-based assay using mink lung epithelial cells carrying a TGF-beta-responsive luciferase reporter gene that is activated upon binding to the TGF-beta receptor. Proteolytic processing of LAP-TGF-beta1 in plants requires co-expression of furin
transient expression of homogeneously glycosylated His-tagged furin in HEK-293S cells
transient expression of the enzyme in HEK-293 cells, co-expression of inhibitor mutant alpha1-antitrypsin M352R
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cytokine transforming growth factor TGF-beta stimulates furin mRNA expression in HepG2 cells
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furin expression is detected in all rhabdomyosarcoma cell lines tested at high levels, while myoblasts and fibroblasts show low levels of furin transcripts
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furin expression is upregulated by the Th1 hallmark cytokine interleukin-12. T cell activation via T cell receptor induces furin expression
furin expression is upregulated by the Th1 hallmark cytokine interleukin-12. T-cell activation via T-cell receptor induces FURIN expression
in heaptitis C virus-infected cells, furin expression is upregulated about 3fold
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the enzyme is induced by forskolin and amphiregulin, periovulatory furin expression is also increased by human chorionic gondotropin in follicles, overview
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the enzyme is upregulated and cleaves certain substrates during hypoxia in cancer cells. In oxygen-glucose deprivation, expression of the enzyme and of brain-derived neurotrophic factor is upregulated
the enzyme is upregulated and cleaves certain substrates during hypoxia in cancer cells. In oxygen-glucose deprivation, expression of the enzyme and of brain-derived neurotrophic factor is upregulated
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the enzyme is upregulated and cleaves certain substrates during hypoxia in cancer cells. In oxygen-glucose deprivation, expression of the enzyme and of brain-derived neurotrophic factor is upregulated
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
industry
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furin may be applied in mass production of a potent antimicrobial peptide histonin as a natural form, whereby overcoming its inherent toxicity and the low yield of production
medicine
pharmacology
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development of an immunoproapoptotic molecule with antitumor activity: Her2-antigen e23sFv-TD-tBID with a 10-amino acid residue furin cleavage sequence. e23sFv-TD-tBID shows therapeutic value to humans by its cytotoxic effects on primary patient-derived breast tumor cells but not on endothelial cells. It also shows in vivo antitumor activity in female BALB/c athymic mice, overview
additional information
analysis
-
bioluminogenic probes can specifically image furin activity in xenografted breast cancer tumors in mice
analysis
-
sensitive and specific assay for furin activity using an antibody capture step to immobilise furin from whole cell lysates. The assay has a minimum detection limit of 0.006 nM and is sensitive enough to determine the furin activity of many of the cell lines tested
drug development
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extensive clinical use, high bioavailability and relatively low toxicity of dicoumarols suggests that the dicoumarol structure will be a good starting point for development of drug-like inhibitors of furin and other proprotein convertases that can act both intracellularly and at the cell surface
drug development
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good prospect of using quantitative structure-activity relationship models for the rational design of novel therapeutic furin inhibitors toward anthrax and furin-dependent diseases
drug development
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furin is considered a major target for intervention of cancer, tumorgenesis, viral and bacterial pathogenesis
drug development
furin inhibitors are promising therapeutics for the treatment of cancer and numerous infections caused by bacteria and viruses, including the highly lethal Bacillus anthracis or the pandemic influenza virus
drug development
the activation of viral glycoproteins by the host protease furin is an essential step in the replipation of numerous pathogenic viruses. Thus, effective inhibitors of furin can serve as broad-spectrum antiviral drugs, rational design of various types of cyclic inhibitors
drug development
the deglycosylated active recombinant enzyme can be used for structure-guided drug discovery
medicine
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potential therapeutic value of furin inhibitors, alpha1-PDX is able to block in vivo maturation of pro-gB, the cytomegalovirus envelope glycoprotein
medicine
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copper and zinc complexes of terpyridine derivatives are stable under various conditions and are not expected to pose delivery problems, qualities vital for the development of a wide-scope anti-bioterror agent for civil and military uses
medicine
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cell-to-cell spread of Borna disease virus requires neither the expression of cellular receptors involved in virus primary infection, nor the furin-mediated processing of Borna disease virus glycoprotein
medicine
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furin is predominantely expressed in tumors from patients surviving less than five years. Furin may constitute a marker for ovarian tumor progression and may contribute to predict the outcome of the disease
medicine
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furin-like protease activity may be involved in mediating host-parasite interactions. Inhibition of infection is due to an effect on the parasite-derived furin activity rather than the host cell furin
medicine
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inhibiting furin-like proprotein convertases protects the host from the distinct furin-dependent infections and lay a foundation for novel, host cell-focused therapies against acute diseases
medicine
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inhibiting furin-like proprotein convertases protects the host from the distinct furin-dependent infections and lay a foundation for novel, host cell-focused therapies against acute diseases
medicine
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interleukin 12 induction of furin plays a role in interferon gamma protein regulation and control of T helper 1 cell differentiation
medicine
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interleukin 12 induction of furin plays a role in interferon gamma protein regulation and control of T helper 1 cell differentiation
medicine
-
introduction of a prototypic furin recognition motif at R667 of the SARS coronavirus spike glycoprotein allows for efficient cleavage of the mutant glycoprotein and increases cell-cell fusion activity but shows no effect on virion infectivity
medicine
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massive vaccination of host poultry results in an influenza variant Fujian-like H5N1 strain with two mutations at the furin-processing site of hemagglutinin, which is resistant to immunization
medicine
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pivotal role for furin, MT1-MMP, and MMP2 in tumor necrosis factor alpha-induced sphingolipid signaling. This system may be a possible target to inhibit smooth muscle cell proliferation in vascular diseases
medicine
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some mutations of H5N1 H5 cleavage sequence fit less well into furin and hence may reduce the high pathogenicity of the H5N1 virus
medicine
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specific and opposing roles of furin and PACE4 in the regulation of MMP-9/TIMP-1 mediated cell motility and invasion. Furin prosegment inhibits cell migration and invasion as well as MMP-9 activity without affecting TIMP-1. It prevents adequate repair of scratch wounds
medicine
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furin expression is detected in all rhabdomyosarcoma cell lines tested at high levels, while myoblasts and fibroblasts show low levels of furin transcripts. Peptide CMGTINTRTKKC has strong affinity for rhabdomyosarcoma cells in vitro and in vivo, by binding to furin
medicine
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hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells. Exposing these cells back to normoxic conditions reverses furin redistribution, suggesting that the tumor microenvironment modulates furin trafficking in a highly regulated manner. Both Rab4GTPase-dependent recycling and interaction of furin with the cytoskeletal anchoring protein, filamin-A, are essential for the cell surface relocalization of furin. Interference with the association of furin with filamin A, prevents cell surface relocalization of furin and abolishes the ability of cancer cells to migrate in response to hypoxia
medicine
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increased replication of heaptitis C virus RNA in hepatitis C-infected cells is significantly reduced in the presence of transforming growth factor TGF-beta1 siRNA, thrombospondin-1 siRNA or furin siRNA
medicine
-
peptide CMGTINTRTKKC has strong affinity for rhabdomyosarcoma cells in vitro and in vivo, by binding to furin. Treatment of rhabdomyosarcoma cells in mice with doxorubicin coupled to the targeting peptide results in a two-fold increase in therapeutic efficacy compared to doxorubicin treatment alone. Surface-furin binding may be used as novel mechanism for therapeutic cell penetration
medicine
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inhibiting furin-like proprotein convertases protects the host from the distinct furin-dependent infections and lay a foundation for novel, host cell-focused therapies against acute diseases
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additional information
compartment-specific biosensors can be used to gain insight into the regulation of proprotein convertase trafficking and to map the tropism of PC-specific inhibitors
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Release 2023.1 (January 2023)
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