Information on EC 3.4.21.75 - Furin

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.21.75
-
RECOMMENDED NAME
GeneOntology No.
Furin
-
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
show the reaction diagram
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys, releases albumin, complement component C3 and von Willebrand factor from their respective precursors, the term -+- depicts the point of cleavage
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
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SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Bfurin
-
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Dibasic processing enzyme
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-
-
-
furin
-
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furin convertase
synthetic construct
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furin protease
-
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furin-like prohormone convertase
-
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furin-like proprotein convertase
-
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furin-like protease
-
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furin-like protease
-
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FurinA
-
-
furinase
-
-
hfurin
-
-
PACE
-
-
-
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Paired basic amino acid cleaving enzyme
-
-
-
-
Paired basic amino acid converting enzyme
-
-
-
-
Paired basic amino acid residue cleaving enzyme
-
-
-
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PC1
-
-
-
-
PC1/3
-
-
PCSK3
-
-
proconvertase
-
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prohormone convertase
-
-
-
-
prohormone convertase
-
prohormone convertase
-
-
prohormone convertase
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prohormone convertase 1
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prohormone convertase 1
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prohormone convertase 2
-
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Proprotein convertase
-
-
-
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Proprotein convertase
-
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Proprotein convertase
-
Proprotein convertase
Mus musculus C57BL/6
-
-
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Proprotein convertase
synthetic construct
-
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proprotein convertase subtilisin/kexin type 3
-
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proprotein convertase subtilisin/kexin type3
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Serine proteinase PACE
-
-
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sheddase
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SPC3
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subtilisin-like proprotein convertase
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subtilisin-like protein convertase
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Trans golgi network protease furin
-
-
-
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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; 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
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also cf. EC 3.4.21.93. Prohormone convertases are calcium-dependent serine endoproteases of the subtilisin family
additional information
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furin belongs to MEROPS clan SB, family S8
additional information
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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; 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; one of a group of subtilisin homologues structurally and functionally similar to kexin
CAS REGISTRY NUMBER
COMMENTARY
141760-45-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
overview
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Manually annotated by BRENDA team
gene furina
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Manually annotated by BRENDA team
at least 3 related enzymes are recognized in mammals: PC2
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Manually annotated by BRENDA team
at least 3 related enzymes are recognized in mammals: PC2; at least 3 related enzymes are recognized in mammals: PC3 (identical with PC1)
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-
Manually annotated by BRENDA team
at least 3 related enzymes are recognized in mammals: PC2; at least 3 related enzymes are recognized in mammals: PC3 (identical with PC1); at least 3 related enzymes are recognized in mammals: PC4
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Manually annotated by BRENDA team
at least 3 related enzymes are recognized in mammals: PC3 (identical with PC1)
-
-
Manually annotated by BRENDA team
overview
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Manually annotated by BRENDA team
rat somatomammotroph cell line, GH4C1 infected with vaccinia virus recombinants of human PC1
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Manually annotated by BRENDA team
recombinant
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Manually annotated by BRENDA team
C57/BL6 mice
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Manually annotated by BRENDA team
expression in Chinese hamster ovary cells
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Manually annotated by BRENDA team
expression in Chinese hamster ovary cells; truncated form
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Manually annotated by BRENDA team
rat somatomammotroph cell line, GH4C1 infected with vaccinia virus recombinants of murine PC1
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Manually annotated by BRENDA team
recombinant
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-
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57/BL6 mice
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Manually annotated by BRENDA team
female Sprague-Dawley rats
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-
Manually annotated by BRENDA team
rat SPC3 cDNA expressed in a mouse L cell line
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Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
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Manually annotated by BRENDA team
synthetic construct
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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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
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molecular evolution of enzyme function in the proprotein convertase family, overview
evolution
-
furin is a member of the pro-hormone/pro-protein convertase family of subtilisin-like endoproteinases
evolution
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furin is a member of the proprotein convertase family
evolution
-
the enzyme belongs to the family of serine proteases
evolution
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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
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furin is a member of the subtilisin-like proteases and belongs to the proprotein convertase subtilisin/kexin-like proteases, subgroup PCSK3
evolution
-
the enzyme belongs to the proprotein convertase family of proteases
evolution
-
the enzyme is a member of the subtilisin-like proprotein convertase family
malfunction
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furin inhibition leads to a 38% reduction of oocyte release from ovaries, overview
malfunction
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
malfunction
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blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview
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
-
furin is involved in many physiological and pathological processes
malfunction
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furin is linked to cancer, tumorgenesis, and viral and bacterial pathogenesis
malfunction
-
furin-specific siRNAs or inhibitors inhibit cell fusion in choriocarcinoma BeWo cells, as well as trophoblast syncytialization in human placental explants
malfunction
-
placenta-specific knockdown of furin in the mouse leads to severe defects in syncytialization and embryonic lethality, phenotype, overview
malfunction
-
furin inhibition reduces brain-derived neurotrophic factor maturation and secretion
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 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
-
knockdown of the enzyme expression in C8161.9, MelJuSo, and HeLa cells by shRNA leads to reduced or complete loss of KISS1 processing
malfunction
-
ablation of productive infectious bronchitis virus, IBV, infection by knockdown of furin expression in H1299 cells
metabolism
-
the enzyme activates large numbers of proprotein substrates and is ubiquitously expressed and implicated in many physiological and pathological processes
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
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the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 7fold
physiological function
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 30fold
physiological function
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the enzyme plays a key role in the posttranslational processing of precursors for bioactive peptides
physiological function
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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 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
-
bone morphogenetic proteins, BMPs, require proteolytic activation by members of the proprotein convertase family
physiological function
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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
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furin is involved in many physiological and pathological processes, it plays a role in human trophoblast invasion and migration
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
-
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
-
furin is involved in processing of bone morphogenetic protein BMP10. Processing occurs mostly intracellularly, but also at the cell surface
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
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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, 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
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
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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
-
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
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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
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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
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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 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 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
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furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure, overview
physiological function
-
furin mediates maturation of bone morphogenetic protein-4
metabolism
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cellular furin content might be a potential factor determining the susceptibility of cultured human and animal cells to coronavirus infectious bronchitis virus infection
additional information
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alpha1-PDX blocks cleavage of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase, probably PC7, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
show the reaction diagram
-
-
-
-
2-amino benzoyl-AEQDRNTREVFAQ-T(3-nitro-tyrosine)-A + H2O
2-amino benzoyl-AEQDRNTR + EVFAQ-T(3-nitro-tyrosine)-A
show the reaction diagram
-
furin-mediated cleavage of a fluorogenic peptide derived from hSARS-CoV spike protein
-
?
2-aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
show the reaction diagram
-
-
-
-
-
Abz-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-GIRRKRSVSHQ-EDDnp + H2O
Abz-GIRRKR + SVSHQ-EDDnp
show the reaction diagram
-
-
-
?
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GIRRKR + SVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Rous sarcoma viral envelope glycoprotein
-
?
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GRRTRR + EAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Zaire viral envelope glycoprotein
-
?
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HHRQRR + SVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human A disintegrin and metalloproteinase with thrombospondin ADAM-TS 6
-
?
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HKREKR + QAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human bone morphogenetic protein hBMP-2
-
?
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRREKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 2 viral envelope glycoprotein
-
?
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRRQKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 3 viral envelope glycoprotein
-
?
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-KIRRRR + DVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-6A viral envelope glycoprotein
-
?
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-LKRRRR + DTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Borna disease viral envelope glycoprotein
-
?
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-NLRRRR + DLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-6B viral envelope glycoprotein
-
?
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RERRRKKR + GLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
?
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RKRSRR + QVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Sudan viral envelope glycoprotein
-
?
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRAKR + SPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human bone morphogenetic protein hBMP-4
-
?
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRDKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Dengue 4 viral envelope glycoprotein
-
?
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLfGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from the H5N1 influenza hemagglutinin processing site
-
?
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
?
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + SLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
?
Abz-RVKRGLAY(NO2)D-OH + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-SGRSRRAIDLQEDDnp + H2O
Abz-SGRSRR + AIDLQEDDnp
show the reaction diagram
-
-
-
?
Abz-SKRSRRSVSVQ-EDDnp + H2O
Abz-SKRSRR + SVSVQ-EDDnp
show the reaction diagram
-
-
-
?
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SKRSRR + SVSVQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Japan beta-encephalitis viral envelope glycoprotein
-
?
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRHKR + FAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from measle virus Fo viral envelope glycoprotein
-
?
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + DVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Ebola Ivory Coast viral envelope glycoprotein
-
?
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + SASTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from Herpes HHV-8 viral envelope glycoprotein
-
?
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SSRHRR + ALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from human transforming growth factor TGF-beta3
-
?
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-TRRFRR + SITEQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
FRET-peptide derived from infectious bronchitis viral envelope glycoprotein
-
?
Ac-AAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AAKYKR
show the reaction diagram
-
-
-
?
Ac-AARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AARYKR
show the reaction diagram
-
-
-
?
Ac-Arg-Val-Arg-Arg-4-nitroanilide + H2O
Ac-Arg-Val-Arg-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
Ac-KARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-KARYKR
show the reaction diagram
-
-
-
?
Ac-RA-norvaline-YKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RA-norvaline-YKR
show the reaction diagram
-
-
-
?
Ac-RAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RAKYKR
show the reaction diagram
-
-
-
?
Ac-RARYAR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYAR
show the reaction diagram
-
-
-
?
Ac-RARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYKR
show the reaction diagram
-
-
-
?
Ac-RARYRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYRR
show the reaction diagram
-
-
-
?
Ac-RYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRR
show the reaction diagram
-
-
-
?
Ac-RYRFKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRFKR
show the reaction diagram
-
-
-
?
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Acetyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
show the reaction diagram
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
show the reaction diagram
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
?
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
AcRARYKK-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + AcRARYKK
show the reaction diagram
-
-
-
?
ADAMTS9 propeptide + H2O
?
show the reaction diagram
-
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, ADAMTS is a disintegrin and metalloprotease domain with thrombospondin type 1 repeats
-
-
?
alpha-Subunit of the rat endopeptidase-24.18 + H2O
?
show the reaction diagram
-
-
-
-
-
anthrax protective antigen + H2O
?
show the reaction diagram
synthetic construct
-
-
-
-
?
anthrax protective antigen precursor + H2O
?
show the reaction diagram
-
-
-
-
?
anthrax protective antigen-83 + H2O
anthrax protective antigen-63 + ?
show the reaction diagram
-
-
-
?
anthrax protective antigen-83 + H2O
?
show the reaction diagram
-
-
-
-
?
avian influenza virus A hemagglutinin + H2O
?
show the reaction diagram
-
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
Boc-RVRR-4-methylcoumarin 7-amide + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Boc-RVRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Boc-RVRR
show the reaction diagram
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Carboxybenzyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
chimeric transforming growth factor-beta1/beta2 + H2O
?
show the reaction diagram
synthetic construct
-
consists of the transforming growth factor-beta1 LAP region, the transforming growth factor-beta2 cleavage site and the transforming growth factor-beta2 mature peptide, efficiently cleaved
-
-
?
CPA95 + H2O
?
show the reaction diagram
-
-
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
show the reaction diagram
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316, peptide-derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
?
duck carboxypeptidase D + H2O
?
show the reaction diagram
-
i.e. DCPD, duck carboxypeptidase D acts as species-specific docking receptor for the duck hepatitis B virus. No cleavage of recombinant DCPD expressed in LMH cells
-
-
?
duck hepatitis B virus large envelope pre-S protein + H2O
?
show the reaction diagram
-
the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus
-
-
?
epithelial Na+ channel + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
-
?
epithelial Na+ channel + H2O
?
show the reaction diagram
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
extracellular superoxide dismutase + H2O
?
show the reaction diagram
-
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
show the reaction diagram
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview, 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
-
-
?
glycoprotein 160 + H2O
?
show the reaction diagram
-
from HIV-1, low activity
-
-
?
gp40/15 + H2O
gp40 + gp15
show the reaction diagram
-
cleaves recombinant Cryptosporidium parvum and Cryptosporidium hominis gp40/15. Putative furin cleavage site RSRR
-
?
gp40/15 + H2O
gp40 + gp15
show the reaction diagram
-
putative furin cleavage site RSRR
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
show the reaction diagram
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
?
hBMP-2 precursor protein + H2O
?
show the reaction diagram
-
cleavage sites are HKREKR-/-QAKH and HVRISR-/-SLHQ
-
-
?
hBMP-4 precursor protein + H2O
?
show the reaction diagram
-
cleavage sites are RRRAKR-/-SPKH and HVRISR-/-SLPQ
-
-
?
hemagglutinin + H2O
?
show the reaction diagram
-
-
-
-
?
hemagglutinin + H2O
?
show the reaction diagram
-
from avian influenza H5N1 virus, high activity
-
-
?
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O
?
show the reaction diagram
-
hemagglutinin loop of high pathogenic avian influenza virus subtype H5 binds much more tightly into the catalytic site of furin than the hemagglutinin low pathogenic avian influenza virus subtype H3 and hemagglutinin low pathogenic avian influenza virus subtype H5 systems. The -RRRKK- insertion in the hemagglutinin high pathogenic avian influenza virus subtype H5 in particular two arginines at S4 and S6 positions helps directly to hold the hemagglutinins cleavage loop in place by forming many strong hydrogen bonds between residues of hemagglutinin and furin
-
-
?
hemagglutinin low pathogenic avian influenza virus subtype H3 + H2O
?
show the reaction diagram
-
-
-
-
?
hemagglutinin low pathogenic avian influenza virus subtype H5 + H2O
?
show the reaction diagram
-
-
-
-
?
heparan sulfate 6-O-endosufatase Sulf2 + H2O
?
show the reaction diagram
-
cleavage at arginine 570, located in the consensus sequence for the cleavage by furin-type proprotein convertases. The consensus sequence of the cleavage by furin and PCs is R/K-X-R/K-X-R/K-R-/-X. R, K, X, and denote arginine, lysine, any amino acid. Proteolytic processing of SulfFP2 protein by furin and furin-like proprotein convertases, and activity with Sulf2 truncation and exchange mutants, overview
-
-
?
hepatitis B e antigen precursor + H2O
?
show the reaction diagram
-
-
-
-
?
hepatitis B e antigen precursor + H2O
?
show the reaction diagram
-
furin can cleave the RRDR, RRGR, and RSPR motifs
-
-
?
high pathogenic H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
furin can only cleave the high pathogenic hemagglutinin. It generates most of its selectivity through interactions with subsites P1, P4, and P6, with interactions at P2 being less important and little preference at P3, P5, P7, and P8. The S1, S4, and S6 pockets are specifically designed to accommodate arginine, with lysine substitution fitting less well in different degrees
-
-
?
highly pathogenic Queretaro H5N2 hemagglutinin + H2O
?
show the reaction diagram
-
only processed in the presence of heparin
-
-
?
histonin + H2O
?
show the reaction diagram
-
furin releases intact histonin monomers from F4-multimeric histonin (12-mer). Histonin has an RLKR motif at the C-terminus after which furin cleaves specifically
-
-
?
HIV-1 gp160 + H2O
?
show the reaction diagram
-
13mer and 19mer peptides digested equally well by furin at site1, showing complete processing at 5 h. 41mer and 51mer peptides are either barely or unprocessed, respectively. Product inhibition does not explain inability of furin to process the 41mer and 51mer peptides. Extended sequences require heparin for optimal processing
-
-
?
HIV-1 Tat protein + H2O
?
show the reaction diagram
-
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, furin cleaves full-length Tat protein between amino acid 56 and 57, irrespective of seuence differences at amino acid 57
-
-
?
human semaphorin 3F + H2O
?
show the reaction diagram
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview, 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
-
-
?
IBV spike protein + H2O
?
show the reaction diagram
-
-
-
-
?
inactive pro-MT1-MMP + H2O
active MT1-MMP + ?
show the reaction diagram
-
-
-
?
influenza deltaK-Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
76% processed
-
-
?
influenza Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
70% processed
-
-
?
influenza variant Fujian-like H5N1 hemagglutinin + H2O
?
show the reaction diagram
-
mutations at the furin-processing site of the hemagglutinin, is less cleaved (38%) by furin as compared to the parent Fujian-like strain derived peptides
-
-
?
insulin-like growth factor-1 receptor + H2O
?
show the reaction diagram
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
lethal factor inhibitor 2 + H2O
?
show the reaction diagram
-
-
-
-
?
membrane type-1 matrix metalloproteinase + H2O
?
show the reaction diagram
-
-
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
show the reaction diagram
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
?
membrane-bound collagen XXIII + H2O
shed collagen XXIII
show the reaction diagram
-
furin is the major protease to process collagen XXIII. Processing occurs after the downstream recognition motif 94KIRTVR99, releasing the ectodomain
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
show the reaction diagram
-
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, there are two furin cleavage motifs, R89-R-P-R-C93 and R108-R-K-R-Y112
-
-
?
membrane-type 1-matrix metalloproteinase + H2O
?
show the reaction diagram
-
-
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
show the reaction diagram
-
production of mature growth hormone-releasing hormone from pro-growth hormone-releasing hormone is a stepwise process mediated predomionantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus, furin is the most efficient convertase in cleaving the N-terminal RXXR/RXRR site
-
-
?
N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
nodal + H2O
?
show the reaction diagram
-
cripto interacts with the nodal pro segment and mature domain and presents uncleaved precursor to extracellular furin that is recruited through its P-domain
-
-
?
p-Glu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
PA83 + H2O
PA63
show the reaction diagram
-
-
-
?
parathyroid hormone-related peptide + H2O
?
show the reaction diagram
-
-
-
-
?
PC1/3 C-terminal peptide + H2O
?
show the reaction diagram
-
cleavage by furin into a peptide with an apparent molecular mass of 12.5 kDa. Cleavage of the C-terminal to the pair of Args occupying positions 627 and 628
-
-
?
PC2-S383A
?
show the reaction diagram
-
furin fully processes the PC2 mutant at the secondary site in AtT-20 cells, site is accessible to in trans cleavage
-
-
-
PCSK9 + H2O
?
show the reaction diagram
-
cleavage by furin at Arg218. Mutations R218S, F216L, and D374Y of PCSK9 associated with hypercholesterolemia result in total or partial loss of furin/PC5/6A processing at the motif RFHR21, mutant A443T shows enhanced susceptibility to furin cleavage
-
-
?
PE2 glycoprotein precursor + H2O
?
show the reaction diagram
enzyme is involved in maturation of PE2 glycoprotein of alphaviruses. Enzyme cleaves efficiently PE2 glycoprotein mutants with residues arginine, serine, phenylalanine, histidine, asparagine, or aspartic acid at the +1 position
-
-
-
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
show the reaction diagram
-
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
show the reaction diagram
-
-
?
pERKTR-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
?
show the reaction diagram
-
-
-
-
-
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methycoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methycoumarin
show the reaction diagram
-
-
?
POMC prohormone precursor + H2O
ACTH + alpha-MSH + beta-endorphin
show the reaction diagram
-
human pituitary may utilize the cathepsin L and prohormone convertase pathways for producing POMC-derived peptide hormones
-
?
precursor of transforming growth factor beta + H2O
?
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-ADAMTS4 + H2O
?
show the reaction diagram
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
show the reaction diagram
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin, cleavage sequence is Arg73-Ala-Pro-Arg76-/-Ser77
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
show the reaction diagram
-
pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4, i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin
-
?
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
show the reaction diagram
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
show the reaction diagram
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
show the reaction diagram
-
CD109 is produced as a 205 kDa glycoprotein, which is then processed in the Golgi apparatus into 180 kDa and 25 kDa proteins by furin, CD109 is a glycosylphosphatidylinositol-anchored glycoprotein, cleavage motif comprises amino acids 1270-RRRR-1273
-
?
pro-hADAM-15 protein + H2O
?
show the reaction diagram
-
cleavage site is HIRRRR-/-DVVT
-
-
?
pro-hADAM-TS 4 protein + H2O
?
show the reaction diagram
-
cleavage site is RPRRAKR-/-FASL
-
-
?
pro-hADAM-TS 6 protein + H2O
?
show the reaction diagram
-
cleavage site is HHRQRR-/-SVSI
-
-
?
pro-hADAMTS-17 protein + H2O
?
show the reaction diagram
-
cleavage site is HVRKRR-/-ADPD
-
-
?
pro-hADAMTS-23 protein + H2O
?
show the reaction diagram
-
cleavage site is LKRRKR-/-AVNP
-
-
?
pro-hepcidin + H2O
active mature hepcidin
show the reaction diagram
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
?
pro-hTGF-beta1 protein + H2O
?
show the reaction diagram
-
cleavage site is NRRKKR-/-ALDA
-
-
?
pro-hTGF-beta2 protein + H2O
?
show the reaction diagram
-
cleavage site is GQRKKR-/-ALDT
-
-
?
pro-hTGF-beta3 protein + H2O
?
show the reaction diagram
-
cleavage site is SSRHRR-/-ALDT
-
-
?
pro-hTGF-beta4 protein + H2O
?
show the reaction diagram
-
cleavage site is RSRGRR-/-FSQS
-
-
?
pro-MT-MMP 1 protein + H2O
?
show the reaction diagram
-
cleavage site is NVRRKR-/-YALT
-
-
?
pro-MT-MMP 11 protein + H2O
?
show the reaction diagram
-
cleavage site is RHRQKR-/-FVLS
-
-
?
pro-MT-MMP 3 protein + H2O
?
show the reaction diagram
-
cleavage site is RNRQKR-/-FVLS
-
-
?
pro-MT-MMP 4 protein + H2O
?
show the reaction diagram
-
cleavage site is QSRRRR-/-QTPP
-
-
?
pro-MT-MMP 6 protein + H2O
?
show the reaction diagram
-
cleavage site is VRRRRR-/-YALS
-
-
?
pro-von Willebrand factor + H2O
?
show the reaction diagram
-
-
-
-
?
proaerolysin + H2O
?
show the reaction diagram
-
cleavage site is KVRRAR-/-SVDG
-
-
?
procollagen V + H2O
?
show the reaction diagram
-
proteolytic processing of the proalpha1(V) C-propeptide chain. Proteolytic C-propeptide removal by furin occurs between Arg1585 and Asn1586. Processing of the C-propeptide by furin is more efficient than processing by bone morphogenetic protein-1
-
-
?
proPDGF-A + H2O
PDGF-A + PGDF-A propeptide
show the reaction diagram
-
a growth factor proform
-
?
proPDGF-B + H2O
PDGF-B + PGDF-B propeptide
show the reaction diagram
-
a growth factor proform of 31 kDa
mature form of 17 kDa
?
proprotein convertase PCSK9 + H2O
?
show the reaction diagram
-
-
PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form, PCSK9 is inactivated by furin by cleavage at residue R218
-
?
Prorenin + H2O
?
show the reaction diagram
-
-
-
-
-
Protective antigen component of anthrax toxin + H2O
?
show the reaction diagram
-
cleavage at the sequence Arg-Lys-Lys-Arg
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
-
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
Sindbis virus gpE2
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
human complement pro-C3
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
human complement pro-C3, fowl plague virus hemagglutinin
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
cleavage following the prosequence Arg-Gly-Val-Phe-Arg-Arg
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
Newcastle disease virus glycoprotein F0, human insulin pro-receptor
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
also cleaves chicken proalbumin after a single arginine residue following the Arg-Asn-Leu-Gln-Arg-Phe-Ala-Arg prosequence
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
human immunodeficiency virus glycoprotein 160
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
measles glycoprotein F0, human cytomegalovirus glycoprotein B, the term -+- depicts the point of cleavage, e.g. stromelysin 3
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
proalbumin (human)
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
proalbumin (human)
-
-
-
Protein precursor + H2O
?
show the reaction diagram
-
proalbumin (human)
-
-
-
proVEGF-C + H2O
VEGF-C + VEGF-C propeptide
show the reaction diagram
-
a growth factor proform
-
?
Pseudomonas aeruginosa exotoxin A + H2O
?
show the reaction diagram
-
-
-
-
?
Pseudomonas exotoxin A + H2O
?
show the reaction diagram
Mus musculus, Homo sapiens, Mus musculus C57BL/6
-
-
-
-
?
Pseudomonas toxin + H2O
?
show the reaction diagram
-
cleavage site is RHRQPR-/-GWEQ
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pyr-Arg-Thr-Lys-Arg
show the reaction diagram
-
pERTKR-MCA
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
a fluorogenic substrate
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
pyroglutamic acid-RTKR-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-RTKR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
RPTPkappa + H2O
?
show the reaction diagram
-
-
-
-
?
RPTPkappa + H2O
?
show the reaction diagram
-
furin is required for S1 processing of RPTPkappa in the secretory pathway. Purified furin cleaves RPTPkappa within the membrane-proximal fibronectin type III domain at the sequence RTKR
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + Arg-Thr-Lys-Arg
show the reaction diagram
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
show the reaction diagram
-
-
?
SARS coronavirus spike glycoprotein + H2O
?
show the reaction diagram
-
introduction of a prototypic furin recognition motif at R667 allows for efficient cleavage of the mutant glycoprotein
-
-
?
Shiga toxin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage site is ASRVAR-/-MASD
-
-
?
Synthetic peptides + H2O
?
show the reaction diagram
-
based on the N-terminal sequence of human proalbumin
-
-
-
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
TACE/ADAM17 + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-RVRR-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
TGFbeta1 + H2O
?
show the reaction diagram
-
-
-
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
?
type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
?
viral precursor protein E3E2
?
show the reaction diagram
synthetic construct
-
processes E3E2 from African Chikungunya virus strain at the HRQRR642ST site, whereas a Chikungunya virus strain of Asian origin is cleaved at site RRQRR642SI
-
-
?
Viral spike glycoproteins + H2O
?
show the reaction diagram
-
-
-
-
-
Moloney murine leukemia virus Env precursor protein + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
survey of furin substrate specificity using substrate phage display
-
-
-
additional information
?
-
-
no processing of: human lactase-phlorizin hydrolase
-
-
-
additional information
?
-
-
synthetic tripeptide substrates containing only pairs of basic amino acids are not well cleaved, 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
?
-
-
Preference for Arg-Glu-Lys-Arg-+-Ala vs. Lys-Ala-Lys-Arg-+-Arg, 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
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
-
?
additional information
?
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
-
?
additional information
?
-
-
viruses can be activated by furin
-
-
-
additional information
?
-
-
probably plays a role in proprotein maturation
-
-
-
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
-
additional information
?
-
-
role in processing of proenkephalin
-
-
-
additional information
?
-
-
proprotein processing activity
-
-
-
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
?
-
-
processing of viral glycoproteins
-
-
-
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
-
?
additional information
?
-
plays an important role in posttranslatioal protein processing
-
-
?
additional information
?
-
-
proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
-
-
?
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
?
-
-
is not able to cleave mutant Shiga-2D toxin
-
-
-
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
?
-
-
no cleavage of the low pathogenic H1N1 H1 hemagglutinin
-
-
-
additional information
?
-
synthetic construct
-
regular (short) form of transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin
-
-
-
additional information
?
-
-
soluble hemojuvelin originates from a furin cleavage at position 332-335. Soluble hemojuvelin is increased in cells overexpressing exogenous furin
-
-
-
additional information
?
-
synthetic construct
-
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
-
-
-
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
?
-
-
intracellular processing by furin-like prohormone convertases is required for secretion of cysteine-rich FGF receptor
-
-
-
additional information
?
-
-
furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
-
-
-
additional information
?
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
-
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
-
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase, recombinatly expressed as GFP-tagged enzyem in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
-
-
-
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
?
-
-
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 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
?
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADAMTS9 propeptide + H2O
?
show the reaction diagram
-
the intact zymogen is secreted to the cell surface and is subsequently processed by furin before release into thge medium. ADAMTS9 processing is exclusively extracellular and occurs at the cell surface in cells that express high levels of furin
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
show the reaction diagram
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
show the reaction diagram
-
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
show the reaction diagram
-
i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
?
G-protein-coupled receptor GPR107 + H2O
?
show the reaction diagram
-
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
HIV-1 Tat protein + H2O
?
show the reaction diagram
-
furin processing is a likely mechanism for inactivating extracellular HIV-1 Tat protein. Furin cleavage reduces the transactivation activity of tat without preventing Tat uptake and entry into the nucleus
-
-
?
human semaphorin 3F + H2O
?
show the reaction diagram
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
IBV spike protein + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor-1 receptor + H2O
?
show the reaction diagram
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
show the reaction diagram
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
show the reaction diagram
-
furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP at the surface of cancer cells. Furin and related PCs are the essential components of the specialized cellular machinery that controls the levels of the functionally active, mature, MT1-MMP enzyme on the cell surface to continually support the potency of pericellular proteolysis
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
show the reaction diagram
-
production of mature growth hormone-releasing hormone from pro-growth hormone-releasing hormone is a stepwise process mediated predomionantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus
-
-
?
precursor of transforming growth factor beta + H2O
?
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-ADAMTS4 + H2O
?
show the reaction diagram
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
show the reaction diagram
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
show the reaction diagram
-
pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4
-
?
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
show the reaction diagram
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
show the reaction diagram
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
show the reaction diagram
-
CD109 is produced as a 205 kDa glycoprotein, which is then processed in the Golgi apparatus into 180 kDa and 25 kDa proteins by furin
-
?
proprotein convertase PCSK9 + H2O
?
show the reaction diagram
-
-
PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form
-
?
type 1 IGF receptor + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
?
type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
show the reaction diagram
-
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
viruses can be activated by furin
-
-
-
additional information
?
-
-
probably plays a role in proprotein maturation
-
-
-
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
-
additional information
?
-
-
role in processing of proenkephalin
-
-
-
additional information
?
-
-
proprotein processing activity
-
-
-
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
?
-
-
processing of viral glycoproteins
-
-
-
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
-
?
additional information
?
-
Q26489
plays an important role in posttranslatioal protein processing
-
-
?
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
?
-
Q91000
prohormone convertases specificities for prohormone cleavage, overview
-
-
-
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
-
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase, recombinatly expressed as GFP-tagged enzyem in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
-
-
-
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
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
required
Ca2+
-
5-10 mM inhibit; half-maximal activity at: 0.2 mM; required
Ca2+
-
2.46 mM; required
Ca2+
-
maximal activity at: 10 mM; required
Ca2+
-
5 mM; required
Ca2+
-
activated between 0.1 and 10 mM, optimum at about 1 mM
Ca2+
activated at concentrations below 0.01 mM
Ca2+
-
dependent
Ca2+
optimal concentration of mutant furin is 0.5 mM, activity gradually reduced with increasing Ca2+ concentrations
Ca2+
-
-
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
required
Ca2+
-
required
CoCl2
-
partially restores activity after EDTA treatment
Mg2+
-
selective activation of furin by Mg2+ ions as a result of cooperativity between furin subsites. Furin hydrolysis of peptides from measles virus fusion protein Fo and from Asian avian influenza A, H5N1, is activated between 60- and 80-fold by MgCl2. Both the pH profile of furin and its intrinsic fluorescence are modified by Mg2+ ions, which bind to furin with a Kd value of 1.1 mM
MnCl2
-
partially restores activity after EDTA treatment
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(3-guanidinophenylcarbamate)
synthetic construct
-
-
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
synthetic construct
-
-
(D-Arg)6 amide
-
IC50: 0.3 mM
(D-Arg)9 amide
-
IC50: 0.01 mM
(D-Arg)9-amide
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
-
competitive inhibitor
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
-
competitive inhibitor
1,10-phenanthroline
-
-
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(azeno)-4,10-benzodiazacyclopentadecine
-
12% inhibition at 0.1 mM
1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
10% inhibition at 0.1 mM
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
synthetic construct
-
-
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
synthetic construct
-
-
11-amino-undecanoyl-RARRRKKRT
-
-
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
noncompetitive inhibitor
2-Bromopalmitate
-
inhibits nodal processing by Flag-tagged furin
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
-
-
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
noncompetitive inhibitor
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
-
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
-
competitive inhibitor
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
-
competitive inhibitor
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
-
-
4,6-bis(4-guanidinylphenoxy)-1-guanidinyl-3-(4-guanidinylphenylamino)cyclohexane
-
-
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
-
-
4-(2-aminoethyl)benzenesulphonyl fluoride
-
-
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
-
4-Hydroxycoumarin
-
-
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
-
-
8,11,22,25-tetrabenzyl-5,6,13,14,19,20,27,28-octadehydro-7,8,9,10,11,12,21,22,23,24,25,26-dodecahydrodibenzo[h,t][1,4,13,16]tetraazacyclotetracosine
-
-
8-amino-octanoyl-RARRRKKRT
-
-
a1-PDX
-
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
-
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
-
Ac-HHKRRR-NH2
-
-
Ac-HRKRRR-NH2
-
-
Ac-KHKRRR-NH2
-
-
Ac-KRKRRR-NH2
-
-
Ac-LLRVKR
-
-
Ac-LLRVKR-NH2
-
-
Ac-MHKRRR-NH2
-
-
Ac-MRKRRR-NH2
-
-
Ac-RHKRRR-NH2
-
-
Ac-RRKRRR-NH2
-
-
acetyl-RARRRKKRT
-
-
acetyl-Val-Arg-4-amidinobenzylamide
-
-
AEBSF
-
partially inhibits ectodomain shedding by 45%
alpha1-Antichymotrypsin
-
incorporation of furin recognition sequences within the reactive site loop of alpha1-antiprypsin leads to the production of furin inhibitors, construction of a series of alpha1-antichymotrypsin mutants by modifying the P7-P1 region of the reactive site loop
-
Alpha1-antitrypsin
-
not inhibited by normal antitrypsin M
-
Alpha1-antitrypsin
-
type Pittsburgh as well as wild type
-
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
-
-
-
Alpha1-antitrypsin
-
-
-
alpha1-antitrypsin M352R
-
i.e. alpha1-PDX. Engineering of alpha1-antitrypsin variants, containing Arg at the P1 site within the reactive site loop, with improved specificity for the proprotein convertase furin using site-directed random mutagenesis, screening, overview. The engineered a1-antitrypsin variant carrying the RXXR consensus motif for furin within its reactive site loop. Furin-mediated maturation of bone morphogenetic protein-4 is completely inhibited by ectopic expression of the AVNR variant
-
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
alpha1-AT
-
a naturally occurring serpin and a potent inhibitor of furin
-
alpha1-PDX
-
-
-
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
-
alpha1-PDX inhibitor
-
-
-
antipain
-
moderately
antipain
-
-
antipain
-
-
antipain
-
minimal inhibition of ectodomain shedding
antithrombin
-
not
-
antithrombin
-
-
-
antithrombin/heparin
-
not: antithrombin alone
-
beta-Ala-TPRARRRKKRT-amide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
-
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
-
brefeldin A
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
brefeldin A
-
inhibits the secretion of furin
Ca2+
-
5-10 mM inhibit; activation below
Ca2+
-
100 mM; activation below
Chloroquine
synthetic construct
-
weakly affects proprotein convertase activity and E3E2 processing. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
cholyl-RARRRKKRT
-
-
chymostatin
-
-
chymostatin
-
minimal inhibition of ectodomain shedding
Cu(2,2':6,2''-terpyridine)Cl2
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.005 mM
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu(di-[2-picolyl]amine)Cl2
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Cu2+
-
IC50: 0.014 mM
CuSO4
-
-
D-poly-Arg-NH2
-
-
D-Tyr-Ala-Lys-Arg-CH2Cl
-
-
Dec-RVKR-CMK
-
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
efficiently inhibits ectodomain shedding by 95%
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
significantly blocks the processing of ADAMTS4 in HEK-293 cells
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks furin activity, 99% inhibition of parathyroid hormone-related peptide maturation
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
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
-
furin inhibitor, pro-hepcidin activity is abolished
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks cleavage of the first and second motifs in human hepatoma cells
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
-
fully blocks the substrate cleavage by the wild-type enzyme
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
decanoyl-RVKR-chloromethyl ketone
synthetic construct
-
furin inhibitor, inhibits E3E2 cleavage. Additive inhibitory effect of chloroquine and decanoyl-RVKR-chloromethyl ketone on viral infection
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethyl ketone
-
inhibition of furin inhibits processing of pro-B-type natriuretic peptide
decanoyl-RVKR-chloromethyl ketone
-
-
decanoyl-RVKR-chloromethylketone
-
the furin inhibitor reduces DHBV infection of primary duck hepatocytes
decanoyl-RVRR-chloromethyl ketone
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
moderately
diisopropyl fluorophosphate
-
-
dithiothreitol
-
-
DYYHFWHRGVKRSLSPHRPRHSR
-
i.e. profurin 39-62
E-64
-
minimal inhibition of ectodomain shedding
EDTA
-
-
EDTA
-
97% inhibition, Ca2+ can reverse the inhibitory effect
EDTA
-
completely inhibits
Eglin c
-
engineered variants
eglin c Arg replaced with Asp at P3
-
-
-
eglin c mutant D42R
-
-
-
eglin c mutant L45R
-
-
-
eglin variant M1 RVTR
-
-
-
eglin variant M2 RVKR
-
-
-
eglin variant M3 RVTRDERY
-
-
-
eglin variant M4 RVTRDRRY
-
-
-
eglin variant M5 RVTRDLDY
-
-
-
eglin variant M6 RVTRDLRR
-
-
-
eglin variant M7 RVTRDLRE
-
-
-
eglin variant M8 RVTRDARY
-
-
-
furin inhibitor I
-
-
-
furin-Eda peptide acyclic
-
synthesis, overview. Designed a potent furin inhibitor that contains a highly reactive beta-turn inducing and radical generating enediynyl amino acid moiety, which is inserted between P1 and P19 residues of hfurin98-112 peptide, derived from the primary cleavage site of furin's own prodomain. The inhibitor displays a predominantly beta-turn structure. The inhibitor protects furin protein from self degradation
furin-Eda peptide cyclic
-
synthesis, overview
Glu-Gly-Arg-chloromethylketone
-
poor inhibitor
hepta-L-arginine
-
-
hexa-D-arginine
-
-
hexa-D-arginine
-
blocks furin activity, 85% inhibition of parathyroid hormone-related peptide maturation
hexa-L-arginine
-
-
hfurin25-107
-
i.e. furin prodomain protein, competitive inhibitor, blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain, overview. Secondary structure of furin prodomain protein, overview
-
Hg2+
-
-
HgCl2
-
-
histone H1
-
efficiently blocks furin-dependent pro-von Willebrand factor processing in a dose-dependent manner, interaction between histone H1 and furin mainly takes place on the cell surface. H1 may be involved in extracellular and/or intracellular furin regulation
-
human proteinase inhibitor 8
-
-
-
inter-alpha-inhibitor protein IalphaIp
-
blocks furin activity in vitro and provides significant protection against cytotoxocity for murine peritoneal macrophages exposed to up to 500 ng/ml anthrax lethal toxin
-
iodoacetamide
-
-
iodoacetamide
-
about 50% inhibition
iodoacetamide
about 50% inhibition
L-1-chloro-3-(4-tosylamido)-7-amino-2-heptanone
-
-
lethal factor inhibitor 2
-
IC50: 0.002 mM
-
Leupeptin
-
moderately
Leupeptin
-
moderately
Leupeptin
-
minimal inhibition of ectodomain shedding
LLRVKR
-
-
LLRVKR-NH2
-
-
Lys-Arg chloromethyl ketone
-
-
m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
-
a competitive, noncovalent inhibitor, binding structure, overview
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
noncompetitive inhibitor
MnCl2
-
-
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
competitive inhibitor
N-(benzo[d][1,3]dioxol-5-yl)-1,2,3,4-tetrahydroacridin-9-amine
-
competitive inhibitor
N-(thiazol-2-yl)-4-(5-((2,4,6-trioxotetrahydropyrimidin-5(6H)-ylidene)methyl)furan-2-yl)benzenesulfonamide
-
competitive inhibitor
N-tosyl-L-lysine chloromethyl ketone
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
-
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
-
N-[5-guanidino-2,4-bis-(4-guanidino-phenoxy)-cyclohexyl]-guanidine
-
-
N-[5-guanidino-2,4-bis-(5-guanidino-pyridin-2-yloxy)-cyclohexyl]-guanidine
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
-
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
-
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
-
NEM
-
moderately
nona-L-arginine
-
most potent inhibitor
octa-L-arginine
-
-
Octapeptidyl chloromethane inhibitor
-
potent irreversible inhibitor
-
p-chloromercuribenzenesulfonic acid
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
PenLen (rSAAS-(221-2546))
-
neuroendocrine protein proSAAS-derived peptide
penta-L-arginine
-
-
Peptidyl chloroalkyl ketones
-
-
Phe-Pro-Arg-chloromethylketone
-
poor inhibitor
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
-
phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
-
a competitive, noncovalent inhibitor, binding structure, overview
-
phenylmethanesulfonyl fluoride
-
moderately
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
not
phenylmethylsulfonyl fluoride
-
-
Pro-Gly-Lys-Arg-CH2Cl
-
-
pro-hepcidin
-
hydrolytic activity of membrane furin against the fluorescent substrate Boc-RVRR-7-amino-4-methyl-coumarin is reduced by approximately 50% in presence of 2 micromol pro-hepcidin and completely abolished in presence of 5 micromol pro-hepcidin
-
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
-
profurin 48-62 VTKRSLSPHRPRHSR
-
peptide derived from proprotein convertase 1/3
profurin 54-62 SPHRPRHSR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62 NHYLFKHKSHPRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-62 RRSRR SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
peptide derived from proprotein convertase 1/3
-
proPC1/3 55-62 SALHITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 55-62/A SALAITKR
-
peptide derived from proprotein convertase 1/3
proPC1/3 74-83 QQYEKERSKR
-
peptide derived from proprotein convertase 1/3
RARRRKKRT
-
-
SAAS-(235-244)
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P1'A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P2'A
-
neuroendocrine protein proSAAS-derived peptide
-
SAAS-(235-246)P3A
-
neuroendocrine protein proSAAS-derived peptide
SAAS-(235-246)P3AP5A
-
neuroendocrine protein proSAAS-derived peptide
siRNA
-
-
-
siRNA
-
furin mRNA knockdown, pro-hepcidin activity is diminished
-
tetra-L-arginine
-
-
tosyl-Lys chloromethyl ketone
-
-
TPQRARRRKKRF
-
-
TPQRARRRKKRT
-
-
TPQRARRRKKRW
-
-
TPQRARRRKKRY
-
-
TPRARRRKKRG
-
-
TPRARRRKKRI
-
-
TPRARRRKKRT
-
-
TPRARRRKKRT
-
-
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
-
0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
Zn2+
-
-
Zn2+
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
ZnCl2
-
-
[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
monensin
-
blocks the tumor necrosis factor alpha-induced activation of furin and subsequent neutral sphingomyelinase activation, without altering the basal level of furin
additional information
-
a potent inhibitor containing a ketomethylene arginyl pseudopeptide bond; contains Cys near the active site His
-
additional information
-
not: pepstatin
-
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
-
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
-
soluble hemojuvelin is reduced in cells treated with a furin inhibitor
-
additional information
-
aprotinin has no effect on furin-like protease activity
-
additional information
-
pepstatin A, 1,10-ortho-phenanthroline, EDTA, or TAPI-0 do not inhibit ectodomain shedding
-
additional information
synthetic construct
-
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
-
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 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
-
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
-
no inhibition by metalloprotease inhibitor GM6001
-
additional information
-
EC values of furin inhibitors, overview. Inhibition of cell-surface PA83 processing in cell-based assays, overview
-
additional information
-
design of specific small molecule inhibitors targeting furi, 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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
parasite expresses a Ca2+ dependent, furin-like protease activity
Tumor necrosis factor alpha
-
-
-
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
-
L-Sox5 and Sox-6 act as negative regulators of Sox9-induced furin expression
-
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
-
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
-
furin induced by interleukin 12
-
additional information
-
furin is up-regulated by iron deficiency and hypoxia in association with the stabilization of HIF-1alpha
-
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
-
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
-
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
-
-
0.0038
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
-
-
0.00039
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00042
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00021
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0012
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0003
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0032
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00038
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0027
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0002
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00022
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00028
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00037
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00005
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0001
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00028
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0052
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00033
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0014
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0001
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.0002
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0065
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.0012
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0122
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00039
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00041
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.0155
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
-
0.00022
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00023
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00041
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00049
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00007
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.00015
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00045
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00014
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.005
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00086
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+
0.00416
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, presence of Mg2+
0.00053
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.0, 37C, absence of Mg2+; pH 7.0, 37C, presence of Mg2+
0.0123
Ac-Arg-Val-Arg-Arg-4-nitroanilide
-
-
0.001
Ac-norleucineYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.016
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.008
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.345
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
-
-
0.0015
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.005
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.106
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.028
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.00194
acetyl-RVRR-4-methylcoumarin 7-amide
-
pH 7.0, 37C
0.0071
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
-
-
0.0009
AcRARYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.0008
AcRYKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.0006
AcRYRFKR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.019
Boc-RVRR-4-methylcoumarin-7-amide
-
pH 7.0, 37C
0.01
Boc-RVRR-7-amido-4-methyl-coumarin
-
-
0.029
Boc-RVRR-7-amido-4-methylcoumarin
-
0.035
DSSARIRRNAKG
-
pH 7.0, 37C
-
0.0059
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate
-
-
0.00007
hBMP-2 precursor protein
-
first cleavage site, pH 7.0, 37C
-
0.0013
hBMP-2 precursor protein
-
second cleavage site, pH 7.0, 37C
-
0.0014
hBMP-4 precursor protein
-
second cleavage site, pH 7.0, 37C
-
0.00124
pERKTR-7-amido-4-methylcoumarin
-
0.005
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
-
0.0002
pro-hADAM-15 protein
-
pH 7.0, 37C
-
0.00055
pro-hADAM-TS 4 protein
-
pH 7.0, 37C
-
0.0004
pro-hADAM-TS 6 protein
-
pH 7.0, 37C
-
0.0091
pro-hADAMTS-17 protein
-
pH 7.0, 37C
-
0.0067
pro-hADAMTS-23 protein
-
pH 7.0, 37C
-
0.0001
pro-hTGF-best1 protein, pro-hTGF-beta2 protein
-
pH 7.0, 37C
-
0.00014
pro-hTGF-beta3 protein
-
pH 7.0, 37C
-
0.0022
pro-hTGF-beta4 protein
-
pH 7.0, 37C
-
0.00015
pro-MT-MMP 1 protein
-
pH 7.0, 37C
-
0.00011
pro-MT-MMP 11 protein, pro-MT-MMP 3 protein
-
pH 7.0, 37C
-
0.00045
pro-MT-MMP 4 protein
-
pH 7.0, 37C
-
0.00037
pro-MT-MMP 6 protein
-
pH 7.0, 37C
-
0.00064
proaerolysin
-
pH 7.0, 37C
-
0.002
protective antigen
-
(-Arg-Lys-Lys-Arg-Ser-Thr-Ser-Ala-Gly-)
-
0.0118
Pseudomonas toxin
-
pH 7.0, 37C
-
0.0032
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide
-
pH 7.5, 37C
0.0026
Shiga toxin
-
pH 7.0, 37C
-
0.01517
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.0156
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
-
-
0.000036
viral precursor protein E3E2
synthetic construct
-
R64A mutant peptide of E3E2 from Asian Chikungunya virus strain
-
0.000122
viral precursor protein E3E2
synthetic construct
-
wild-type E3E2 from Asian Chikungunya virus strain
-
0.0015
hBMP-4 precursor protein
-
first cleavage site, pH 7.0, 37C
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.3
2-Aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH
Mammalia
-
-
29.6
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
30.3
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
3.6
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
4.2
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
28.9
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
39.5
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
6.3
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
6.9
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
7.6
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
12.2
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
9.2
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
14.9
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
0.6
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
3.1
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
0.61
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
6.7
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
2
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
3.5
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
2.6
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
12.3
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
8.4
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
11.3
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
5.3
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
8.7
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
12.2
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
14.6
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
5
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
-
2.4
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
6.7
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
1
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
7.6
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
10.5
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
18.3
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
0.21
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
2.4
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
9.2
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
9.9
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
10
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
11.1
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
5.6
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
7.1
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
16.4
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19.8
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
50
Ac-norleucineYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
0.000934
Acetyl-Arg-Glu-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.02
Acetyl-Arg-Lys-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.0507
Acetyl-Arg-Phe-Ala-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00111
Acetyl-Arg-Pro-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.0403
Acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00159
Acetyl-Lys-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.00088
Acetyl-Orn-Ser-Lys-Arg-4-methylcoumarin 7-amide
Homo sapiens
-
-
0.7
acetyl-RVRR-4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.0, 37C
0.00135
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-4-methylcoumarin 7-amide
Homo sapiens
-
-
250
AcRARYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
193
AcRYKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
200
AcRYRFKR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
21
Boc-RVRR-4-methylcoumarin-7-amide
Homo sapiens
-
pH 7.0, 37C
0.003
Boc-RVRR-7-amido-4-methylcoumarin
Trichoplusia ni
Q5DNW1
-
3
hBMP-2 precursor protein
Homo sapiens
-
second cleavage site, pH 7.0, 37C
-
3.6
hBMP-2 precursor protein
Homo sapiens
-
first cleavage site, pH 7.0, 37C
-
3.6
hBMP-4 precursor protein
Homo sapiens
-
second cleavage site, pH 7.0, 37C
-
0.008
pERKTR-7-amido-4-methylcoumarin
Trichoplusia ni
Q5DNW1
-
5.5
pro-hADAM-15 protein
Homo sapiens
-
pH 7.0, 37C
-
4.5
pro-hADAM-TS 4 protein
Homo sapiens
-
pH 7.0, 37C
-
40
pro-hADAM-TS 6 protein
Homo sapiens
-
pH 7.0, 37C
-
1
pro-hADAMTS-17 protein, pro-hADAMTS-23 protein
Homo sapiens
-
pH 7.0, 37C
-
1.5
pro-hTGF-beta1 protein
Homo sapiens
-
pH 7.0, 37C
-
3.4
pro-hTGF-beta2 protein
Homo sapiens
-
pH 7.0, 37C
-
8.4
pro-hTGF-beta3 protein
Homo sapiens
-
pH 7.0, 37C
-
1.2
pro-hTGF-beta4 protein
Homo sapiens
-
pH 7.0, 37C
-
2.4
pro-MT-MMP 1 protein
Homo sapiens
-
pH 7.0, 37C
-
1.3
pro-MT-MMP 11 protein
Homo sapiens
-
pH 7.0, 37C
-
0.5
pro-MT-MMP 3 protein
Homo sapiens
-
pH 7.0, 37C
-
5.5
pro-MT-MMP 4 protein
Homo sapiens
-
pH 7.0, 37C
-
0.84
pro-MT-MMP 6 protein
Homo sapiens
-
pH 7.0, 37C
-
12.2
proaerolysin
Homo sapiens
-
pH 7.0, 37C
-
11
protective antigen
Mammalia
-
(-Arg-Lys-Lys-Arg-Ser-Thr-Ser-Ala-Gly-)
-
0.54
Pseudomonas toxin
Homo sapiens
-
pH 7.0, 37C
-
16
Shiga toxin
Homo sapiens
-
pH 7.0, 37C
-
0.192
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
Mammalia
-
-
5.6
hBMP-4 precursor protein
Homo sapiens
-
first cleavage site, pH 7.0, 37C
-
additional information
additional information
Homo sapiens
-
-
-
additional information
additional information
Homo sapiens
-
over the pH intercal 6.0 to 9.0 kcat occurs as a bell-shaped form with a maximum at pH 7.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
70550
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19588
77100
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19588
3085
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19582
20190
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19582
9031
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19597
116100
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19597
2354
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19598
17730
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19598
38300
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19587
55640
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19587
32430
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19585
40270
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19585
6000
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19590
53450
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19590
1303
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19592
2184
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19592
1470
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19591
10610
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19591
1555
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19601
123000
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19601
1291
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19581
56300
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19581
710
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19595
4383
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19595
29660
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19586
37510
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19586
322
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
28605
797
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19599
30500
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19599
606
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19600
33040
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19600
25360
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19584
37350
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19584
559
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19593
33860
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19593
20470
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19583
66000
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19583
1992
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19589
76230
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19589
1707
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19596
6488
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19596
28360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, absence of Mg2+
19594
37360
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine
Homo sapiens
-
pH 7.0, 37C, presence of Mg2+
19594
361
acetyl-RVRR-4-methylcoumarin 7-amide
Homo sapiens
-
pH 7.0, 37C
40584
2331
hBMP-2 precursor protein
Homo sapiens
-
second cleavage site, pH 7.0, 37C
19262
50710
hBMP-2 precursor protein
Homo sapiens
-
first cleavage site, pH 7.0, 37C
19262
2649
hBMP-4 precursor protein
Homo sapiens
-
second cleavage site, pH 7.0, 37C
19263
3700
hBMP-4 precursor protein
Homo sapiens
-
first cleavage site, pH 7.0, 37C
19263
27600
pro-hADAM-15 protein
Homo sapiens
-
pH 7.0, 37C
40570
8127
pro-hADAM-TS 4 protein
Homo sapiens
-
pH 7.0, 37C
40571
100000
pro-hADAM-TS 6 protein
Homo sapiens
-
pH 7.0, 37C
40569
109
pro-hADAMTS-17 protein
Homo sapiens
-
pH 7.0, 37C
40573
143
pro-hADAMTS-23 protein
Homo sapiens
-
pH 7.0, 37C
40572
14700
pro-hTGF-beta1 protein
Homo sapiens
-
pH 7.0, 37C
81568
34200
pro-hTGF-beta2 protein
Homo sapiens
-
pH 7.0, 37C
40575
60140
pro-hTGF-beta3 protein
Homo sapiens
-
pH 7.0, 37C
40574
534
pro-hTGF-beta4 protein
Homo sapiens
-
pH 7.0, 37C
40576
15800
pro-MT-MMP 1 protein
Homo sapiens
-
pH 7.0, 37C
40577
11450
pro-MT-MMP 11 protein
Homo sapiens
-
pH 7.0, 37C
40579
4545
pro-MT-MMP 3 protein
Homo sapiens
-
pH 7.0, 37C
40580
12670
pro-MT-MMP 4 protein
Homo sapiens
-
pH 7.0, 37C
40578
2240
pro-MT-MMP 6 protein
Homo sapiens
-
pH 7.0, 37C
40581
20670
proaerolysin
Homo sapiens
-
pH 7.0, 37C
40582
45
Pseudomonas toxin
Homo sapiens
-
pH 7.0, 37C
40583
6134
Shiga toxin
Homo sapiens
-
pH 7.0, 37C
37353
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)
synthetic construct
-
-
0.000812
(1R,3S,4S,6R)-4-(2-carbamimidoylhydrazinyl)-6-guanidinocyclohexane-1,3-diyl bis(4-guanidinophenylcarbamate)
synthetic construct
-
-
0.0000013
(D-Arg)9-amide
-
-
0.000046
1-[(1R,2R,4S,5S)-2,4-bis(4-carbamimidamidophenoxy)-5-[(4-carbamimidamidophenyl)amino]cyclohexyl]guanidine
synthetic construct
-
-
0.000423
1-[4-([(1S,2S,4R,5R)-5-carbamimidamido-2,4-bis[(4-carbamimidamidonaphthalen-1-yl)oxy]cyclohexyl]amino)naphthalen-1-yl]guanidine
synthetic construct
-
-
0.0000089
11-amino-undecanoyl-RARRRKKRT
-
pH 7.5, 37C
0.000169
2-((1S,2S,4R,5R)-2,4-bis(2,4-diguanidinophenoxy)-5-guanidinocyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000404
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000089
2-((1S,2S,4R,5R)-2-(2,4-diguanidinophenoxy)-5-guanidino-4-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000022
2-((1S,2S,4R,5R)-2-(2-amino-4-guanidinophenoxy)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000069
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinonaphthalen-1-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000012
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000042
2-((1S,2S,4R,5R)-5-guanidino-2,4-bis(5-guanidinopyridin-2-yloxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.000006
2-((1S,2S,4R,5R)-5-guanidino-4-(4-guanidinonaphthalen-1-yloxy)-2-(4-guanidinophenoxy)cyclohexyl)hydrazinecarboximidamide
synthetic construct
-
-
0.012
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
with CPA95 as substrate/with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.0033
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.00104
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
0.1851
3,3'-((2-bromophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0783
3,3'-((2-chlorophenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.022
3,3'-((3,4,5-trimethoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0208
3,3'-((4-isopropoxyphenyl)methylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00605
3,3'-(benzo[d][1,3]dioxol-5-ylmethylene)bis(4-hydroxy-2H-chromen-2-one)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0188
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
-
with CPA95 as substrate
2
3-(alpha-acetonyl-benzyl)-4-(hydroxycoumarin)
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
1.3
4-hydroxy-3-oxo-1-phenylbutylcoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
7.3
4-Hydroxycoumarin
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.0000083
8-amino-octanoyl-RARRRKKRT
-
pH 7.5, 37C
0.0024
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2
-
pH 7.0, 37C
0.0053
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Arg-D-Leu-NH2
-
pH 7.0, 37C
0.007
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Arg-NH2
-
pH 7.0, 37C
0.0227
Ac-D-Trp-D-Arg-D-Arg-D-Arg-D-Ile-D-Leu-NH2
-
pH 7.0, 37C
0.0103
Ac-HHKRRR-NH2
-
pH 7.0, 37C
0.0021
Ac-HRKRRR-NH2
-
pH 7.0, 37C
0.0052
Ac-KHKRRR-NH2
-
pH 7.0, 37C
0.0016
Ac-KRKRRR-NH2
-
pH 7.0, 37C
0.0132
Ac-MHKRRR-NH2
-
pH 7.0, 37C
0.0023
Ac-MRKRRR-NH2
-
pH 7.0, 37C
0.0034
Ac-RHKRRR-NH2
-
pH 7.0, 37C
0.0013
Ac-RRKRRR-NH2
-
pH 7.0, 37C
0.0000065
acetyl-RARRRKKRT
-
pH 7.5, 37C
0.00239
acetyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0035
AcLLRVKR
-
pH 7.0, 37C
0.0000574
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.000009
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0000151
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0000383
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0042
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0000152
cholyl-RARRRKKRT
-
pH 7.5, 37C
0.0000078
eglin c mutant Arg replaced with Asp at P3
-
pH 7.5, 37C
-
0.000023
eglin c mutant D42R, eglin c mutant L45R, eglin variant M1 RVTR
-
pH 7.5, 37C
-
0.0000016
eglin variant M2 RVKR
-
pH 7.5, 37C
-
0.00092
eglin variant M3 RVTRDERY
-
pH 7.5, 37C
-
0.0003
eglin variant M4 RVTRDRRY
-
pH 7.5, 37C
-
0.0000078
eglin variant M5 RVTRDLDY
-
pH 7.5, 37C
-
0.000047
eglin variant M6 RVTRDLRR
-
pH 7.5, 37C
-
0.000039
eglin variant M7 RVTRDLRE
-
pH 7.5, 37C
-
0.00002
eglin variant M8 RVTRDARY
-
pH 7.5, 37C
-
0.000068
hepta-L-arginine
-
pH 7.0, 37C
0.000106
hexa-D-arginine
-
pH 7.0, 37C
0.000156
hfurin25-107
-
pH 7.4, 37C, versus N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide
-
0.0000000538
human proteinase inhibitor 8
-
pH 7.5, 37C
-
0.00042
LLRVKR
-
pH 7.0, 37C
0.0008
LLRVKR-NH2
-
pH 7.0, 37C
0.0034
LLRVKR-NH2
-
pH 7.0, 37C
0.0118
N''-[(1E)-[2-[(4-chlorobenzyl)oxy]phenyl]methylidene]carbonohydrazonic diamide
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
0.00058
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-2-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenoxy]acetamide
-
pH 7.0,22C
0.00046
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-4-carbamimidamidobutanamide
-
pH 7.0,22C
0.00104
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-5-carbamimidamidopentanamide
-
pH 7.0,22C
0.00113
N-[3,5-bis[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]-N'-[3-[(1E)-1-(2-carbamimidoylhydrazinylidene)ethyl]-5-[(1Z)-1-(2-carbamimidoylhydrazinylidene)ethyl]phenyl]propanediamide
-
pH 7.0,22C
0.00302
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-aminopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000063
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(3-carbamimidamidopropyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00749
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-aminobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000078
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidamidobutyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00000081
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000553
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-aminopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00107
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(5-carbamimidamidopentyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00971
N2-(phenylacetyl)-L-arginyl-L-valyl-N-(piperidin-4-ylmethyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000053
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00132
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00273
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[3-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000627
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(aminomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.00143
N2-(phenylacetyl)-L-arginyl-L-valyl-N-[4-(carbamimidamidomethyl)benzyl]-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.000001
N2-acetyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000016
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 7.0, temperature not specified in the publication
0.0000033
N2-decanoyl-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-lysinamide
-
pH 7.0, temperature not specified in the publication
0.00004
nona-L-arginine
-
pH 7.0, 37C
0.000042
nona-L-arginine
-
pH 7.0, 37C
0.000061
octa-L-arginine
-
pH 7.0, 37C
0.0193
PenLen (rSAAS-(221-246))
-
pH 7.4, 37C
-
0.00099
penta-L-arginine
-
pH 7.0, 37C
0.0000367
phenylacetyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.000006
phenylacetyl-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37C
0.0009
profurin 39-62 DYYHFWHRGVKRSLSPHRPRHSR
-
pH 7.0, 25C
0.0028
profurin 48-62 VTKRSLSPHRPRHSR
-
pH 7.0, 25C
0.023
profurin 54-62 SPHRPRHSR
-
pH 7.0, 25C
0.0007
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
-
pH7.0, 25C
0.0154
proPC1/3 39-62 NHYLF KHKSHPRRSALAITKR
-
pH 7.0, 25C
0.0012
proPC1/3 39-62/A NAYLF KAKSAPRRSRRSALAITKR
-
pH 7.0, 25C
0.0023
proPC1/3 50-62 RRSRR SALHITKR
-
pH 7.0, 25C
0.0048
proPC1/3 50-83 RRSRRSALHITKRLSDDDRVTWAEQQYEKERSKR
-
pH 7.0, 25C
-
0.0316
proPC1/3 55-62 SALHITKR
-
pH 7.0, 25C
0.013
proPC1/3 55-62/A SALAITKR
-
pH 7.0, 25C
0.0475
proPC1/3 74-83 QQYEKERSKR
-
pH 7.0, 25C, competitive inhibition
0.000008
RARRRKKRT
-
pH 7.5, 37C
0.000261
SAAS-(235-244)
-
pH 7.4, 37C
0.0394
SAAS-(235-246)
-
pH 7.4, 37C
-
0.00128
SAAS-(235-246)P1'A
-
pH 7.4, 37
0.0044
SAAS-(235-246)P2'A
-
pH 7.4, 37C
-
0.092
SAAS-(235-246)P3A
-
pH 7.4, 37C
0.000114
tetra-L-arginine
-
pH 7.0, 37C
0.0064
tetra-L-arginine
-
pH 7.0, 37C
0.000038
TPQRARRRKKRF
-
-
0.000033
TPQRARRRKKRT
-
-
0.000034
TPQRARRRKKRW
-
-
0.000047
TPQRARRRKKRY
-
-
0.000057
TPRARRRKKRG
-
-
0.00003
TPRARRRKKRI
-
-
0.000023
TPRARRRKKRT
-
-
0.000023
TPRARRRKKRT
-
pH 7.5, 37C
0.1452
methyl 4-(bis(4-hydroxy-2-oxo-2H-chromen-3-yl)methyl)benzoate
-
with Ac-Arg-Val-Arg-Arg-4-nitroanilide as substrate
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
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
(D-Arg)6 amide
Mus musculus
-
IC50: 0.3 mM
0.01
(D-Arg)9 amide
Mus musculus
-
IC50: 0.01 mM
0.0037
(D-Arg)9-amide
Homo sapiens
-
protects RAW264.7 cells against anthrax toxemia with an IC50 of 0.0037 mM
0.102
(E)-N-((E)-5-(2-chloro-5-nitrobenzylidene)-4-oxothiazolidin-2-ylidene)-4-methylbenzenesulfonamide
Homo sapiens
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.084
(N'Z,N''Z)-4,4'-oxybis(N'-(2-hydroxybenzylidene)benzenesulfonohydrazide)
Homo sapiens
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.007
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
Homo sapiens
-
with CPA95 as substrate/with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.025
3'-oxo-6a,14a-dihydro-3'H-spiro[dibenzo[c,h]xanthene-7,1'-isobenzofuran]-3,11-diyl diacetate
Homo sapiens
-
with CPA95 as substrate
0.055
3,3',3'',3'''-(1,4-phenylenebis(methanetriyl))tetrakis(4-hydroxy-2H-chromen-2-one)
Homo sapiens
-
with CPA95 as substrate
0.004
3,3'-((2,3-dihydro-1H-inden-5-yl)methylene)bis(4-hydroxy-2H-chromen-2-one)
Homo sapiens
-
with CPA95 as substrate
0.02
3,3'-methylenebis(4-hydroxy-2H-chromen-2-one)
Homo sapiens
-
with CPA95 as substrate
0.051
3-allyl-1-methyl-1,2,3,4-tetrahydroisoquinoline
Homo sapiens
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.137
3-hydroxy-5-(4-methoxyphenyl)-2-(4-phenoxy-3-sulfophenyl)-3H-pyrazol-2-ium
Homo sapiens
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.0000142
4,10-bis[(4-methylphenyl)sulfonyl]-1,2,12,13-tetradehydro-3,4,10,11-tetrahydro-5,9-(metheno)-4,10-benzodiazacyclopentadecine
Homo sapiens
-
-
0.0000105
4,7-dibenzyl-1,2,9,10-tetradehydro-3,4,5,6,7,8-hexahydro-4,7-benzodiazacyclododecine
Homo sapiens
-
-
0.028
6-oxo-6H-benzo[c]chromen-3-yl 2-chlorobenzoate
Homo sapiens
-
with N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin amide as substrate
0.00016
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
-
-
0.000023
beta-Ala-TPRARRRKKRT-amide
Homo sapiens
-
pH 7.5, 37C
0.0077
Cu(2,2':6,2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.0077 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0072
Cu(4'-hydroxo-2,2':6',2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.0072 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0051
Cu(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.0051 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.014
Cu(4,4''-dimethyl-4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.014 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.038
Cu(di-[2-picolyl]amine)Cl2
Homo sapiens
-
IC50: 0.038 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.014
Cu2+
Homo sapiens
-
IC50: 0.014 mM
0.00004
furin-Eda peptide acyclic
Homo sapiens
-
versus substrate N-benzyloxy-RVRR-4-methylcoumarin 7-amide; 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
0.000193
furin-Eda peptide cyclic
Homo sapiens
-
versus substrate fluorogenic peptide derived from hSARS-CoV spike protein
0.002
lethal factor inhibitor 2
Mus musculus
-
IC50: 0.002 mM
-
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
0.002
pro-hepcidin
Mus musculus
-
-
-
0.009
Zn(4'-[4-methoxyphenyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.009
Zn(4'-[p-tolyl]-2,2':6',2''-terpyridine)Cl2
Homo sapiens
-
IC50: 0.009 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.021
Zn2+
Homo sapiens
-
IC50: 0.021 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.0069
[Cu(2,2':6,2''-terpyridine)Cl2] (OCl4)
Homo sapiens
-
IC50: 0.0069 mM, irreversible, competitive with substrate tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000025
-
with Boc-RVRR-7-amido-4-methyl-coumarin as substrate
0.35
-
recombinant furin
57
-
purified recombinant enzyme, pH 7.0, 37C
18000
mutant, 64fold purified
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
-
proalbumin
5.5 - 6.5
-
-
6
-
acetyl-Arg-Ser-Lys-Arg-4-methylcoumaryl 7-amide
6
-
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
6.5 - 7.5
-
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
6.5 - 7.5
-
-
7
-
around, tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide
7
-
hydrolysis tert-butyloxycarbonyl-RVRR-4-methylcoumaryl-7-amide
7
-
assay at
7
-
assay at
7 - 7.5
-
-
7.4
-
assay at
7.5
-
assay at
additional information
between pH 7-9, mutant has a broad pH optimum shifted toward alkalinity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
-
5: about 35% of activity maximum, 6.5: about 15% of activity maximum, mouse, acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
6 - 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
6 - 8.5
-
more than 50% of activity maximum at pH 6.0 and 8.5
additional information
-
pH-profiles of furin activity in the presence and absence of salts, e.g. KCl. The pK1 values for the pH-profiles of hydrolysis of all four substrates in the presence of KCl are lower than those in its absence
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary cortical
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
basement membrane
Manually annotated by BRENDA team
-
chief cells, coordinated decrease of pepsinogen, furin, and transforming growth factor beta
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
chief cells, coordinated decrease of pepsinogen, furin, and transforming growth factor beta
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
limiting amounts of furin
Manually annotated by BRENDA team
-
extravillous cells
Manually annotated by BRENDA team
-
infected by heaptitis C virus
Manually annotated by BRENDA team
-
expression and regulation of furin in ovarian tissue, injection of equine and human chorionic gondotropin, overview
Manually annotated by BRENDA team
-
expresses PC1/3 and PC2
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
proprotein convertase furin is highly expressed in syncytial trophoblast in the first trimester human placentas, and expression of furin in the syncytiotrophoblast is significantly lower in the placentas from pre-eclamptic patients as compared with their gestational age-matched control placentas
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
proprotein convertase furin is highly expressed in syncytial trophoblast in the first trimester human placentas, and expression of furin in the syncytiotrophoblast is significantly lower in the placentas from pre-eclamptic patients as compared with their gestational age-matched control placentas
Manually annotated by BRENDA team
additional information
-
absent from LoVo cells
Manually annotated by BRENDA team
additional information
-
ATDC5 cell
Manually annotated by BRENDA team
additional information
-
preferentially expressed in T helper 1 cells in a Stat4-dependent manner
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
lysate
Manually annotated by BRENDA team
additional information
-
absent from LoVo-C5 cells
Manually annotated by BRENDA team
additional information
-
airway cell
Manually annotated by BRENDA team
additional information
-
DF11 cell
Manually annotated by BRENDA team
additional information
-
present in glucagon cells, absent from insulin cells, somatostatin cells and pancreatic polypeptide cells
Manually annotated by BRENDA team
additional information
-
Colo-16 cell
Manually annotated by BRENDA team
additional information
-
colorectal carcinoma LoVo cell line is devoid of furin activity
Manually annotated by BRENDA team
additional information
no PCSK3 in head, ovary, and small intestine, expression in the adult, not embryo stage
Manually annotated by BRENDA team
additional information
-
furin is ubiquitously expressed
Manually annotated by BRENDA team
additional information
-
ubiquitous expression, although furin is expressed universally, expression levels vary and can be quite low depending on tissue types
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
the enzyme is constitutively expressed in all cell lines. No enzyme activity in LoVo colorectal carcinoma cells
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cytoplasmic tail
Manually annotated by BRENDA team
-
colocalization with matrix metalloproteinase MMP-28
Manually annotated by BRENDA team
-
furin-propeptide complex is restricted to the endoplasmic reticulum by a PACS-2- and COPI-dependent mechanism. His69 is a pH sensor that allows enzyme activation following transport of the furin-propeptide complex from the endoplasmic reticulum to the mildly acidic TGN/endosomal system
Manually annotated by BRENDA team
synthetic construct
-
furin localizes to endosomes when Mint3 expression is knocked down
Manually annotated by BRENDA team
-
hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
Manually annotated by BRENDA team
synthetic construct
-
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
Manually annotated by BRENDA team
-
hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the membrane-bound enzyme undergoes post-translational processing to produce a soluble form of the enzyme that can be secreted
Manually annotated by BRENDA team
-
human, mainly, the enzyme can translocate between the cell surface and the trans-Golgi network
-
Manually annotated by BRENDA team
-
cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
-
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
synthetic construct
-
-
Manually annotated by BRENDA team
synthetic construct
-
knockdown of Mint3 increases the distribution of furin at the membrane
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
additional information
-
localization of furin predominantly outside lipid rafts
-
Manually annotated by BRENDA team
additional information
-
furin is present both in the intracellular secretory pathway and at the cell surface
-
Manually annotated by BRENDA team
additional information
-
furin is a protease localized in the trans-Golgi network and in late endocytic compartments
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
59000
-
gel filtration
652060
61000
-
Western blotting with anti-furin antiserum MON148
652060
68000
mutant, Western blot analysis
682710
90000
synthetic construct
-
immunoprecipitation, mature form of furin
699103
96000
-
mouse, gel filtration
29687
96000
synthetic construct
-
immunoprecipitation, proprotein furin
699103
additional information
-
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
29691
additional information
-
x * 60000-65000, Western blot analysis, PC1/3 and PC2
697621
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 80000-85000, mouse, SDS-PAGE
?
-
x * 55000, soluble furin, SDS-PAGE
additional information
-
3 MW forms: MW 64000, 75000 and 86000, SDS-PAGE, COOH-terminal truncation is responsible for the different molecular mass forms
additional information
-
secondary structure of furin prodomain protein, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with inhibitors m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine or phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, mixing of 7.5 mg/ml enzyme with 0.290 mM m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine and 3 mM phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, respectively, and 50 mM Tris, pH 8.5, 2.8 M sodium formate and 0.015 mM Cymal-7, at 30C, displacement of the highly potent inhibitor m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine by competitive soaking with excessive amounts of the less potent phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
crystal structure of furin with bound decanoyl-Arg-Val-Lys-Arg-chloromethylketone inhibitor
-
triclinic crystals, space group P1, unit cell dimensions a = 93.3 A, b = 135.4 A, c = 137.8 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
30C, 2 h, 50 mM MES buffer, 10% loss of activity
29700
7
-
30C, 2 h, 50 mM MES buffer, about 90% loss of activity
29700
additional information
-
a positively-charged Lys residue replacing His43 in the 16-49 fragment imparts stability to the super-secondary structure of the furin prodomain at both acidic and neutral pH
678743
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
rapidly inactivated by increasing temperatures above
650437
55
-
682710
60
stable up to
650437
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Unstable at low protein concentration
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 26% loss of activity of furin mutant hFUR713t, 21% loss of activity of soluble furin after 3 weeks, optimal conditions of conservation are at 50% glycerol
-
-10C, 10% glycerol, 90% loss of activity after 1 week
-
-20C, 5 mg/ml bovine serum albumin, less than 5% loss of activity after 2 months
-
-80C, 10% glycerol, no detectable loss of activity over 6 months
-
-80C, 5-20% loss of activity after 2 weeks
-
4C, 5 mg/ml bovine serum albumin, 0.02% NaN3, less than 5% loss of activity after 2 months
-
-80C, Tris-HCl buffer, pH 8.0, 50% glycerol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by metal-chelating chromatography
-
by Ni2+ affinity chromatography
-
partially, recombinant hfurin
-
recombinant enzyme 300fold from HEK-293 cells by metal affinity chromatography, inhibitor based affinity chromatography, and gel filtration
-
recombinant enzyme mutant R466G/K468G from HEK-293T cells
-
recombinant furin from the stably transfected Sf9 insect cells
-
recombinant Her2-antigen e23sFv-TD-tBID from Escherichia coli strain M15
-
to homogeneity
-
partial
-
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
-
recombinant furin
-
on Ni2+-NTA column, 64fold
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Bfurin expressed in Sf9 cells
-
plasmid pC-BDVG-furin
-
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
-
DNA and amino acid sequence determination of neuropeptides and expression profiling, overview
PC1, DNA and amino acid sequence determination and analysis, phylogenetic tree
-
BSC40 cells infected with soluble furin
-
CHO cell lines stably expressing Tac-furin chimeric protein (extracellular/transmembrane domain of the interleukin-2 receptor alpha-chain (Tac) and the cytoplasmic domain of furin)
-
expressed in CHO cells
-
expressed in Sf9 cells using baculovirus expression system
-
expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
expression of Her2-antigen e23sFv-TD-tBID in Escherichia coli strain M15
-
full-length epitope-tagged furin constructs or mutants expressed in A7 cells or BSC-40 cells
-
full-length furin prodomain overexpressed in Escherichia coli strain BL21 (DE3)
-
furin and pro-von Willebrand factor co-expressed in BHK21 cells. cDNA of furin subcloned into the pcDNA3/VSV expression vector between the EcoRI and XbaI sites. HeLa cells transiently transfected with pCMV-furin, pCDNA3-furin-VSV or pSVHVWF1.1
-
furin expression in CHO cells, COS-7 cells, furin-deficient FD11 cells, and furin-overexpressing cells
-
furin mutant and wild-type constructs transiently transfected into HEK-293 cells
-
furin overexpressed from vaccinia virus
-
furin precursor cDNA transferred to pcDNA3.1-. Co-expression of furin-site-containing spike glycoprotein with furin cDNA in FD11 cells or CHO cells
-
HEK-293 cells transiently cotransfected with cDNA encoding V5-tagged wild-type PCSK9 and furin
-
HepG2 cells transiently transfected with furin luciferase reporter constructs pGL2-P1, pGL2-P1A and pGL2-P1B
-
human furin cDNA transfected to Huh-7 cells, HepG-2 cells and HEK-293 cells
-
LoVo cells stably expressing furin. Furin cleavage-site mutant (LNTR) transfected into COS-7 cells
-
LoVo cells transfected with vector pSVLFur encoding furin
-
MDA-MB-231 breast cancer cells stably transfected with a vector containing furin prosegment
-
mutants expressed in Sf9 cells. Mutant constructs transiently transfected in LoVo cells
-
plasmid pEFGRAPfurin expressed in CHO cells
-
recombinant expression in HEK-293 cells
-
recombinant expression of enzyme mutant R466G/K468G in HEK-293T cells
-
recombinant furin prepared in the S2 Drosophila expression system
-
recombinant hfurin from the sectreted culture media of somatomammotroph GH4C1 cells following infection with respective cDNA encoding vaccinia viruses
-
recombinant soluble C-terminus truncated furin expressed in Sf9 insect cells
-
transient expression of the enzyme in HEK-293 cells, co-expression of inhibitor mutant alpha1-antitrypsin M352R
-
vector pcDNA3-furin expressed in HEK-293 cells
-
293T cells transfected with furin
-
cDNA cloning
-
expression in COS-1 cell
-
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
-
soluble ectodomain of furin is expressed in dihydrofolate reductase-amplified CHO cells
-
stably transfected LoVo cells expressing either furin (LoVo/fur) or the vector alone (LoVo/neo)
-
DNA and amino acid sequence determination and analysis
-
cDNA sequenced, cloned from a cDNA library of Sf9 cells, overexpressed from a baculovirus vector in Sf9 cells
membrane-bound or soluble furin transiently expressed in HEK-293 cells
synthetic construct
-
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
synthetic construct
-
PCR product of the truncated mutant inserted between the EcoR1 and Not1 sites of the pFastBac1H vector, expression in Tn5 cells
determination of polyadenylation of endogenous furin transcripts
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
furin expression is detected in all rhabdomyosarcoma cell lines tested at high levels, while myoblasts and fibroblasts show low levels of furin transcripts
-
cytokine transforming growth factor TGF-beta stimulates furin mRNA expression in HepG2 cells
-
in heaptitis C virus-infected cells, furin expression is upregulated about 3fold
-
forskolin induces the enzyme expression in choriocarcinoma cells
-
the enzyme is induced by forskolin and amphiregulin, periovulatory furin expression is also increased by human chorionic gondotropin in follicles, overview
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D153A
-
inactive furin mutant, fails to up-regulate interferon gamma protein
D153N
-
is catalytically inert, is efficiently synthesized but inefficiently processed and secreted and therefore is difficult to be purified. Is incapable of self-activation, is less active than the wild-type
D4K
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G5
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G6
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H6
-
is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H66L
-
profurin mutant, shows no measurable effect on propeptide excision relative to the control (65% mature furin). No effect on the pH-triggered activation and propeptide release or on the trypsin-mediated unmasking of furin
H69K
-
profurin mutant, 80% reduced efficiency of propeptide excision, fails to be activated by acidic pH or trypsinolysis
H69L
-
profurin mutant, 70% reduced efficiency of propeptide excision. Completely blocked ability of acid pH to trigger furin activation and propeptide cleavage but shows no effect on the trypsin-mediated activation step. Propeptide fails to dissociate from mature furin
K117P
-
mutation does not affect the efficiency of autocatalytic processing and the resulting secretory mutants are capable of prodomain processing at the primary cleavage site Arg-Thr-Lys-Arg107-Asp108. Is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
K74G/R75G
-
secondary cleavage sites are inactivated, is incapable of self-activation
K74G/R75G/R107G
-
is incapable of self-activation
K74G/R75G/R89G
-
is incapable of self-activation
R107G
-
primary cleavage sites are inactivated, is incapable of self-activation
R1584A/R1585A
-
mutations efficiently protect the C-propeptide cleavage from furin activity. In absence of furin activity, bone morphogenetic protein-1 is capable of processing the C-propeptide even though less efficiently than furin
R75A
-
profurin mutant, substitution at the P1 position of the internal cleavage site, which blocks profurin activation but not propeptide excision or endoplasmic reticulum export of the furin-propeptide complex. No effect on the folding of the catalytic domain but blocked sensitivity of the furin-propeptide complex to acid pH
R89G
-
efficiency of self-activation of the mutant in which the tertiary cleavage site (Arg-Leu-Gln-Arg89Q-Glu90) is inactivated, is significantly reduced compared to that of wild-type furin
R335Q
-
cleavage mutant, soluble hemojuvelin is reduced
DELTA759-780
synthetic construct
-
furin mutant lacking both the YKGL motif and the acidic cluster, shows low-affinity interactions with Mint3
R138A
-
mutation of the furin cleavage site in the gamma subunit, gamma furin site mutation interfers with protein synthesis and/or degradation
R205A/R231A
-
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
-
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
-
the zebrafish craniofacial mutant sturgeon in the proprotein convertase FurinA displays mild blisters in the median fin folds
K74G/R75G/R89G/R107G
-
is incapable of self-activation
additional information
-
furin cleavage-site mutant, neither trifluoperazine-induced nor basal shedding causes P-stalk accumulation
additional information
-
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
-
FD11 cell line, deficient in furin protease, processing of furin-site-containing glycoproteins is abrogated
additional information
-
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
-
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
-
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
-
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
-
enhancement of productive IBV infection by knockin of furin in A-549 cells
R89G/R107G
-
is incapable of self-activation
additional information
-
LoVo/neo cells lacking functional furin are unable to activate both wild type Shiga toxin and mutant Shiga-2D toxin
additional information
-
deletion of the cysteine-rich domain and the cytoplasmic tail of furin does not abolish binding to cripto
additional information
-
production of lentiviruses carrying shRNA for furin and infection of blastocyststage embryos with the viruses, along with lentiviruses expressing EGFP
DELTA769-780
synthetic construct
-
furin mutant with a deleted acidic cluster, shows low-affinity interactions with Mint3
additional information
synthetic construct
-
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
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
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
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
-
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
-
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
industry
-
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
-
potential therapeutic value of furin inhibitors, alpha1-PDX is able to block in vivo maturation of pro-gB, the cytomegalovirus envelope glycoprotein
medicine
-
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
-
interleukin 12 induction of furin plays a role in interferon gamma protein regulation and control of T helper 1 cell differentiation
medicine
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
pharmacology
-
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
analysis
-
bioluminogenic probes can specifically image furin activity in xenografted breast cancer tumors in mice
medicine
-
some mutations of H5N1 H5 cleavage sequence fit less well into furin and hence may reduce the high pathogenicity of the H5N1 virus
medicine
-
interleukin 12 induction of furin plays a role in interferon gamma protein regulation and control of T helper 1 cell differentiation
medicine
-
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
Mus musculus C57BL/6
-
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
-
drug development
synthetic construct
-
good prospect of using quantitative structure-activity relationship models for the rational design of novel therapeutic furin inhibitors toward anthrax and furin-dependent diseases
medicine
-
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
additional information
furin A activates endothelin 1 signaling; furin B activates endothelin 1 signaling
medicine
-
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
additional information
-
Sox-9 regulates furin during chondrogenesis
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
additional information
-
Sox-9 regulates furin during chondrogenesis