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3.4.21.75: Furin

This is an abbreviated version!
For detailed information about Furin, go to the full flat file.

Word Map on EC 3.4.21.75

Reaction

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 =

Synonyms

Bfurin, Dfurin1, Dibasic processing enzyme, FUR, furin, furin A, furin B, furin convertase, furin protease, furin-like pro-protein convertase, furin-like prohormone convertase, furin-like proprotein convertase, furin-like protease, furin-like proteinase, FurinA, furinase, hfurin, KPC-1, More, PACE, Paired basic amino acid cleaving enzyme, Paired basic amino acid converting enzyme, Paired basic amino acid residue cleaving enzyme, PC1, PC1/3, PC2, PCSK3, proconvertase, prohormone convertase, prohormone convertase 1, prohormone convertase 2, Proprotein convertase, proprotein convertase subtilisin/kexin 3, proprotein convertase subtilisin/kexin type 3, proprotein convertase subtilisin/kexin type3, Serine proteinase PACE, Sfurin, sheddase, SPC3, subtilisin-like proprotein convertase, subtilisin-like protein convertase, Trans golgi network protease furin

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.75 Furin

Crystallization

Crystallization on EC 3.4.21.75 - Furin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme furin in complexes with inhibitors N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde, N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide, N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide, N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide, diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate, diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate, and diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate, vapor diffusion method, 9.0 mg/ml glycosylated human furin in 10 mm HEPES, pH 7.5, 100 mm NaCl, and 2 mm CaCl2 is mixed with an equal volume of crystallization solution containing 100 mm MES, 200 mm K/NaH2PO4, pH 5.5-6.0, and 2m NaCl, and equilibrated against reservoir solution with 3.0-3.6m NaCl, at 20°C, crystals are soaked for 16 h in soaking solution containing 3.13 M NaCl, 100 mM Mes/NaOH, pH 5.5, 200 mM NaH2PO4, 1 mM CaCl2, and 20% DMSO supplemented with inhibitor N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde (5 mM), N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide (5 mM), N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide (5 mM), N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide (5 mM), diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate (5 mM), diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate (1 mM), or diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate (1 mM), X-ray diffraction structure determination and analysis
purified furin in complex with a non-substrate-like small molecule inhibitor N,N'-[[(1S,3R,4R,6S)-4-carbamimidamido-6-(4-carbamimidamidoanilino)cyclohexane-1,3-diyl]bis(oxy-4,1-phenylene)]diguanidine, hexagonal crystals of unliganded furin are soaked in a 5 mM solution of inhibitor in 100 mM MES, pH 5.5, 200 mM K/NaH2PO4, 1 mM CaCl2, 10% DMSO, and 3.4 mM NaCl for 16 h, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified recombinant enzyme in complex with inhibitors m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine or phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, mixing of 7.5 mg/ml enzyme with 0.290 mM m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine and 3 mM phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, respectively, and 50 mM Tris, pH 8.5, 2.8 M sodium formate and 0.015 mM Cymal-7, at 30°C, displacement of the highly potent inhibitor m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine by competitive soaking with excessive amounts of the less potent phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine, X-ray diffraction structure determination and analysis at 2.7 A resolution
purified recombinant furin mutant N387D/N440D in nonglycosylated apo-form, vapor diffusion method, 400 nl of 6 mg/ml of apo-furin (aa108-574-TEV-FLAG-His6 N387D/N440D) in 10 mM HEPES, pH 7.5, 150 mM NaCl, and 5 mM CaCl2, is mixed with 400 nl of crystallization solution containing 11-13% PEG 8000, 0.11-0.16 M potassium dihydrogen phosphate, and 0.1 M HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 1.89 A resolution. The nonglycosylated furin protein reliably forms extremely durable apo crystals that diffract to high resolution, crystals are stable at 4°C for over one year. Digestion with TEV protease for the removal of the His6 and FLAG tags is not necessary for crystallization
purified recombinant His-tagged enzyme in complexes with three peptide-derived inhibitors, vapor diffusion method, mixing of 9 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, and 2 mM CaCl2, with an equal volume of crystallization solution containing 100 mM MES, 200 mM K/NaH2PO4, pH 5.5-6.0, 3-4 M NaCl, and 3% dimethyl sulfoxide, and equilibration against reservoir solution containing 3-4 M NaCl, 20°C, crystals are soaked for about 16 h in a soaking solution conatining 3.16 M NaCl, 100 mM MES/NaOH, pH 5.5, 200 mM Na/KH2PO4, and 1 mM CaCl2 and supplemented with 2 mM Arg-Arg-Arg-Val-Arg-4-aminomethyl-benzamidine, or 1 mM phenylacetyl-Cit-Val-Arg-4-aminomethyl-benzamidine, or 1 mM 4-aminomethyl-phenylacetyl-Arg-Tle-Arg-4-aminomethyl-benzamidine, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
purified unliganded furin in different functional states, different Ca2+- and inhibitor (3-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(4-amidomethyl)-benzamidine)-bound forms of the enzyme, crystals of human furin are grown in sitting drops mixing equal volumes of 9 mg/ml protein solution and crystallization solution containing 100 mM MES, 200 mM K/NaH2PO4, pH 5.5-6.0, 3-4 M NaCl, and 3% v/v DMSO, the reservoir contains 3-4 M NaCl, for inhibitor binding studies the crystals are soaked with inhibitor and for calcium-studies the crystals are soaked with EDTA and Ca2+, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution
crystal structure of furin with bound decanoyl-Arg-Val-Lys-Arg-chloromethylketone inhibitor
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triclinic crystals, space group P1, unit cell dimensions a = 93.3 A, b = 135.4 A, c = 137.8 A
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