3.1.21.1 2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione - 232669 3.1.21.1 2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione - 232667 3.1.21.1 2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione - 232668 3.1.21.1 2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine - 232666 3.1.21.1 2-(4-amidinophenyl)-6-indolecarbamidine significantly inhibits DNase I activity 151313 3.1.21.1 2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine - 232665 3.1.21.1 2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine - 232663 3.1.21.1 2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine - 232662 3.1.21.1 2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine - 232664 3.1.21.1 2-mercaptoethanol inhibition, but reversal by addition of 3 mM CaCl2 63 3.1.21.1 2-mercaptoethanol inhibition after treatment with EGTA 63 3.1.21.1 2-mercaptoethanol inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction 63 3.1.21.1 2-mercaptoethanol 70% inhibition at 1 mM 63 3.1.21.1 2-mercaptoethanol slight inhibition 63 3.1.21.1 2-mercaptoethanol - 63 3.1.21.1 2-Nitro-5-thiocyanobenzoic acid inhibition at identical rates 10489 3.1.21.1 2-Nitro-5-thiocyanobenzoic acid inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135 10489 3.1.21.1 2-nitro-5-thiosulfobenzoic acid the presence of Ca2+ or Mg2+ at pH 7.5 results in 80% inactivation without fragmentation of the enzyme. In the absence of metal ions it retains 80% of its activity. It binds DNase I through covalent modification, since dialysis and gel filtration can not reverse the inactivation reaction. After dilution into an acid buffer of pH 4.7, the inactivated enzyme regains about 40% of its initial activity. The inhibitor fails to inactivate other enzymes, suggesting that the inhibition is unique to DNase I 74901 3.1.21.1 2-nitro-5-thiosulfobenzoic acid is a novel inhibitor specific for DNase I 74901 3.1.21.1 3'-AMP - 652 3.1.21.1 5'-deoxy-GMP competitive, product inhibition 53884 3.1.21.1 5'-GDP - 53886 3.1.21.1 5'-GMP - 1022 3.1.21.1 5'-GTP - 53885 3.1.21.1 actin 40 mM HEPES pH 7.0, 5 mM MgCl2, 1 mM CaCl2 796 3.1.21.1 actin inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage 796 3.1.21.1 actin inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone 796 3.1.21.1 actin inhibits the DNA-nicking activity of DNAse I/CdtB chimera 796 3.1.21.1 Aflatoxin B2a non-competitive inhibitor 92316 3.1.21.1 Aflatoxin G2 non-competitive inhibitor 92317 3.1.21.1 Aflatoxin G2a non-competitive inhibitor 92318 3.1.21.1 Aflatoxin M1 non-competitive inhibitor 92319 3.1.21.1 Ag2+ - 1041 3.1.21.1 Al3+ - 264 3.1.21.1 Aprotinin inhibits DNase1 as a result of plasmin inhibition 405 3.1.21.1 aurintricarboxylic acid i.e ATA, a general inhibitor of nucleases, weak inhibition 1818 3.1.21.1 Bile acids inhibit the enzyme in concert with cholesterol sulfate 10606 3.1.21.1 Ca2+ inhibitory above 1 mM 15 3.1.21.1 Ca2+ complete inhibition at 1-10 mM 15 3.1.21.1 Ca2+ 80% inhibition at 0.1 mM 15 3.1.21.1 Ca2+ slight inhibition of mutant D201A 15 3.1.21.1 calf spleen inhibitor protein II molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7 102584 3.1.21.1 calf thymus inhibitor protein molecular weight: 49000 Da, maximum stability at pH 6 102585 3.1.21.1 carbodiimide presence of divalent cations slows the rate of inactivation 5948 3.1.21.1 Cholesterol sulfate from human gastric fluid, the sulfate group and the hydrophobic side chain of cholesterol sulfate are indispensable for the inhibitory effect, irreversible, dependent on bile acids, a ratio of 342:1 of bile acids to cholesterol sulfate is required for complete inhibition 6498 3.1.21.1 Co2+ - 23 3.1.21.1 Crystal violet - 15685 3.1.21.1 Cu-iodoacetate at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min 102638 3.1.21.1 Cu2+ complete inhibition 19 3.1.21.1 Cu2+ complete inhibition at 1-10 mM 19 3.1.21.1 Cu2+ - 19 3.1.21.1 diphosphate - 17 3.1.21.1 dithiothreitol - 45 3.1.21.1 DTT 80% inhibition at 1 mM 177 3.1.21.1 E2-immunity protein complete inhibition of activity on plasmid DNA 102750 3.1.21.1 EDTA complete inhibition at 10 mM 21 3.1.21.1 EDTA - 21 3.1.21.1 EDTA 50% inhibition at 0.3 mM 21 3.1.21.1 EDTA slight inhibition 21 3.1.21.1 EDTA complete inhibition at 20 mM 21 3.1.21.1 EDTA complete inhibition at 1 mM 21 3.1.21.1 EDTA complete ihibition at 1 mM; complete inhibition at 1 mM 21 3.1.21.1 EDTA inhibition observed above 50 microM, complete inhibition at 0.5 mM 21 3.1.21.1 EDTA complete inhibition at 5 mM 21 3.1.21.1 EDTA 10 mM, complete loss of activity 21 3.1.21.1 EDTA current peaks of the Fc-oligo-SH-immobilized electrode are relatively stable within error before and after treatment of DNase I solution with EDTA or RNaseA solution, suggesting that this electrode can be used for the detection of DNase I activity specifically 21 3.1.21.1 EGTA - 173 3.1.21.1 EGTA complete inhibition at 10 mM 173 3.1.21.1 EGTA inhibition at 1 mM 173 3.1.21.1 EGTA activity inhibited 173 3.1.21.1 EGTA inhibition at 0.01 mM in the presence of 2.5 mM Mg2+ 173 3.1.21.1 EGTA complete inhibition of the enzyme from serum at 5 mM 173 3.1.21.1 EGTA complete inhibition at 5 mM 173 3.1.21.1 EGTA complete inhibition at 1 mM 173 3.1.21.1 EGTA complete ihibition at 1 mM; complete inhibition at 1 mM 173 3.1.21.1 EGTA 1 mM, complete loss of activity 173 3.1.21.1 Fe3+ - 70 3.1.21.1 G-actin - 3702 3.1.21.1 G-actin inhibition with actin-gelsolin segment I complex 3702 3.1.21.1 G-actin 50% inhibition at 0.002 mg/ml 3702 3.1.21.1 G-actin complete inhibition at 0.05 mg/ml 3702 3.1.21.1 G-actin DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity 3702 3.1.21.1 G-actin 15% inactivation at 0.004 mg 3702 3.1.21.1 G-actin 66% inhibition in an 1:1 molar ratio of DNase I-actin complex 3702 3.1.21.1 G-actin complete inhibition at 0.001 mg 3702 3.1.21.1 G-actin specific, strong inhibition 3702 3.1.21.1 G-actin slight inhibition 3702 3.1.21.1 G-actin heat labile inhibitor of DNase 1, released from white blood cells and platelets. Binds to and almost completely inhibits the nucleolytic activity of DNase 1. Inhibition of DNase 1 by actin (about 95% inhibition at equimolar ratio) requires ATP and leads both to the inhibition of DNase 1 and the depolymerization of the actin 3702 3.1.21.1 gamma-actin - 10967 3.1.21.1 guanidinium hydrochloride over 80% inhibition at 0.5 M 3124 3.1.21.1 heparin - 227 3.1.21.1 heparin directly inhibits recombinant DNase1/3 227 3.1.21.1 Hg2+ - 33 3.1.21.1 HPO42- - 2843 3.1.21.1 iodoacetate 50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min 93 3.1.21.1 iodoacetate complete inhibition 93 3.1.21.1 iodoacetate inhibition in the presence of Mn2+ or Ca2+ at pH 7.2 93 3.1.21.1 iodoacetate formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation 93 3.1.21.1 iodoacetate strong inhibition in presence of Cu2+ 93 3.1.21.1 K+ no inhibition at 50 mM, 50% inhibition at 200 mM 39 3.1.21.1 KCl less inhibitory than NaCl 79 3.1.21.1 KCl stimulating between 25 and 50 mM, inhibitory above 50 mM 79 3.1.21.1 LiCl - 815 3.1.21.1 mannitol inhibition of enzyme activity during the entire growth period of seedlings 1791 3.1.21.1 mannitol induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days 1791 3.1.21.1 methanesulfonylchloride inactivation at pH 5.0 103017 3.1.21.1 Mg2+ - 6 3.1.21.1 additional information no inhibition by G-actin 2 3.1.21.1 additional information no inhibition by G-actin; no inhibition by G-actin 2 3.1.21.1 additional information no inhibition by sulfatides and membrane lipids, galactose ceramide, no inhibition by steroid sulfates such as estrone sulfate, pregnenolone sulfate, dehydroepiandrosterone sulfate, no inhibition by DMSO, Tween 20, sodium cholate, and sodium taurocholate 2 3.1.21.1 additional information no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes 2 3.1.21.1 additional information the phosphate residue is responsible for the inhibitory effect of guanosine 5'-nucleotides 2 3.1.21.1 additional information resistant to trypsin inactivation in absence of Ca2+ 2 3.1.21.1 additional information is resistant to trypsin 2 3.1.21.1 additional information thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I 2 3.1.21.1 additional information DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks 2 3.1.21.1 additional information G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms 2 3.1.21.1 additional information DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations 2 3.1.21.1 additional information efficiency of cleavage of DNA duplex on gold nanoparticles by DNase I is about 82% whereas the cleavage efficiency in solution phase at the same conditions is nearly 100%. Cleavage efficiencies using Pb2+-mediated DNA enzyme on gold nanoparticles and in solution phase are about 55% and 95%, respectively 2 3.1.21.1 N-bromosuccinimide inactivation by modification at Trp155 208 3.1.21.1 N-bromosuccinimide modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity 208 3.1.21.1 Na+ no inhibition at 50 mM, 50% inhibition at 200 mM 59 3.1.21.1 NaCl 10fold lower activity at 150 mM 42 3.1.21.1 NaCl 50% inhibition at 60 mM, mutated enzyme less sensitive against increased salt concentrations 42 3.1.21.1 NaCl inhibitory at concentrations below 100 mM 42 3.1.21.1 NaCl decreasing activity with increasing ionic strength 42 3.1.21.1 NaCl - 42 3.1.21.1 NaCl Na-DNA is inhibitory 42 3.1.21.1 NaCl 50% inhibition at 80 mM and pH 5.8 and at 165 mM and pH 7.0 42 3.1.21.1 NaCl inhibitory at concentrations above 80 mM 42 3.1.21.1 NaCl stimulating between 25 and 50 mM, inhibitory above 50 mM 42 3.1.21.1 NaCl increasing concentrations of NaCl (approximately half activity in the presence of 50 mM NaCl) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (approximately half activity in the presence of 150 mM NaCl) 42 3.1.21.1 Ni2+ - 38 3.1.21.1 oligonucleotides competitive inhibition 1834 3.1.21.1 P2O74- - 12650 3.1.21.1 phosphate - 16 3.1.21.1 plasmin directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1 4317 3.1.21.1 protein Im9 an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell 129666 3.1.21.1 RNA enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA 527 3.1.21.1 SDS - 124 3.1.21.1 SDS over 80% inhibition at 0.04% w/v 124 3.1.21.1 Somatostatin 2 enzyme forms: a somatostatin-sensitive and a somatostatin-resistant, controls the enzyme level in the lower gut, in vivo transient down-regulation of gene expression of the sensitive enzyme form 6593 3.1.21.1 Tris increasing concentrations of Tris (approximately half activity in the presence of 80 mM Tris) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (no inhibitory influence of Tris) 317 3.1.21.1 Tris-HCl buffer - 6606 3.1.21.1 Tris-HCl buffer inhibition at high concentration 6606 3.1.21.1 Trypsin is less resistant to trypsin than human DNase I, DNase I activity decreases gradually 393 3.1.21.1 Urea 20% inhibition at 4 M 116 3.1.21.1 Zn2+ inhibition at millimolar concentrations 14 3.1.21.1 Zn2+ complete inhibition 14 3.1.21.1 Zn2+ complete inhibition at 1-10 mM 14 3.1.21.1 Zn2+ complete inhibition at 1 mM 14 3.1.21.1 Zn2+ - 14