1.4.3.10 (2-aminoethyl)-trimethylammonium competitive inhibitor 68897 1.4.3.10 1,1,4,4-tetramethyl-1,4-diaminobutane - 49612 1.4.3.10 1,10-Diaminodecane - 7963 1.4.3.10 1,12-diaminododecane - 5228 1.4.3.10 1,3-diaminopropane - 721 1.4.3.10 1,3-diaminopropane competitive inhibitor 721 1.4.3.10 1,6-diaminohexane - 1524 1.4.3.10 1,7-Diaminoheptane - 1960 1.4.3.10 1,8-diaminooctane - 2927 1.4.3.10 1-aminoethanol - 107860 1.4.3.10 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide the activity of the modified enzyme towards putrescine is 5.6% of that of the native enzyme. The modified enzyme shows activity towards monoamines such as n-butylamine, n-hexylamine and n-octylamine, which are not substrates of the native enzyme 3174 1.4.3.10 2-Aminoethanol - 9009 1.4.3.10 3-Amino-1-propanol - 8002 1.4.3.10 4-amino-1-butanoic acid - 49801 1.4.3.10 5-amino-1-pentanoic acid - 49841 1.4.3.10 5-amino-1-pentanol - 49842 1.4.3.10 6-amino-1-hexanoic acid - 31313 1.4.3.10 6-amino-1-hexanol - 49864 1.4.3.10 8-amino-1-octanoic acid - 49872 1.4.3.10 agmatine - 505 1.4.3.10 allylamine - 49899 1.4.3.10 Aminoethanol competitive inhibitor 15628 1.4.3.10 aminoguanidine - 1553 1.4.3.10 Aminoguanidine hydrogen carbonate - 92434 1.4.3.10 ammonium - 4224 1.4.3.10 benzylamine - 529 1.4.3.10 Butylamine - 1463 1.4.3.10 cadaverine noncompetitive against putrescine 533 1.4.3.10 Cd2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 52 1.4.3.10 Co2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 23 1.4.3.10 Cu2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 19 1.4.3.10 cyanide - 118 1.4.3.10 dodecylamine - 11199 1.4.3.10 ethylamine - 701 1.4.3.10 ethylenediamine - 4008 1.4.3.10 ethylenediamine competitive inhibitor 4008 1.4.3.10 heptylamine - 50033 1.4.3.10 Hexylamine - 7208 1.4.3.10 Hg2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 33 1.4.3.10 hydroxylamine - 85 1.4.3.10 Iproniazid - 5558 1.4.3.10 methylamine - 324 1.4.3.10 methylglyoxal bis(guanylhydrazine)dihydrochloride monohydrate - 50105 1.4.3.10 additional information short diamines and monoamines strongly inhibit activity 2 1.4.3.10 additional information not inhibited by spermidine and cadevarine 2 1.4.3.10 additional information no substrate inhibition at concentrations as high as 100 mM/l cadaverine 2 1.4.3.10 N,N,N',N'-tetramethyl-1,4-diaminobutane - 50116 1.4.3.10 n-butylamine competitive inhibitor 1381 1.4.3.10 Ni2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 38 1.4.3.10 PCMB - 78 1.4.3.10 pentylamine - 10880 1.4.3.10 Phenylethylamine - 900 1.4.3.10 Propylamine - 1419 1.4.3.10 putrescine substrate inhibition at 10 mM or above 155 1.4.3.10 putrescine substrate inhibition 155 1.4.3.10 putrescine inhibition potency of the enzyme in the combined cross-linked enzyme aggregate of monoamine oxidase and putrescine oxidase by the substrate is reduced by two-fold in comparison of the mixed free enzymes 155 1.4.3.10 spermidine competitive inhibition of putrescine oxidation 148 1.4.3.10 spermine competitive inhibition of putrescine oxidation 197 1.4.3.10 tyramine - 280 1.4.3.10 Zn2+ inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme 14