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putrescine + NAD+ + H2O = ?
-
putrescine + O2 + H2O = 4-aminobutanal + NH3 + H2O2
395442, 395449, 395441, 395445, 395436, 395437, 395438, 395443, 395446, 395447, 395448, 395450, 288077, 395444, 395440, 687763, 726504, 724314, 742489, 742361, 725184, 724877, 684634, 654187
-
putrescine + O2 + H2O = ?
-
1,4-diaminobutane + H2O + O2 = ?
-
putrescine + H2O + O2 = 4-aminobutanal + NH3 + H2O2
-
putrescine + H2O + O2 = 4-aminobutyraldehyde + NH3 + H2O2
-
putrescine + H2O + O2 = ?
-
1,4-diaminobutane + H2O + O2 = 4-aminobutanal + NH3 + H2O2
391940, 391941, 391922, 391923, 391947, 391920, 391952, 391953, 689424, 391944, 391948, 391959, 391925, 391926, 391945, 391943, 391954, 391935, 724291, 720756, 347973
-
putrescine + H2O + O2 = 4-aminobutanal + NH3 + H2O2
-
putrescine + H2O + O2 = ?
725810, 656295, 672200, 725767, 672448, 686654, 743259, 675098, 741597, 741656, 685658, 655478, 704172, 675286, 702356, 742953, 672497
-
putrescine + H2O + O2 = ? + NH3 + H2O2
-
putrescine + H2O + O2 = gamma-aminobutyraldehyde + NH3 + H2O2
-
putrescine + H2O + 2,6-dichlorophenol indophenol = 4-aminobutanal + NH3 + reduced 2,6-dichlorophenol indophenol
-
L-aspartate 4-semialdehyde + putrescine + NADPH + H+ = carboxyspermidine + H2O + NADP+
-
S-adenosyl-L-methionine + putrescine = S-adenosyl-L-homocysteine + N-methylputrescine
485443, 485444, 485446, 485448, 676574, 676729, 720663, 756809, 676557, 706130, 676734, 485449, 676699, 485447, 676733, 703724, 706106, 719169, 756127, 485445, 758065
-
S-adenosyl-L-methionine + putrescine = S-adenosylhomocysteine + N-methylputrescine
-
carbamoyl phosphate + diaminobutane = phosphate + ?
-
carbamoyl phosphate + putrescine = phosphate + N-carbamoyl-putrescine
-
carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine
-
4-coumaroyl-CoA + putrescine = CoA + N-coumaroylputrescine
-
4-fluorocinnamoyl-CoA + putrescine = CoA + N-4-fluorocinnamoylputrescine
-
caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine
-
cinnamoyl-CoA + putrescine = CoA + N-cinnamoylputrescine
-
coumaroyl-CoA + putrescine = CoA + N-coumaroylputrescine
-
feruloyl-CoA + putrescine = CoA + N-feruloylputrescine
-
sinapoyl-CoA + putrescine = CoA + N-sinapoylputrescine
-
2 sinapoyl-CoA + putrescine = ?
-
acetyl-CoA + 1,4-butanediamine = ?
-
acetyl-CoA + putrescine = ?
-
acetyl-CoA + putrescine = CoA + acetylputrescine
-
acetyl-CoA + putrescine = CoA + N-acetylputrescine
-
acetyl-CoA + putrescine = CoA + N1-acetylputrescine
-
feruloyl-CoA + putrescine = CoA + feruloylputrescine
-
p-coumaroyl-CoA + putrescine = CoA + p-coumaroylputrescine
-
Ac-PQLPF-NH2 + putrescine = ?
-
dimethyl casein glutamine + putrescine = ?
-
N,N-dimethylcasein + putrescine = ?
-
protein-bound gamma-glutamine + putrescine = ?
-
putrescine + bovine muscle actin = ?
-
putrescine + casein = ?
-
putrescine + fibronectin = ?
-
putrescine + L-glutamine = bis-(glutamyl)-putrescine
-
putrescine + light-harvesting complex of photosystem II = ?
-
putrescine + N,N'-dimethylcasein = ?
487852, 487825, 487831, 487832, 487836, 487837, 487840, 487846, 487848, 487866, 658929, 487854, 487857, 487850, 487875, 487861
-
putrescine + N,N-dimethylcasein = ?
-
thylakoid protein + putrescine = ?
-
Z-Gln-Gly + putrescine = ?
-
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
-
S-5'-deoxyadenosyl-5'-3-butylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-butylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-butylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-ethylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-ethylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-ethylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-propylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-propylthiopropylamine + 1,4-diaminobutane = ?
S-5'-deoxyadenosyl-5'-3-propylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489861, 489862, 489867, 489872, 489876, 489878, 639693, 639705, 639688, 639712, 639718, 639689, 639710, 639714, 639700, 639697, 489866, 489871
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489861, 489862, 489867, 489872, 489876, 489878, 639693, 639705, 639688, 639712, 639718, 639689, 639710, 639714, 639700, 639697, 489866, 489871
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489861, 489862, 489867, 489872, 489876, 489878, 639693, 639705, 639688, 639712, 639718, 639689, 639710, 639714, 639700, 639697, 489866, 489871
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-(5')-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-3-butylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-butylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-butylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-carboxymethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-carboxymethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-carboxymethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489862, 489866, 489867, 489870, 489872, 489876, 489878, 639693, 639700, 639705, 639688, 639697, 639714, 639712, 639718, 639689, 489861
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489862, 489866, 489867, 489870, 489872, 489876, 489878, 639693, 639700, 639705, 639688, 639697, 639714, 639712, 639718, 639689, 489861
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane = 5'-methylthioadenosine + spermidine
392545, 639702, 639704, 639706, 639707, 639709, 489862, 489866, 489867, 489870, 489872, 489876, 489878, 639693, 639700, 639705, 639688, 639697, 639714, 639712, 639718, 639689, 489861
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfone + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfone + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfone + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfoxide + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfoxide + 1,4-diaminobutane = ?
S-adenosyl-3-thiopropylamine sulfoxide + 1,4-diaminobutane = ?
S-adenosyl-5',1-methyl-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-5',1-methyl-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-5',1-methyl-3-methylthiopropylamine + 1,4-diaminobutane = ?
S-adenosyl-L-ethionine + 1,4-diaminobutane = ?
S-adenosyl-L-ethionine + 1,4-diaminobutane = ?
S-adenosyl-L-ethionine + 1,4-diaminobutane = ?
S-adenosyl-L-homocysteine sulfone + 1,4-diaminobutane = ?
S-adenosyl-L-homocysteine sulfone + 1,4-diaminobutane = ?
S-adenosyl-L-homocysteine sulfone + 1,4-diaminobutane = ?
S-adenosyl-L-methionine + 1,4-diaminobutane = ?
S-adenosyl-L-methionine + 1,4-diaminobutane = ?
S-adenosyl-L-methionine + 1,4-diaminobutane = ?
5'-methyl,5'-deoxymethylthioadenosine + putrescine = ?
5'-methyl,5'-deoxymethylthioadenosine + putrescine = ?
5'-methyl,5'-deoxymethylthioadenosine + putrescine = ?
putrescine + (methyl-14C)-S-adenosylmethioninamine = spermidine + ?
putrescine + (methyl-14C)-S-adenosylmethioninamine = spermidine + ?
putrescine + (methyl-14C)-S-adenosylmethioninamine = spermidine + ?
putrescine + S-5'-deoxyadenosyl-(5')-3-methylthiopropylamine = spermidine + ?
putrescine + S-5'-deoxyadenosyl-(5')-3-methylthiopropylamine = spermidine + ?
putrescine + S-5'-deoxyadenosyl-(5')-3-methylthiopropylamine = spermidine + ?
putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine
putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine
putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylthio)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylthio)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylthio)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine = spermidine + 5'-methylthioadenosine
S-adenosylmethioninamine + putrescine = spermidine + 5'-methylthioadenosine
S-adenosylmethioninamine + putrescine = spermidine + 5'-methylthioadenosine
S-adenosylmethioninamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
-
putrescine + 1,3-diaminopropane = homospermidine + spermidine
putrescine + 1,3-diaminopropane = homospermidine + spermidine
putrescine + 1,3-diaminopropane = homospermidine + spermidine
putrescine + 1,3-diaminopropane = homospermidine + spermidine
putrescine + 1,6 diaminohexane = homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
putrescine + 1,6 diaminohexane = homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
putrescine + 1,6 diaminohexane = homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
putrescine + 1,6 diaminohexane = homospermidine + N-(4-aminobutyl)-1,6-diaminohexane
putrescine + 1,7-diaminoheptane = homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
putrescine + 1,7-diaminoheptane = homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
putrescine + 1,7-diaminoheptane = homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
putrescine + 1,7-diaminoheptane = homospermidine + N-(4-aminobutyl)-1,7-diaminoheptane
putrescine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
putrescine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
putrescine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
putrescine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
putrescine = sym-homospermidine + NH3 + H+
putrescine = sym-homospermidine + NH3 + H+
putrescine = sym-homospermidine + NH3 + H+
putrescine = sym-homospermidine + NH3 + H+
spermidine + putrescine = homospermidine + 1,3-diaminopropane
spermidine + putrescine = homospermidine + 1,3-diaminopropane
spermidine + putrescine = homospermidine + 1,3-diaminopropane
spermidine + putrescine = homospermidine + 1,3-diaminopropane
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine + putrescine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine + putrescine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine + putrescine
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine + putrescine
putrescine + spermidine = N-(4-aminobutyl)butane-1,4-diamine + propane-1,3-diamine
676383, 660106, 638080, 638084, 706129, 288699, 638089, 638062, 638090, 638091, 638088
-
putrescine + spermidine = sym-homospermidine + propane-1,3-diamine
-
putrescine + spermine = sym-homospermine + propane-1,3-diamine
-
spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
-
1-ethylspermidine + putrescine = homospermidine + ?
1-methylspermidine + putrescine = homospermidine + ?
8-ethylspermidine + putrescine = ethylhomospermidine + ?
8-methylspermidine + putrescine = methylhomospermidine + ?
caldine + putrescine = spermidine + ?
homospermidine + putrescine = homospermidine + ?
N-(3-aminopropyl)-1,4-diamino-cis-but-2-ene + putrescine = (1Z)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
N-(3-aminopropyl)-1,4-diamino-trans-but-2-ene + putrescine = (1E)-N4-(4-aminobutyl)but-1-ene-1,4-diamine + 1,3-diaminopropane
spermidine + putrescine = homospermidine + ?
putrescine + pyruvate = 4-aminobutanal + alanine
-
putrescine + 2-oxoglutarate = L-glutamate + 4-aminobutanal
-
putrescine + 2-oxoglutarate = L-glutamate + 4-aminobutanol
-
putrescine + 2-oxoglutarate = 4-aminobutanal + L-glutamate
-
putrescine + pyruvate = 4-aminobutanal + L-alanine
-
1,4-diaminobutane + pyruvate = ? + L-alanine
-
alpha-ketobutyric acid + putrescine = L-aspartate + 4-aminobutanal
putrescine + 2-oxoglutarate = 1-pyrroline + L-glutamate + H2O
putrescine + 2-oxoglutarate = L-glutamate + 4-aminobutanal
pyruvate + putrescine = L-alanine + 4-aminobutanal
1-phenylpentane-2,4-dione + putrescine = ?
-
4-phenylbutan-2-one + putrescine = ?
-
ATP + glutamate + putrescine = ADP + phosphate + gamma-L-glutamylputrescine
-
ATP + L-glutamate + putrescine = ADP + phosphate + gamma-L-glutamylputrescine
-
ATP + H2O + putrescine/out = ADP + phosphate + putrescine/in
-
putrescine/out + ATP + H2O = putrescine/in + ADP + phosphate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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up to 50% stimulation at 1 mm
-
activates, inhibitory at optimal Mg2+ concentration
-
aliphatic, positively charged polyamine, required for in vitro activity of ORF47, polyamine depletion leads to 80% reduced activity
-
optimal polymerization activity requires polyamines, 2fold increase in activity at 30 mM
-
can replace missing Mg2+ to a small extent
-
divalent cation, metal or polyamine is required, 0.01 M putrescine is as effective as Mg2+
-
activate in presence of Mg2+, no activation in absence of Mg2+. Effective at 2-5 mM
-
in presence of Mg2+ and Ca2+
-
activity is increased 6fold at 10 mM
-
maximal stimulation at 6 mM
-
at 0.1 mM concentration enhances arginase activity by 18%
-
but it inhibits at concentrations about 14 mM agmatine
-
treatment of peach shoots from Mochizuki with exogenous putrescine (indirect product of ADC) remarkably induces accumulation of ADC mRNA, incubation of shoots in 1 and 5 mM exogenous putrescine for 2 days leads to obvious and significant increase in endogenous putrescine
-
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
0.25 mM required for maximal activation
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
accelarates the conversion of the proenzyme into the enzyme subunits
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
enhances activity up to 350fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
increase of kcat up to 9fold
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
maximal stimulation at 1 mM
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
stimulation
4668, 4675, 4693, 4673, 4678, 4679, 4682, 4676, 4684, 4687, 4694
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
enhances activity against poly(C) and yeast RNA
-
can replace Mg2+ in activation with 27% efficiency in aminoacylation
-
enhances activity, optimum concentrations is 0.07 mM
-
can partially replace Mg2+ in activation, with 32% efficiency
-
optimal concentration: 5.5 mM
-
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Unusual enzyme characteristics of aspartyl-tRNA synthetase from hyperthermophilic archaeon Pyrococcus sp. KOD1
1996
Fujiwara, S.; Lee, S.; Haruki, M.; Kanaya, S.; Takagi, M.; Imanaka, T.
FEBS Lett.
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Amino acid substrate specificity of asparaginyl-, aspartyl- and glutaminyl-tRNA synthetase isolated from higher plants
1973
Lea, P.J.; Fowden, L.
Phytochemistry
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Characteristics of a leucine aminoacyl transfer RNA synthetase from Tritrichomonas augusta
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Horner, J.; Champney, W.S.; Samuels, R.
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Some properties of the theanine synthesizing enzyme in tea seedlings
1965
Sasaoka, K.; Kito, M.; Onishi, Y.
Agric. Biol. Chem.
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A multienzyme complex of carbamoyl-phosphate synthase (glutamine):aspartate carbamoyltransferase:dihydroorotase (rat ascites hepatoma cells and rat liver)
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Mori, M.; Tatibana, M.
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Studies on the fermentation of D-alpha-lysine. Purification and properties of an adenosine triphosphate regulated B12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium sticklandii
1970
Morley, C.G.D.; Stadtman, T.C.
Biochemistry
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Isolation and characterization of the mouse ornithine decarboxylase gene
1988
Katz, A.; Kahana, C.
J. Biol. Chem.
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7604-7609
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Ornithine decarboxylase from embryos of jute seeds
1988
Pandit, M.; Ghosh, B.
Phytochemistry
27
1609-1610
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Purification and properties of ornithine decarboxylase from germinated barley seeds
1988
Koromilas, A.E.; Kyriakidis, D.A.
Phytochemistry
27
989-992
Molecular properties of ornithine decarboxylase from mouse kidney. Detailed comparison with those of the enzyme from rat liver
1988
Kitani, T.; Fujisawa, H.
J. Biochem.
103
547-553
Ornithine decarboxylase from mouse epidermis and epidermal papillomas: differences in enzymatic properties and structure
1986
O'Brien, T.G.; Madara, T.; Pyle, J.A.; Holmes, M.
Proc. Natl. Acad. Sci. USA
83
9448-9452
Purification of mouse brain ornithine decarboxylase reveals its presence as an inactive complex with antizyme
1986
Laitinen, P.H.; Hietala, O.A.; Pulkka, A.E.; Pajunen, A.E.I.
Biochem. J.
236
613-616
Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney
1985
Seely, J.E.; Persson, L.; Sertich, G.J.; Pegg, A.E.
Biochem. J.
226
577-586
Characterization of highly purified ornithine decarboxylase from rat heart
1984
Flamigni, F.; Guarnieri, C.; Caldarera, C.M.
Biochim. Biophys. Acta
802
245-252
Ornithine decarboxylase (mouse kidney)
1983
Seely, J.E.; Pegg, A.E.
Methods Enzymol.
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158-161
Ornithine decarboxylase (Saccharomyces cerevisiae)
1983
Tyagi, A.K.; Tabor, C.W.; Tabor, H.
Methods Enzymol.
94
135-139
Ornithine decarboxylase in mouse kidney. Purification, characterization, and radioimmunological determination of the enzyme protein
1983
Isomaa, V.V.; Pajunen, A.E.I.; Bardin, C.W.; Jaenne, O.A.
J. Biol. Chem.
258
6735-6740
Ornithine decarboxylase activity from an extremely thermophilic bacterium, Clostridium thermohydrosulfuricum
1983
Paulin, L.; Poesoe, H.
Biochim. Biophys. Acta
742
197-205
Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a
1980
Guirard, B.M.; Snell, E.E.
J. Biol. Chem.
255
5960-5964
Studies on ornithine decarboxylase from the liver of thioacetamide-treated rats
1972
Ono, M.; Inoue, H.; Suzuki, F.; Takeda, Y.
Biochim. Biophys. Acta
284
285-297
Partial purification and characterization of ornithine decarboxylase from Entamoeba histolytica
1996
Arteaga-Nieto, P.; Villagomez-Castro, J.C.; Calvo-Mendez, C.; Lopez-Romero, E.
Int. J. Parasitol.
26
253-260
Panagrellus redivivus ornithine decarboxylase: structure of the gene, expression in Escherichia coli and characterization of the recombinant protein
1996
Niemann, G.; von Besser, H.; Walter, R.D.
Biochem. J.
317
135-140
Plasmodium falciparum: purification, properties, and immunochemical study of ornithine decarboxylase, the key enzyme in polyamine biosynthesis
1988
Assaraf, Y.G.; Kahana, C.; Spira, D.T.; Bachrach, U.
Exp. Parasitol.
67
20-30
Purification and some properties of rat intestinal ornithine decarboxylase
1989
Miyamoto, K.; Oka, T.; Fujii, T.; Yamaji, M.; Minami, H.; Nakabou, Y.; Hagihira, H.
J. Biochem.
106
167-171
Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by a alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites
1992
Poulin, R.; Lu, L.; Ackermann, B.; Bey, P.; Pegg, A.E.
J. Biol. Chem.
267
150-158
Characterization of a high affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans
1990
Schaeffer, J.M.; Donatelli, M.R.
Biochem. J.
270
599-604
Trichomonas vaginalis: characterization of ornithine decarboxylase
1993
Yarlett, N.; Goldberg, B.; Moharrami, M.A.; Bacchi, C.J.
Biochem. J.
293
487-493
Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors
1993
Coleman, C.S.; Stanley, B.A.; Pegg, A.E.
J. Biol. Chem.
268
24572-24579
Hepatic ornithine decarboxylase from the frog, Rana negromaculata: dietary induction, purification and some properties
1991
Baby, T.G.; Hayashi, S.
Comp. Biochem. Physiol. B
99
151-156
Properties of purified L-ornithine decarboxylase (EC 4.1.1.17) from Tetrahymena thermophila
1989
Eichler, W.
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36
577-582
Methods for the study of the experimental interruption of pregnancy by ornithine decarboxylase inhibitors
1983
Fozard, J.R.; Part, M.L.
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Immunocytochemical localization of ornithine decarboxylase
1983
Persson, L.; Rosengren, E.; Sundler, F.; Uddman, R.
Methods Enzymol.
94
166-169
Autoradiographic localization of ornithine decarboxylase
1983
Zagon, I.S.; Seely, J.E.; Pegg, A.E.
Methods Enzymol.
94
169-176
-
Arginine decarboxylase of oat seedlings
1979
Smith, T.A.
Phytochemistry
18
1447-1452
Arginine decarboxylase from a Pseudomonas species
1976
Rosenfeld, H.J.; Roberts, J.
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125
601-607
Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties
1975
Ramakrishna, S.; Adiga, P.R.
Eur. J. Biochem.
59
377-386
Purification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls
1997
Nam, K.H.; Lee, S.H.; Lee, J.
Plant Cell Physiol.
38
1150-1155
Agmatine is synthesized by a mitochondrial arginine decarboxylase in rat brain
1995
Li, G.; Regunathan, S.; Reis, D.J.
Ann. N. Y. Acad. Sci.
763
325-329
Modulation of arginine decarboxylase activity from Mycobacterium smegmatis
1989
Balasundaram, D.; Tyagi, A.K.
Eur. J. Biochem.
183
339-345
-
Purification and partial characterization of arginine decarboxylase from Brassica campestris
1996
Das, S.; Bhaduri, T.J.; Bose, A.; Ghosh, B.
J. Plant Biochem. Biotechnol.
5
123-126
Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by berenil, pentamidine and methylglyoxal bis(guanylhydrazone)
1986
Bitonti, A.J.; Dumont, J.A.; McCann, P.P.
Biochem. J.
237
685-689
S-Adenosylmethionine decarboxylase and spermidine synthase from Chineses cabbage
1985
Yamanoha, B.; Cohen, S.S.
Plant Physiol.
78
784-790
Methionine adenosyltransferase (S-adenosylmethionine synthetase) and S-adenosylmethionine decarboxylase
1984
White Tabor, C.; Tabor, H.
Adv. Enzymol. Relat. Areas Mol. Biol.
56
251-282
S-Adenosylmethionine decarboxylase (Saccharomyces cerevisiae)
1983
Cohn, M.S.; Tabor, C.W.; Tabor, H.
Methods Enzymol.
94
231-234
Comparison of S-adenosylmethionine decarboxylase from rat liver and muscle
1982
Pösö, H.; Pegg, A.E.
Biochemistry
21
3116-3122
Purification and characterization of S-adenosyl-L-methionine decarboxylase from mouse mammary gland and liver
1979
Sakai, T.; Hori, C.; Kano, K.; Oka, T.
Biochemistry
18
5541-5548
S-Adenosylmethionine decarboxylase from baker's yeast
1975
Pösö, H.; Sinervirta, R.; Jänne, J.
Biochem. J.
151
67-73
Comparative properties of rat liver and sea urchin eggs S-adenosyl-L-methionine decarboxylase
1974
Manen, C.A.; Russell, D.H.
Biochemistry
13
4729-4735
Purification and characterization of S-adenosyl-L-methionine decarboxylase from rat liver
1972
Feldman, M.J.; Levy, C.C.; Rusell, D.H.
Biochemistry
11
671-677
Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase
1987
Kameij, T.; Pegg, A.E.
Biochem. J.
243
285-288
Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme
1998
Persson, K.; Aslund, L.; Grahn, B.; Hanke, J.; Heby, O.
Biochem. J.
333
527-537
MGBG analogues as potent inhibitors of S-adenosylmethionine decarboxylase of Onchocerca volvulus
1998
Da'dara, A.A.; Mett, H.; Walter, R.D.
Mol. Biochem. Parasitol.
97
13-19
Purification of S-adenosylmethionine decarboxylase from soybean
1991
Yang, Y.G.; Cho, Y.D.
Biochem. Biophys. Res. Commun.
181
1181-1186
Characterization of S-adenosylmethionine decarboxylase induced by human cytomegalovirus infection
1994
White, E.L.; Arnett, G.; Secrist III, J.A.; Shannon, W.M.
Virus Res.
31
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S-Adenosyl-L-methionine decarboxylase of Acanthamoeba castellanii (Neff): purification and properties
1993
Hugo, E.R.; Byers, T.J.
Biochem. J.
295
203-209
S-Adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus
1991
Cacciapuoti, G.; Porcelli, M.; de Rosa, M.; Gambacorta, A.; Bertoldo, C.; Zappia, V.
Eur. J. Biochem.
199
395-400
-
Inhibition of the methionine cycle enzymes
1987
Miyazaki, J.H.; Yang, S.F.
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