Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5'-methyl,5'-deoxymethylthioadenosine + putrescine
?
putrescine + (methyl-14C)-S-adenosylmethioninamine
spermidine + ?
-
-
-
-
?
putrescine + S-5'-deoxyadenosyl-(5')-3-methylthiopropylamine
spermidine + ?
-
-
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
S-5'-deoxyadenosyl-5'-3-butylthiopropylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-5'-deoxyadenosyl-5'-3-ethylthiopropylamine + 1,4-diaminobutane
?
S-5'-deoxyadenosyl-5'-3-propylthiopropylamine + 1,4-diaminobutane
?
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,3-diaminopropane
?
-
weak substrate
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diamino-2-butene
5'-methylthioadenosine + N-3-aminopropyl-1,4-diamino-2-butene
-
-
in a lower yield than with the natural combination
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diamino-2-butene
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diamino-2-butene
N-3-aminopropyl-1,4-diamino-2-butene + 5'-methylthioadenosine
-
-
forms with a low yield
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,6-diaminohexane
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1-methyl-1,4-butanediamine
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 2,2-difluoro-1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 2-chloro-1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 2-hydroxy-1,4 butanediamine
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 2-methyl-1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + spermidine
5'-methylthioadenosine + spermine
S-adenosyl-(5')-3-methylthiopropylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-3-butylthio-1-propylamine + 1,4-diaminobutane
?
-
prostate enzyme
-
-
?
S-adenosyl-3-carboxymethylthio-1-propylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane
?
S-adenosyl-3-methylthio-1-propylamine + 1,3-diaminopentane
?
-
poor substrate
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane
?
S-adenosyl-3-thiopropylamine sulfone + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-3-thiopropylamine sulfoxide + 1,4-diaminobutane
?
S-adenosyl-5',1-methyl-3-methylthiopropylamine + 1,4-diaminobutane
?
S-adenosyl-L-ethionine + 1,4-diaminobutane
?
S-adenosyl-L-homocysteine sulfone + 1,4-diaminobutane
?
S-adenosyl-L-methionine + 1,4-diaminobutane
?
S-adenosylmethioninamine + putrescine
5'-methylthioadenosine + spermidine
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine
spermidine + 5'-methylthioadenosine
spermidine + S-adenosylmethioninamine
spermine + 5'-methylthioadenosine
in contrast to mammalian spermidine synthases, spermidine can replace to some extent putrescine as the aminopropyl acceptor
-
-
?
additional information
?
-
5'-methyl,5'-deoxymethylthioadenosine + putrescine
?
low activity
-
-
?
5'-methyl,5'-deoxymethylthioadenosine + putrescine
?
low activity
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
ir
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
-
?
putrescine + S-adenosylmethioninamine
spermidine + 5'-methylthioadenosine
-
-
-
?
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-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-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
?
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
the enzyme is highly specific for putrescine as an amine acceptor. When using cadaverine or 1,6-hexanediamine, a diamine with longer chain length, there is no detectable product formation
-
-
?
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
?
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
the enzyme is highly specific for putrescine as an amine acceptor. When using cadaverine or 1,6-hexanediamine, a diamine with longer chain length, there is no detectable product formation
-
-
?
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-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
derivatives of 1,4-diaminobutane are substrates too. Substitution of 1,4-diaminobutane in the immediate vicinity of an amino group produces weak substrates, whereas substituents in the 2-position are tolerated
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
analogues of decarboxylated S-adenosylmethionine act as propylamine donors
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
the reaction is linear from 1 to 10 nmol of spermidine
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
ir
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
+ H+
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
linear at least up to 6 nmol of spermidine formed, linearity not maintained in the absence of DTT
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
the enzyme transfers only the aminopropyl group, not an aminoethyl or aminobutyl groups
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
sulfonium analogs must carry the aminopropyl group to qualify as a substrate
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
analogues of decarboxylated S-adenosylmethionine act as propylamine donors
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
synthetic diamines are substrates too
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
the enzyme transfers only the aminopropyl group, not an aminoethyl or aminobutyl groups
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
sulfonium analogs must carry the aminopropyl group to qualify as a substrate
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
analogues of decarboxylated S-adenosylmethionine act as propylamine donors
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
linear at least up to 6 nmol of spermidine formed, linearity not maintained in the absence of DTT
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,6-diaminohexane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,6-diaminohexane
?
-
1% the reaction rate than with 1,4-diaminobutane
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + 1,6-diaminohexane
?
-
-
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + spermidine
5'-methylthioadenosine + spermine
-
at a reduced rate
-
-
?
S-adenosyl-(5')-3-methylthio-1-propylamine + spermidine
5'-methylthioadenosine + spermine
-
at a reduced rate
the reaction rate is slower than with 1,4-diaminobutane
?
S-adenosyl-(5')-3-methylthio-1-propylamine + spermidine
5'-methylthioadenosine + spermine
-
weak substrate
-
-
?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-3-ethylthio-1-propylamine + 1,4-diaminobutane
?
-
prostate enzyme
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
i.e. S-adenosylmethioninamine or decarboxylated S-adenosylmethionine + putrescine, involved in polyamine biosynthetic pathway
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
6% the reaction rate than with 1,4-diaminobutane
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
aminopropylcadaverine
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
cadaverine
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
20 times less active than 1,4-diaminobutane at the same concentration
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
20 times less active than 1,4-diaminobutane at the same concentration
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane
5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane
-
weak substrate
-
-
?
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-3-propylthio-1-propylamine + 1,4-diaminobutane
?
-
prostate enzyme
-
-
?
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
?
-
brain enzyme
-
-
?
S-adenosyl-5',1-methyl-3-methylthiopropylamine + 1,4-diaminobutane
?
-
prostate enzyme
-
-
?
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
?
-
-
-
-
?
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
-
PAPTs are essential for bacterial cell viability
-
-
?
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
the enzyme is highly specific for putrescine
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
polyamine biosynthetic enzyme
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
functional ACL5 and SPMS are independently involved in apple fruit development and cell growth
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
Val149, Ser161, Ala205, and Val235 are involved in the S-adenosylmethioninamine binding
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
spermidine plays an important role in the activation of the eukaryotic translation initiation factor and cell proliferation
-
-
?
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
the enzyme shows a relatively low substrate specificity for putrescine
-
-
?
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
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
S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
spermidine + 5'-methylthioadenosine
low activity
-
-
?
S-adenosylmethioninamine + putrescine
spermidine + 5'-methylthioadenosine
low activity
-
-
?
additional information
?
-
-
using yeast two-hybrid assays, spermidine synthase2 is identified as a specific 10A06 interactor. 10A06 is a cyst nematode (Heterodera glycines) secretory protein able to infect Arabidopsis thaliana, that is secreted as an effector into the developing syncytia during early plant parasitism
-
-
?
additional information
?
-
amine substrate specificity, overview
-
-
?
additional information
?
-
-
amine substrate specificity, overview
-
-
?
additional information
?
-
amine substrate specificity, overview
-
-
?
additional information
?
-
-
amine substrate specificity, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
additional information
?
-
-
using yeast two-hybrid assays, spermidine synthase2 is identified as a specific 10A06 interactor. 10A06 is a cyst nematode (Heterodera glycines) secretory protein able to infect Arabidopsis thaliana, that is secreted as an effector into the developing syncytia during early plant parasitism
-
-
?
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-(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-(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-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
i.e. S-adenosylmethioninamine or decarboxylated S-adenosylmethionine + putrescine, involved in polyamine biosynthetic pathway
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
?
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
PAPTs are essential for bacterial cell viability
-
-
?
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
-
polyamine biosynthetic enzyme
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
functional ACL5 and SPMS are independently involved in apple fruit development and cell growth
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
spermidine plays an important role in the activation of the eukaryotic translation initiation factor and cell proliferation
-
-
?
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
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
S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,5-Diaminopentane
-
weak, competitive
1,6-diaminohexane
-
23% inhibition
1-Aminooxy-3-aminopropane
1H-benzimidazol-5-yl(4-[(2Z)-3-phenylprop-2-en-1-yl]piperazin-1-yl)methanone
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site and partially competes with binding of methylthioadenosine
2-phenyl-1,2-thiazol-3(2H)-one
-
2-[(6-amino-5,9-dihydro-4H-purin-8-yl)sulfanyl]acetamide
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site and competes with binding of methylthioadenosine
2H-1,4-benzothiazin-3-amine
-
4-methylenecyclohexylamine
-
-
5'-deoxy-5'-methylthioadenosine
5'-deoxy-5'-methylthiotubercidine
5-(1H-benzimidazol-2-yl)pentan-1-amine
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site
5-[(4-methylbenzyl)oxy]quinazolin-2-amine
-
agmatine
-
89% inhibition at 0.1 mM and 61% inhibition at 1 mM
alpha,omega-Diamines
-
with 3 carbon atoms, at 0.25 mM, not at 2.5 mM substrate concentration
arginine
-
98% inhibition at 0.01 mM, 95% inhibition at 0.1 mM and 84% inhibition at 1 mM
benzimidazol-(2-yl)pentan-1-amine
-
bis-cyclohexylammonium sulfate
-
in vitro, 0.2 mM provokes strong decrease in cellular spermidine content, inhibition in cell growth, decrease in DNA synthesis, alterations in cell morphology, disorganization of microfilaments and changes in microtubule network structure, impairs the rate of microtubule reappearance after disruption with colchicine, alterations are prevented with spermidine addition
CGC-11038
-
polyamine analogue
CGC-11098
-
polyamine analogue
CGC-11099
-
polyamine analogue
CGC-11108
-
polyamine analogue
CGC-11114
-
polyamine analogue
CGC-11121
-
polyamine analogue
CGC-11122
-
polyamine analogue
CGC-11144
-
polyamine analogue
CGC-11150
-
polyamine analogue
CGC-11157
-
polyamine analogue
CGC-11158
-
polyamine analogue
CGC-11159
-
polyamine analogue
CGC-11160
-
polyamine analogue
CGC-11172
-
polyamine analogue
CGC-11175
-
polyamine analogue
CGC-11207
-
polyamine analogue
CGC-11211
-
polyamine analogue
CGC-11217
-
polyamine analogue
CGC-11226
-
polyamine analogue
CGC-11227
-
polyamine analogue
CGC-11231
-
polyamine analogue
CGC-11235
-
polyamine analogue
CGC-11237
-
polyamine analogue
CGC-11239
-
polyamine analogue
CGC-11241
-
polyamine analogue
deaminated analogs of decarboxy-S-adenosyl-(5')-3-methylthiopropylamine
-
competitive inhibition with 1,4-diaminobutane and non-competitive with decarboxy-S-adenosyl-(5')-3-methylthiopropylamine
decarboxylated S-adenosylhomocysteine
Dicyclohexylamine
poor inhibition
DTNB
-
potent inhibition, activity is restored to more than 95% with 0.1 mM DTT
exo-2-aminonorbornane
-
potent and selective, 98% inhibition at 0.1 mM in the presence of 1 mM of putrescine
Homospermidine
-
95% inhibition at 0.01 mM, 92% inhibition at 0.1 mM and 30% inhibition at 1 mM
methyl (2E)-2-(4-hydroxy-3-methoxybenzylidene)hydrazinecarbimidothioate
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site and partially competes with binding of methylthioadenosine
N,N'-Bis-(2-aminoethyl)propane-1,3-diamine
-
strong, 52% inhibition
N-methyl-6-(piperidin-1-yl)hexan-1-amine
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site
N-methyl-N-phenyl-2,3-dihydro-1,4-benzodioxine-2-carboxamide
-
N-[2-(phenylsulfanyl)ethyl]-1H-benzotriazole-5-carboxamide
-
identified by a five-step structure-based virtual screening procedure as a binder to spermidine synthase active site. Binds reversibly to the active site and partially competes with binding of methylthioadenosine
quinolin-8-yl piperidine-1-carboxylate
-
S-5'-Deoxyadenosyl(5')-2-ethylthioethylamine
-
uncompetitive with S-adenosyl-3-methylthio-1-propylamine at high concentrations but competitive with S-5'-deoxyadenosyl-5'-3-ethylthiopropylamine
S-5'-Deoxyadenosyl(5')-2-methylthioethylamine
S-5'-Deoxyadenosyl(5')-2-thioethylamine
-
weak
S-5'-Deoxyadenosyl(5')-3-butylthiopropylamine
-
weak
S-5'-deoxyadenosyl(5')-3-thiopropylamine
-
weak
S-5'-Deoxyadenosyl(5')-4-methylthiobutylamine
-
weak
S-5'-Deoxyadenosyl(5')-4-thiobutylamine
-
uncompetitive with S-Adenosyl-3-methylthio-1-propylamine
S-Adenosyl(5')-2-methylthioethylamine
-
-
S-Adenosyl(5')-3-methylthiopropanol
-
kinetics
S-adenosyl-(5')-3-methylthio-1-propylamine
S-Adenosyl-1,8-diamino-3-methylthiooctane
-
less efficient than the thioether
S-adenosyl-1,8-diamino-3-thio-octane
S-Adenosyl-1,8-diamino-3-thiooctane
S-Adenosyl-3-thiopropylamine sulfone
-
-
S-Adenosyl-4-methylthiobutyric acid
-
-
S-adenosyl-L-ethionine
-
-
S-Adenosyl-L-homocysteine sulfone
-
-
S-Inosyl(5')-3-methylthiopropylamine
-
not S-inosyl(5')-3-methylthiopropanol
S-Tubercidinylmethionine
-
-
spermine
-
99% inhibition at 0.1 mM and 90% inhibition at 1 mM
Substrate and product analogues
-
overview
-
sulfhydryl reagents
-
W strain
Sulfoxide and sulfone derivatives of decarboxylated S-adenosyl-L-homocysteine
-
-
-
trans-4-ethyl-cyclohexylamine
-
-
trans-4-hydroxycyclohexylamine
-
-
trans-4-Methylcyclohexylamine
triethylenetetramine
-
39% inhibition
1,3-diaminopropane
-
34% inhibition
1,3-diaminopropane
-
96% inhibition at 0.01 mM and 100% inhibition at 0.1 mM
1-Aminooxy-3-aminopropane
-
brain enzyme, specific, no inhibition of spermine synthase, reversible, competitive with 1,4-diaminobutane
1-Aminooxy-3-aminopropane
poor inhibition
2-mercaptoethylamine
poor inhibition
2-mercaptoethylamine
-
competitive with 1,4-diaminobutane, reversible, its removal restores the enzyme activity, the amino group is necessary to inhibit the enzyme
4-methylcyclohexylamine
-
-
4-methylcyclohexylamine
-
-
5'-deoxy-5'-methylthioadenosine
-
weak
5'-deoxy-5'-methylthioadenosine
-
above 0.05 mM
5'-deoxy-5'-methylthiotubercidine
-
weak
5'-deoxy-5'-methylthiotubercidine
-
-
5'-ethylthioadenosine
-
-
5'-ethylthioadenosine
-
-
5'-ethylthioadenosine
-
strong
5'-ethylthioadenosine
-
-
5'-methylthioadenosine
-
-
5'-methylthioadenosine
-
non-competitive, mixed type inhibition
5'-methylthioadenosine
-
weak inhibition
5'-methylthioadenosine
-
W strain
5'-methylthioadenosine
-
-
5'-methylthioadenosine
feedback inhibition
5'-methylthioadenosine
-
-
5'-methylthioadenosine
-
strong
5'-methylthioadenosine
-
-
5'-methylthioadenosine
-
weak inhibition
5'-methylthioadenosine
-
83% inhibition at 0.01 mM and 22% inhibition at 1 mM
5'-methylthiotubercidin
-
in vivo and in vitro, strong
5'-methylthiotubercidin
-
-
5-amino-1-pentene
50% inhibition at 6.5 microM
cadaverine
-
26-39% inhibition
cadaverine
-
77% inhibition at 0.01 mM and 22% inhibition at 1 mM
Cyclohexylamine
competitive inhibitor. The inhibitor occupies the polyamine binding site of the enzyme where it binds at the bottom of the active site with the amine group placed analogously to the substrate; competitive inhibitor. The inhibitor occupies the polyamine binding site of the enzyme where it is binds at the bottom of the active site with the amine group placed analogously to the substrate
Cyclohexylamine
-
IC50 2.4 +/- 0.7 microM
Cyclohexylamine
-
potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
50% inhibition at 19.7 microM
Cyclohexylamine
-
potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
-
potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
-
50% inhibition at 0.0081 mM, competitive with 1,4-diaminobutane
Cyclohexylamine
-
in vitro, 50% inhibition at 0.015 mM, competitive with 1,4-diaminobutane
decarboxylated S-adenosylhomocysteine
active site binding structure, overview
decarboxylated S-adenosylhomocysteine
-
-
decarboxylated S-adenosylhomocysteine
-
-
n-butylamine
-
specific inhibitor of the enzyme in vivo and in vitro
N-ethylmaleimide
-
-
N-ethylmaleimide
-
potent inhibition
p-hydroxymercuribenzoate
-
2-mercaptoethanol restores activity
p-hydroxymercuribenzoate
-
-
S-5'-Deoxyadenosyl(5')-2-methylthioethylamine
-
prostate
S-5'-Deoxyadenosyl(5')-2-methylthioethylamine
-
the most potent inhibitor, competitive with decarboxylated S-adenosylmethionine and S-5'-deoxyadenosyl-(5')-3-ethylthiopropylamine
S-adenosyl-(5')-3-methylthio-1-propylamine
-
at concentrations above 0.05 mM
S-adenosyl-(5')-3-methylthio-1-propylamine
-
competitive substrate inhibition
S-adenosyl-(5')-3-methylthio-1-propylamine
-
complete inhibition at 0.080 mM
S-adenosyl-1,8-diamino-3-thio-octane
-
S-adenosyl-1,8-diamino-3-thio-octane
-
S-Adenosyl-1,8-diamino-3-thiooctane
-
transition-state analogue, potent inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
competitive with 1,4-diaminobutane, potent inhibition, stronger than dicyclohexylamine in vitro, but not in vivo, at concentrations of S-adenosyl-3-methylthio-1-propylamine and 1,4-diaminobutane higher than those normally present in vivo. At concentration of substrates that approximate in vivo conditions, more than 20fold stronger inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
competitive with 1,4-diaminobutane, potent inhibition, stronger than dicyclohexylamine in vitro, but not in vivo, at concentrations of S-adenosyl-3-methylthio-1-propylamine and 1,4-diaminobutane higher than those normally present in vivo. At concentration of substrates that approximate in vivo conditions, more than 20fold stronger inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
prostate
S-Adenosyl-1,8-diamino-3-thiooctane
-
specific and more potent inhibitor than the corresponding fully-charged methyl sulfonium salt; transition-state analogue, potent inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
competitive with 1,4-diaminobutane, potent inhibition, stronger than dicyclohexylamine in vitro, but not in vivo, at concentrations of S-adenosyl-3-methylthio-1-propylamine and 1,4-diaminobutane higher than those normally present in vivo. At concentration of substrates that approximate in vivo conditions, more than 20fold stronger inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
competitive with 1,4-diaminobutane, potent inhibition, stronger than dicyclohexylamine in vitro, but not in vivo, at concentrations of S-adenosyl-3-methylthio-1-propylamine and 1,4-diaminobutane higher than those normally present in vivo. At concentration of substrates that approximate in vivo conditions, more than 20fold stronger inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
-
50% inhibition at 0.0025 mM
S-Adenosyl-1,8-diamino-3-thiooctane
-
IC50 of 0.0002 mM
S-Adenosyl-1,8-diamino-3-thiooctane
-
S-Adenosyl-1,8-diamino-3-thiooctane
-
potent, 50% inhibition at 0.025 mM
S-adenosyl-L-methionine
-
above 0.01 mM
S-adenosyl-L-methionine
-
-
spermidine
-
not competitive, mixed type inhibition
spermidine
-
product inhibition at physiological concentrations
trans-4-Methylcyclohexylamine
-
IC50 7.2 microM
trans-4-Methylcyclohexylamine
IC50 1.4 microM
trans-4-Methylcyclohexylamine
-
i.e. 4MCHA, binding structure
trans-4-Methylcyclohexylamine
-
potent and selective, 98% inhibition at 0.1 mM in the presence of 1 mM of putrescine, in vitro. In vivo, intraperitoneal administration causes effective decrease in spermidine content in prostate, and oral administration causes 28%, 21% and 33% decrease in spermidine content in prostate, liver and kidney, respectively
trans-4-Methylcyclohexylamine
-
-
trans-4-Methylcyclohexylamine
-
in vitro and in vivo inhibition, reduces the spermidine and spermine content in rat tissue after oral application, quantification, overview
trans-4-Methylcyclohexylamine
-
potent, 50% inhibition at 0.0017 mM, competitive with 1,4-diaminobutane
trans-4-Methylcyclohexylamine
-
trans-4-Methylcyclohexylamine
evaluation of an inhibitor activity on spermidine synthase by an NMR biochemical assay for fragment-based drug discovery
additional information
-
inhibition by end products of reaction; no inhibition by phenylhydrazine, semicarbazide, sodium borohydride, NaCN, KCl, NH4Cl, MgCl2, CaCl2, NaNO3, Na2SO4, Na2HPO4
-
additional information
-
inhibition by end products of reaction; no inhibition by carbonyl binding reagents
-
additional information
-
no inhibition by 1,4-diaminobutane
-
additional information
-
no inhibition by 1,4-diaminobutane
-
additional information
-
inhibitory potency of diverse polyamine analogues on the polyamine biosynthesis in wild-type strain and strains overexpressing polyamine biosynthetic enzymes, EC50 values, overview
-
additional information
not inhibitory: S-adenosylmethioninamine concentrations up to 150 microM
-
additional information
-
not inhibitory: S-adenosylmethioninamine concentrations up to 150 microM
-
additional information
-
polyamines
-
additional information
-
S-adenosyl-L-homocysteine
-
additional information
-
no inhibition by 2-mercaptoethanol at 0.1 to 1 mM
-
additional information
-
no inhibition by putrescine up to 10 mM
-
additional information
-
not inhibitory: 4,4-dimethylcyclohexylamine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Yamanoha, B.; Cohen, S.S.
S-Adenosylmethionine decarboxylase and spermidine synthase from Chineses cabbage
Plant Physiol.
78
784-790
1985
Brassica rapa subsp. pekinensis
brenda
Tabor, H.; Tabor, C.W.
Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines
Adv. Enzymol. Relat. Areas Mol. Biol.
36
203-268
1972
Saccharomyces cerevisiae, Escherichia coli, Neurospora crassa, Rattus norvegicus
brenda
Pegg, A.E.; Shuttleworth, K.; Hibasami, H.
Specificity of mammalian spermidine synthase and spermine synthase
Biochem. J.
197
315-320
1981
Rattus norvegicus
brenda
Hannonen, P.; Jnne, J.; Raina, A.
Partial purification and characterization of spermine synthase from rat brain
Biochim. Biophys. Acta
289
225-231
1972
Rattus norvegicus
brenda
Coward, J.K.; Anderson, G.L.; Tang, K.C.
Aminopropyltransferase substrates and inhibitors
Methods Enzymol.
94
286-294
1983
Rattus norvegicus
-
brenda
Pegg, A.E.
Inhibition of aminopropyltransferases
Methods Enzymol.
94
294-297
1983
Rattus norvegicus
brenda
Kajander, E.O.; Kauppinen, L.I.; Pajula, R.L.; Karkola, K.; Eloranta, T.O.
Purification and partial characterization of human polyamine synthases
Biochem. J.
259
879-886
1989
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Hibasami, H.; Borchardt, R.T.; Chen, S.Y.; Coward, J.K.; Pegg, A.E.
Studies of inhibition of rat spermidine synthase and spermine synthase
Biochem. J.
187
419-428
1980
Rattus norvegicus, Rattus norvegicus Sprague Dawley
brenda
Sindhu, R.K.; Cohen, S.S.
Propylaminetransferases in chinese cabbage leaves
Plant Physiol.
74
645-649
1984
Brassica rapa subsp. pekinensis, Spinacia oleracea
brenda
Raina, A.; Pajula, R.L.; Eloranta, T.
A rapid assay method for spermidine and spermine synthases. Distribution of polyamine-synthesizing enzymes and methionine adenosyltransferase in rat tissues
FEBS Lett.
67
252-255
1976
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Shirahata, A.; Takahashi, N.; Beppu, T.; Hosoda, H.; Samejima, K.
Effects of inhibitors of spermidine synthase and spermine synthase on polyamine synthesis in rat tissues
Biochem. Pharmacol.
45
1897-1903
1993
Rattus norvegicus
brenda
Lee, S.H.; Cho, Y.D.
A new assay method for spermidine and spermine synthases using antibody against MTA
J. Biochem. Mol. Biol.
30
443-447
1997
Glycine max, Rattus norvegicus
-
brenda
Shirahata, A.; Morohoshi, T.; Samejima, K.
trans-4-Methylcyclohexylamine, a potent new inhibitor of spermidine synthase
Chem. Pharm. Bull.
36
3220-3222
1988
Sus scrofa
brenda
Bitonti, A.J.; Kelly, S.E.; McCann, P.P.
Characterization of spermidine synthase from Trypanosoma brucei brucei
Mol. Biochem. Parasitol.
13
21-28
1984
Trypanosoma brucei brucei
brenda
Sarhan, S.; Dezeure, F.; Seiler, N.
Putrescine derivatives as substrates of spermidine synthase
Int. J. Biochem.
19
1037-1047
1987
Bos taurus, Rattus norvegicus
brenda
Raina, A.; Hyvnen, T.; Eloranta, T.; Voutilainen, M.; Samejima, K.; Yamanoha, B.
Polyamine synthesis in mammalian tissues. Isolation and characterization of spermidine synthase from bovine brain
Biochem. J.
219
991-1000
1984
Bos taurus
brenda
Khomutov, R.M.; Hyvnen, T.; Karvonen, E.; Kauppinen, L.; Paalanen, T.; Paulin, L.; Eloranta, T.; Pajula, R.L.; Andersson, L.C.; Ps, H.
1-Aminooxy-3-aminopropane, a new and potent inhibitor of polyamine biosynthesis that inhibits ornithine decarboxylase, adenosylmethionine decarboxylase and spermidine synthase
Biochem. Biophys. Res. Commun.
130
596-602
1985
Bos taurus
brenda
Tang, K.C.; Pegg, A.E.; Coward, J.K.
Specific and potent inhibition of spermidine synthase by the transition-state analog, S-adenosyl-3-thio-1,8-diaminooctane
Biochem. Biophys. Res. Commun.
96
1371-1377
1980
Rattus norvegicus
brenda
Samejima, K.; Nakazawa, Y.
Action of decarboxylated S-adenosylmethionine analogs in the spermidine-synthesizing system from rat prostate
Arch. Biochem. Biophys.
201
241-246
1980
Rattus norvegicus, Rattus norvegicus Sprague Dawley
brenda
Hibasami, H.; Kawase, M.; Tsukada, T.; Maekawa, S.; Sakurai, M.; Nakashima, K.
2-Mercaptoethylamine, a competitive inhibitor of spermidine synthase in mammalian cells
FEBS Lett.
229
243-246
1988
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Pegg, A.E.; Bitonti, A.J.; McCann, P.P.; Coward, J.K.
Inhibition of bacterial aminopropyltransferases by S-adenosyl-1,8-diamino-3-thiooctane and by dicyclohexylamine
FEBS Lett.
155
192-196
1983
Escherichia coli, Pseudomonas aeruginosa, Rattus norvegicus, Serratia marcescens
brenda
Sindhu, R.K.; Cohen, S.S.
Putrescine aminopropyltransferase (spermidine synthase) of Chinese Cabbage
Methods Enzymol.
94
279-285
1983
Brassica rapa subsp. pekinensis, Escherichia coli
-
brenda
Samejima, K.; Raina, A.; Yamanoha, B.; Eloranta, T.
Purification of putrescine aminopropyltransferase (spermidine synthase) from eukaryotic tissues
Methods Enzymol.
94
270-276
1983
Bos taurus, Rattus norvegicus
brenda
Bowman, W.H.; White Tabor, C.; Tabor, H.
Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli
J. Biol. Chem.
248
2480-2486
1973
Escherichia coli
brenda
White Tabor, C.; Tabor, H.
Putrescine aminopropyltransferase (Escherichia coli)
Methods Enzymol.
94
265-270
1983
Escherichia coli
brenda
Zappia, V.; Cacciapuoti, G.; Pontoni, G.; Oliva, A.
Mechanism of propylamine-transfer reactions. Kinetic and inhibition studies on spermidine synthase from Escherichia coli
J. Biol. Chem.
255
7276-7280
1980
Escherichia coli
brenda
Samejima, K.; Yamanoha, B.
Purification of spermidine synthase from rat ventral prostate by affinity chromatography on immobilized S-adenosyl(5)-3-thiopropylamine
Arch. Biochem. Biophys.
216
213-222
1982
Escherichia coli, Rattus norvegicus, Rattus norvegicus Wistar
brenda
Graser, G.; Hartmann T.
Biosynthesis of spermidine, a direct precursor of pyrrolizidine alkaloids in root cultures of Senecio vulgaris L.
Planta
211
239-245
2000
Senecio vulgaris
brenda
Panicot, M.; Minguet, E.G.; Ferrando, A.; Alczar, R.; Blzquez, M.A.; Carbonell, J.; Altabella, T.; Koncz, C.; Tiburcio, A.F.
A polyamine metabolon involving aminopropyl transferase complexes in Arabidopsis
Plant Cell
14
2539-2551
2002
Arabidopsis thaliana
brenda
Hashimoto T.; Tamaki, K.; Suzuki, K.; Yamada, Y.
Molecular cloning of plant spermidine synthases
Plant Cell Physiol.
39
73-79
1998
Arabidopsis thaliana, Hyoscyamus niger, Nicotiana sylvestris
brenda
Yoon, S.O.; Lee, Y.S.; Lee, S.H.; Cho, Y.D.
Polyamine synthesis in plants: isolation and characterization of spermidine synthase from soybean (Glycine max) axes
Biochim. Biophys. Acta
1475
17-26
2000
Glycine max
brenda
Friesen, H.; Tanny, J.C.; Segall, J.
SPE3, which encodes spermidine synthase, is required for full repression through NREDIT in Saccharomyces cerevisiae
Genetics
150
59-73
1998
Saccharomyces cerevisiae
brenda
Caruso, A.; Pellati, A.; Bosi, G.; Arena, N.; Stabellini, G.
Effects of spermidine synthase inhibition on cytoskeletal organization in cultured chick embryo fibroblasts
Eur. J. Histochem.
38
245-252
1994
Gallus gallus
brenda
Korolev, S.; Ikeguchi, Y.; Skarina T.; Beasley, S.; Arrowsmith, C.; Edwards, A.; Joachimiak, A.; Pegg, A.E.; Savchenko, A.
The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor
Nat. Struct. Biol.
9
27-31
2002
Thermotoga maritima
brenda
Lu, P.K.; Chien, S.Y.; Tsai, J.Y.; Fong, C.T.; Lee, M.J.; Huang, H.; Sun, Y.J.
Crystallization and preliminary X-ray diffraction analysis of spermidine synthase from Helicobacter pylori
Acta Crystallogr. Sect. D
60
2067-2069
2004
Helicobacter pylori
brenda
Dejima, H.; Kobayashi, M.; Takasaki, H.; Takeda, N.; Shirahata, A.; Samejima, K.
Synthetic decarboxylated S-adenosyl-L-methionine as a substrate for aminopropyl transferases
Biol. Pharm. Bull.
26
1005-1008
2003
Rattus norvegicus
brenda
Goda, H.; Watanabe, T.; Takeda, N.; Kobayashi, M.; Wada, M.; Hosoda, H.; Shirahata, A.; Samejima, K.
Mammalian spermidine synthase--identification of cysteine residues and investigation of the putrescine binding site
Biol. Pharm. Bull.
27
1327-1332
2004
Rattus norvegicus
brenda
Dufe, V.T.; Luersen, K.; Eschbach, M.L.; Haider, N.; Karlberg, T.; Walter, R.D.; Al-Karadaghi, S.
Cloning, expression, characterisation and three-dimensional structure determination of Caenorhabditis elegans spermidine synthase
FEBS Lett.
579
6037-6043
2005
Caenorhabditis elegans, Caenorhabditis elegans Bristol N2
brenda
Franceschetti, M.; Fornale, S.; Tassonia, A.; Zuccherelli, K.; Mayer, M.J.; Bagni, N.
Effects of spermidine synthase overexpression on polyamine biosynthetic pathway in tobacco plants
J. Plant Physiol.
161
989-1001
2004
Datura stramonium
brenda
Haider, N.; Eschbach, M.L.; Dias Sde, S.; Gilberger, T.W.; Walter, R.D.; Luersen, K.
The spermidine synthase of the malaria parasite Plasmodium falciparum: molecular and biochemical characterisation of the polyamine synthesis enzyme
Mol. Biochem. Parasitol.
142
224-236
2005
Plasmodium falciparum (Q9NFS5), Plasmodium falciparum
brenda
Kasukabe, Y.; He, L.; Nada, K.; Misawa, S.; Ihara, I.; Tachibana, S.
Overexpression of spermidine synthase enhances tolerance to multiple environmental stresses and up-regulates the expression of various stress-regulated genes in transgenic Arabidopsis thaliana
Plant Cell Physiol.
45
712-722
2004
Cucurbita ficifolia
brenda
Lee, M.J.; Huang, C.Y.; Sun, Y.J.; Huang, H.
Cloning and characterization of spermidine synthase and its implication in polyamine biosynthesis in Helicobacter pylori strain 26695
Protein Expr. Purif.
43
140-148
2005
Helicobacter pylori (O25503), Helicobacter pylori
brenda
Enomoto, K.; Nagasaki, T.; Yamauchi, A.; Onoda, J.; Sakai, K.; Yoshida, T.; Maekawa, K.; Kinoshita, Y.; Nishino, I.; Kikuoka, S.; Fukunaga, T.; Kawamoto, K.; Numata, Y.; Takemoto, H.; Nagata, K.
Development of high-throughput spermidine synthase activity assay using homogeneous time-resolved fluorescence
Anal. Biochem.
351
229-240
2006
Homo sapiens
brenda
Roberts, S.C.; Jiang, Y.; Gasteier, J.; Frydman, B.; Marton, L.J.; Heby, O.; Ullman, B.
Leishmania donovani polyamine biosynthetic enzyme overproducers as tools to investigate the mode of action of cytotoxic polyamine analogs
Antimicrob. Agents Chemother.
51
438-445
2007
Leishmania donovani
brenda
Wu, H.; Min, J.; Ikeguchi, Y.; Zeng, H.; Dong, A.; Loppnau, P.; Pegg, A.E.; Plotnikov, A.N.
Structure and mechanism of spermidine synthases
Biochemistry
46
8331-8339
2007
Homo sapiens (P19623), Homo sapiens, Thermotoga maritima (Q9WZC2), Thermotoga maritima
brenda
Kobayashi, M.; Watanabe, T.; Xu, Y.J.; Tatemori, M.; Goda, H.; Niitsu, M.; Shirahata, A.; Samejima, K.
Control of spermidine and spermine levels in rat tissues by trans-4-methylcyclohexylamine, a spermidine-synthase inhibitor
Biol. Pharm. Bull.
28
569-573
2005
Rattus norvegicus
brenda
Burger, P.B.; Birkholtz, L.M.; Joubert, F.; Haider, N.; Walter, R.D.; Louw, A.I.
Structural and mechanistic insights into the action of Plasmodium falciparum spermidine synthase
Bioorg. Med. Chem.
15
1628-1637
2007
Plasmodium falciparum
brenda
Kitashiba, H.; Hao, Y.J.; Honda, C.; Moriguchi, T.
Two types of spermine synthase gene: MdACL5 and MdSPMS are differentially involved in apple fruit development and cell growth
Gene
361
101-111
2005
Malus sylvestris (Q4ADY3), Malus sylvestris (Q4ADY4), Malus sylvestris (Q4ADY5)
brenda
Sano, M.; Nishino, I.
Assay for spermidine synthase activity by micellar electrokinetic chromatography with laser-induced fluorescence detection
J. Chromatogr. B
845
80-83
2007
Rattus norvegicus
brenda
Krauss, M.; Langnaese, K.; Richter, K.; Brunk, I.; Wieske, M.; Ahnert-Hilger, G.; Veh, R.W.; Laube, G.
Spermidine synthase is prominently expressed in the striatal patch compartment and in putative interneurones of the matrix compartment
J. Neurochem.
97
174-189
2006
Mus musculus, Rattus norvegicus
brenda
Kasukabe, Y.; He, L.; Watakabe, Y.; Otani, M.; Shimada, T.; Tachibana, S.
Improvement of environmental stress tolerance of sweet potato by introduction of genes for spermidine synthase
Plant Biotechnol.
23
75-83
2006
Cucurbita ficifolia
-
brenda
Lu, P.K.; Tsai, J.Y.; Chien, H.Y.; Huang, H.; Chu, C.H.; Sun, Y.J.
Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-like fold with a distinct active site
Proteins
67
743-754
2007
Helicobacter pylori
brenda
Taylor, M.C.; Kaur, H.; Blessington, B.; Kelly, J.M.; Wilkinson, S.R.
Validation of spermidine synthase as a drug target in African trypanosomes
Biochem. J.
409
563-569
2008
Trypanosoma brucei (Q38EH6), Trypanosoma brucei
brenda
Jacobsson, M.; Gaeredal, M.; Schultz, J.; Karlen, A.
Identification of Plasmodium falciparum spermidine synthase active site binders through structure-based virtual screening
J. Med. Chem.
51
2777-2786
2008
Plasmodium falciparum
brenda
Dufe, V.T.; Qiu, W.; Mueller, I.B.; Hui, R.; Walter, R.D.; Al-Karadaghi, S.
Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO
J. Mol. Biol.
373
167-177
2007
Plasmodium falciparum
brenda
Krauss, M.; Weiss, T.; Langnaese, K.; Richter, K.; Kowski, A.; Veh, R.W.; Laube, G.
Cellular and subcellular rat brain spermidine synthase expression patterns suggest region-specific roles for polyamines, including cerebellar pre-synaptic function
J. Neurochem.
103
679-693
2007
Rattus norvegicus
brenda
He, L.; Ban, Y.; Inoue, H.; Matsuda, N.; Liu, J.; Moriguchi, T.
Enhancement of spermidine content and antioxidant capacity in transgenic pear shoots overexpressing apple spermidine synthase in response to salinity and hyperosmosis
Phytochemistry
69
2133-2141
2008
Malus domestica
brenda
Efrose, R.C.; Flemetakis, E.; Sfichi, L.; Stedel, C.; Kouri, E.D.; Udvardi, M.K.; Kotzabasis, K.; Katinakis, P.
Characterization of spermidine and spermine synthases in Lotus japonicus: induction and spatial organization of polyamine biosynthesis in nitrogen fixing nodules
Planta
228
37-49
2008
Lotus japonicus (A2VC28), Lotus japonicus
brenda
Wen, X.P.; Pang, X.M.; Matsuda, N.; Kita, M.; Inoue, H.; Hao, Y.J.; Honda, C.; Moriguchi, T.
Over-expression of the apple spermidine synthase gene in pear confers multiple abiotic stress tolerance by altering polyamine titers
Transgenic Res.
17
251-263
2008
Malus domestica
brenda
Wu, X.B.; Wang, J.; Liu, J.H.; Deng, X.X.
Involvement of polyamine biosynthesis in somatic embryogenesis of Valencia sweet orange (Citrus sinensis) induced by glycerol
J. Plant Physiol.
166
52-62
2009
Citrus sinensis
brenda
Kim, J.H.; Kim, H.S.; Lee, Y.H.; Kim, Y.S.; Oh, H.W.; Joung, H.; Chae, S.K.; Suh, K.H.; Jeon, J.H.
Polyamine biosynthesis regulated by StARD expression plays an important role in potato wound periderm formation
Plant Cell Physiol.
49
1627-1632
2008
Solanum tuberosum
brenda
Wen, X.; Ban, Y.; Inoue, H.; Matsuda, N.; Moriguchi, T.
Aluminum tolerance in a spermidine synthase-overexpressing transgenic European pear is correlated with the enhanced level of spermidine via alleviating oxidative status
Environ. Exp. Bot.
66
471-478
2009
Malus domestica
-
brenda
Valdes-Santiago, L.; Cervantes-Chavez, J.A.; Ruiz-Herrera, J.
Ustilago maydis spermidine synthase is encoded by a chimeric gene, required for morphogenesis, and indispensable for survival in the host
FEMS Yeast Res.
9
923-935
2009
Ustilago maydis
brenda
Zhou, X.; Chua, T.K.; Tkaczuk, K.L.; Bujnicki, J.M.; Sivaraman, J.
The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket
J. Struct. Biol.
169
277-285
2010
Escherichia coli
brenda
Parvin, S.; Kim, Y.; Pulla, R.; Sathiyamoorthy, S.; Miah, M.; Kim, Y.; Wasnik, N.; Yang, D.
Identification and characterization of spermidine synthase gene from Panax ginseng
Mol. Biol. Rep.
37
923-932
2009
Panax ginseng (C7DZJ5), Panax ginseng
brenda
Hewezi, T.; Howe, P.J.; Maier, T.R.; Hussey, R.S.; Mitchum, M.G.; Davis, E.L.; Baum, T.J.
Arabidopsis spermidine synthase is targeted by an effector protein of the cyst nematode Heterodera schachtii
Plant Physiol.
152
968-984
2010
Arabidopsis thaliana
brenda
Wen, X.P.; Ban, Y.; Inoue, H.; Matsuda, N.; Moriguchi, T.
Spermidine levels are implicated in heavy metal tolerance in a spermidine synthase overexpressing transgenic European pear by exerting antioxidant activities
Transgenic Res.
19
91-103
2010
Malus domestica
brenda
Chattopadhyay, M.K.; Chen, W.; Poy, G.; Cam, M.; Stiles, D.; Tabor, H.
Microarray studies on the genes responsive to the addition of spermidine or spermine to a Saccharomyces cerevisiae spermidine synthase mutant
Yeast
26
531-544
2009
Saccharomyces cerevisiae
brenda
Gomez-Jimenez, M.C.; Paredes, M.A.; Gallardo, M.; Fernandez-Garcia, N.; Olmos, E.; Sanchez-Calle, I.M.
Tissue-specific expression of olive S-adenosyl methionine decarboxylase and spermidine synthase genes and polyamine metabolism during flower opening and early fruit development
Planta
232
629-647
2010
Olea europaea (D2K8S6)
brenda
Shi, C.; Welsh, P.A.; Sass-Kuhn, S.; Wang, X.; McCloskey, D.E.; Pegg, A.E.; Feith, D.J.
Characterization of transgenic mice with overexpression of spermidine synthase
Amino Acids
42
495-505
2012
Homo sapiens
brenda
Grover, A.; Katiyar, S.P.; Singh, S.K.; Dubey, V.K.; Sundar, D.
A leishmaniasis study: structure-based screening and molecular dynamics mechanistic analysis for discovering potent inhibitors of spermidine synthase
Biochim. Biophys. Acta
1824
1476-1483
2012
Leishmania donovani (Q9GSR3), Leishmania donovani
brenda
Gilroy, C.; Olenyik, T.; Roberts, S.C.; Ullman, B.
Spermidine synthase is required for virulence of Leishmania donovani
Infect. Immun.
79
2764-2769
2011
Leishmania donovani, Leishmania donovani LdBob
brenda
Neily, M.H.; Matsukura, C.; Maucourt, M.; Bernillon, S.; Deborde, C.; Moing, A.; Yin, Y.G.; Saito, T.; Mori, K.; Asamizu, E.; Rolin, D.; Moriguchi, T.; Ezura, H.
Enhanced polyamine accumulation alters carotenoid metabolism at the transcriptional level in tomato fruit over-expressing spermidine synthase
J. Plant Physiol.
168
242-252
2011
Malus domestica (Q8GTQ6)
brenda
Lee, M.J.; Yang, Y.T.; Lin, V.; Huang, H.
Site-directed mutations of the gatekeeping loop region affect the activity of Escherichia coli spermidine synthase
Mol. Biotechnol.
54
572-580
2013
Escherichia coli (P09158), Escherichia coli
brenda
Sichhart, Y.; Draeger, B.
Immunolocalisation of spermidine synthase in Solanum tuberosum
Phytochemistry
91
117-121
2013
Solanum tuberosum (Q93X16), Solanum tuberosum, Solanum tuberosum Desiree (Q93X16)
brenda
Neily, M.; Baldet, P.; Arfaoui, I.; Saito, T.; Qiu-li, L.; Asamizu, E.; Matsukura, C.; Moriguchi, T.; Ezura, H.
Overexpression of apple spermidine synthase 1 (MdSPDS1) leads to significant salt tolerance in tomato plants
Plant Biotechnol.
28
33-42
2011
Malus domestica (Q8GTQ6)
-
brenda
Nambeesan, S.; Datsenka, T.; Ferruzzi, M.G.; Malladi, A.; Mattoo, A.K.; Handa, A.K.
Overexpression of yeast spermidine synthase impacts ripening, senescence and decay symptoms in tomato
Plant J.
63
836-847
2010
Saccharomyces cerevisiae
brenda
Seckute, J.; McCloskey, D.E.; Thomas, H.J.; Secrist, J.A.; Pegg, A.E.; Ealick, S.E.
Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine
Protein Sci.
20
1836-1844
2011
Plasmodium falciparum, Thermotoga maritima, Homo sapiens (P19623), Homo sapiens
brenda
Amano, Y.; Namatame, I.; Tateishi, Y.; Honboh, K.; Tanabe, E.; Niimi, T.; Sakashita, H.
Structural insights into the novel inhibition mechanism of Trypanosoma cruzi spermidine synthase
Acta Crystallogr. Sect. D
71
1879-1889
2015
Trypanosoma cruzi (Q4DA73), Trypanosoma cruzi
brenda
Sprenger, J.; Svensson, B.; Halander, J.; Carey, J.; Persson, L.; Al-Karadaghi, S.
Three-dimensional structures of Plasmodium falciparum spermidine synthase with bound inhibitors suggest new strategies for drug design
Acta Crystallogr. Sect. D
71
484-493
2015
Plasmodium falciparum (Q8II73), Plasmodium falciparum
brenda
Mishra, A.K.; Agnihotri, P.; Srivastava, V.K.; Pratap, J.V.
Novel protein-protein interaction between spermidine synthase and S-adenosylmethionine decarboxylase from Leishmania donovani
Biochem. Biophys. Res. Commun.
456
637-642
2015
Leishmania donovani (A4HS53), Leishmania donovani
brenda
Imamura, T.; Fujita, K.; Tasaki, K.; Higuchi, A.; Takahashi, H.
Characterization of spermidine synthase and spermine synthase - The polyamine-synthetic enzymes that induce early flowering in Gentiana triflora
Biochem. Biophys. Res. Commun.
463
781-786
2015
Gentiana triflora (A0A0K2S254), Gentiana triflora
brenda
Das, M.; Singh, S.; Dubey, V.K.
Novel inhibitors of ornithine decarboxylase of Leishmania parasite (LdODC): the parasite resists LdODC inhibition by overexpression of spermidine synthase
Chem. Biol. Drug Des.
87
352-360
2016
Leishmania donovani (A4HS53), Leishmania donovani
brenda
Guedez, G.; Pothipongsa, A.; Siren, S.; Liljeblad, A.; Jantaro, S.; Incharoensakdi, A.; Salminen, T.A.
Crystal structure of dimeric Synechococcus spermidine synthase with bound polyamine substrate and product
Biochem. J.
476
1009-1020
2019
Synechococcus elongatus (Q31QK9), Synechococcus elongatus PCC 7942 (Q31QK9)
brenda
Frohnhoefer, H.G.; Geiger-Rudolph, S.; Pattky, M.; Meixner, M.; Huhn, C.; Maischein, H.M.; Geisler, R.; Gehring, I.; Maderspacher, F.; Nuesslein-Volhard, C.; Irion, U.
Spermidine, but not spermine, is essential for pigment pattern formation in zebrafish
Biol. Open
5
736-744
2016
Danio rerio (F1R3G8), Danio rerio
brenda
Pothipongsa, A.; Jantaro, S.; Incharoensakdi, A.
Spermidine synthase is required for growth of Synechococcus sp. PCC 7942 under osmotic stress
Curr. Microbiol.
73
639-645
2016
Synechococcus elongatus (Q31QK9), Synechococcus elongatus PCC 7942 (Q31QK9)
brenda
Sekula, B.; Dauter, Z.
Spermidine synthase (SPDS) undergoes concerted structural rearrangements upon ligand binding - a case study of the two SPDS isoforms from Arabidopsis thaliana
Front. Plant Sci.
10
555
2019
Arabidopsis thaliana (O48661), Arabidopsis thaliana (Q9ZUB3), Arabidopsis thaliana
brenda
Majumdar, R.; Lebar, M.; Mack, B.; Minocha, R.; Minocha, S.; Carter-Wientjes, C.; Sickler, C.; Rajasekaran, K.; Cary, J.W.
The Aspergillus flavus spermidine synthase (spds) gene, is required for normal development, aflatoxin production, and pathogenesis during infection of maize kernels
Front. Plant Sci.
9
317
2018
Aspergillus flavus (B8N4T3)
brenda
Yamasaki, K.; Tani, O.; Tateishi, Y.; Tanabe, E.; Namatame, I.; Niimi, T.; Furukawa, K.; Sakashita, H.
An NMR biochemical assay for fragment-based drug discovery evaluation of an inhibitor activity on spermidine synthase of Trypanosoma cruzi
J. Med. Chem.
59
2261-2266
2016
Trypanosoma cruzi (Q4DA73), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4DA73)
brenda
Zhang, H.; Lam, K.H.; Lam, W.W.L.; Wong, S.Y.Y.; Chan, V.S.F.; Au, S.W.N.
A putative spermidine synthase interacts with flagellar switch protein FliM and regulates motility in Helicobacter pylori
Mol. Microbiol.
106
690-703
2017
Helicobacter pylori (O25503), Helicobacter pylori
brenda
Pothipongsa, A.; Jantaro, S.; Salminen, T.A.; Incharoensakdi, A.
Molecular characterization and homology modeling of spermidine synthase from Synechococcus sp. PCC 7942
World J. Microbiol. Biotechnol.
33
72
2017
Synechococcus elongatus (Q31QK9), Synechococcus elongatus PCC 7942 (Q31QK9)
brenda