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Information on EC 2.5.1.16 - spermidine synthase
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2.5.1.16 spermidine synthaseIUBMB Comments
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
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Word Map
- 2.5.1.16
- polyamine
- decarboxylase
- spermine
- s-adenosylmethionine
- ornithine
- trypanothione
-
4.1.1.50
- samdc
- methylthioadenosine
- dicyclohexylamine
- adometdc
- alpha-difluoromethylornithine
- 5'-methylthioadenosine
- cadaverine
- thermospermine
- difluoromethylornithine
- 1,3-diaminopropane
- medicine
- nutrition
-
multisubstrate
- biotechnology
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
aminopropyltransferase, aminopropyltransferase spermidine synthase, MdSPDS1, PAPT, PgSPD, putrescine aminopropyltransferase, Spd synthase, SPDS, SPDS2, SPDSYN, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopropyltransferase
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aminopropyltransferase spermidine synthase
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-
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MdSPDS1
PAPT
putrescine aminopropyltransferase
Spd synthase
SPDS
SPDSYN
spe-sdh
-
enzyme is encoded by a chimeric bifunctional gene (Spe-Sdh) that also encodes saccharopine dehydrogenase (Sdh)
spermidine synthase
spermidine synthetase
synthase, spermidine
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putrescine aminopropyltransferase
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spermidine synthetase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
Michaelis-Menten kinetics
-
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
random order or ordered mechanism in which both substrates bind before the release of the products
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
ping-pong mechanism with a propylaminated form of the enzyme as an obligatory intermediate; single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
single displacement reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
first discovered
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
uni uni uni uni ping pong mechanism
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
general mechanistic hypothesis for the aminopropyl transfer reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
general mechanistic hypothesis for the aminopropyl transfer reaction
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
reaction mechanism involving a gate-keeping loop, active site and substrate binding structures and involved residues, structure-function relationship analysis by molecular dynamics simulations of a homology model
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
the enzyme possesses a Rossmann-like fold with a distinct active site, the enzyme from Helicobacter pylori lacks the gatekeeping loop that facilitates substrate binding in other PAPTs, active site structure
-
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
Escherichia coli SPDS follows the ping-pong mechanism, in which an aminopropylated enzyme intermediate was formed by the interaction of SPDS with dcSAM, prior to reaction with putrescine
S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
this mechanism depends on a conserved Asp (residue 173 in hSpdS) in the active site that interacts with the bound amine substrate to deprotonate the attacking nitrogen atom of the amine. This interaction is reinforced by additional interactions of this nitrogen atom with the hydroxyl group of a conserved Tyr (residue 79 in hSpdS) and a backbone carbonyl group (Ser174 in hSpdS). These interactions allow the attack on the methylene carbon atom of the aminopropyl group attached to the sulfonium center of dcAdoMet. Electron transfer to this sulfur atom completes the reaction forming S-methyl-5'-thioadenosine and the polyamine product. The positively charged sulfonium ion is a critical part of the reaction
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S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminopropyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase
The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor [2,7]. The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant towards other amine acceptors, such as spermidine and cadaverine [5,6]. cf. EC 2.5.1.22 (spermine synthase) and EC 2.5.1.23 (sym-norspermidine synthase).
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CAS REGISTRY NUMBER
COMMENTARY
37277-82-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
putrescine + (methyl-14C)-S-adenosylmethioninamine
spermidine + ?
-
-
-
-
?
putrescine + S-5'-deoxyadenosyl-(5')-3-methylthiopropylamine
spermidine + ?
-
-
-
-
?
S-5'-deoxyadenosyl-5'-3-butylthiopropylamine + 1,4-diaminobutane
?
-
-
-
-
?
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
-
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in a lower yield than with the natural combination
?
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-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-3-butylthio-1-propylamine + 1,4-diaminobutane
?
-
prostate enzyme
-
-
?
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
spermidine + S-adenosylmethioninamine
spermine + 5'-methylthioadenosine
in contrast to mammalian spermidine synthases, spermidine can replace to some extent putrescine as the aminopropyl acceptor
-
-
?
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-(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
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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
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-
-
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 + 1,6-diaminohexane
?
-
1% the reaction rate than with 1,4-diaminobutane
-
-
?
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
?
-
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
-
-
-
?
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
?
-
prostate enzyme
-
-
?
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-homocysteine sulfone + 1,4-diaminobutane
?
-
-
-
-
?
S-adenosyl-L-homocysteine sulfone + 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
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-3-methylthio-1-propylamine + 1,4-diaminobutane
5'-methylthioadenosine + 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-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
A0A0K2S254
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
A4HS53
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
Q8II73
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + putrescine
S-methyl-5'-thioadenosine + spermidine
Q4DA73
-
-
-
?
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
-
-
-
?
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
P19623
-
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
-
polyamine biosynthetic enzyme
-
-
?
S-adenosylmethioninamine + putrescine
5'-S-methyl-5'-thioadenosine + spermidine
Q4ADY3, Q4ADY4, Q4ADY5
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
Q9WZC2
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
P09158
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
Q8GTQ6
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
-
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
Q93X16
-
-
-
?
S-adenosylmethioninamine + putrescine
S-methyl-5'-thioadenosine + spermidine
Q93X16
-
-
-
?
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.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Na+
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-[(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
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
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
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
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
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-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-[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
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')-4-thiobutylamine
-
uncompetitive with S-Adenosyl-3-methylthio-1-propylamine
S-Adenosyl-1,8-diamino-3-methylthiooctane
-
less efficient than the thioether
S-Inosyl(5')-3-methylthiopropylamine
-
not S-inosyl(5')-3-methylthiopropanol
Sulfoxide and sulfone derivatives of decarboxylated S-adenosyl-L-homocysteine
-
-
-
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
2-mercaptoethylamine
-
competitive with 1,4-diaminobutane, reversible, its removal restores the enzyme activity, the amino group is necessary to inhibit the enzyme
5'-methylthioadenosine
-
83% inhibition at 0.01 mM and 22% inhibition at 1 mM
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
-
potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
-
in vitro, 50% inhibition at 0.015 mM, competitive with 1,4-diaminobutane
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-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
-
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
-
potent, 50% inhibition at 0.025 mM
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
-
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
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
-
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
-
no inhibition by 2-mercaptoethanol at 0.1 to 1 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerol
-
expression of SPDS is barely detectable in the callus grown on callus growth medium (composed of basal Murashige and Tucker salts), which shows steady increase on embryo-inducing medium including 2% glycerol until the end of culture at day 40. Expression level of the gene is induced by glycerol from globular embryos to cotyledonary-stage embryos to a different extent, suggesting that the polyamine biosynthetic genes are related to somatic embryogenesis
additional information
-
increased enzyme activity after wounding of the potatoe
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Neoplasms
Effects of dicyclohexylamine sulfate, a spermidine synthase inhibitor, in 9L rat brain tumor cells.
Breast Neoplasms
Targeting polyamine biosynthetic pathway through RNAi causes the abrogation of MCF 7 breast cancer cell line.
Carcinoma
Antitumor effect of dicyclohexylammonium sulfate, a potent inhibitor of spermidine, synthase.
Carcinoma, Hepatocellular
Dicyclohexylamine effects on HTC cell polyamine content and ornithine decarboxylase activity.
Carcinoma, Hepatocellular
Inhibition of spermidine synthase gene expression by transforming growth factor-beta 1 in hepatoma cells.
Carcinoma, Hepatocellular
Specific depletion of spermidine and spermine in HTC cells treated with inhibitors of aminopropyltransferases.
Chagas Disease
An NMR Biochemical Assay for Fragment-Based Drug Discovery: Evaluation of an Inhibitor Activity on Spermidine Synthase of Trypanosoma cruzi.
Chagas Disease
In silico, in vitro, X-ray crystallography, and integrated strategies for discovering spermidine synthase inhibitors for Chagas disease.
Cysts
Arabidopsis spermidine synthase is targeted by an effector protein of the cyst nematode Heterodera schachtii.
Dehydration
Genome-wide identification of genes involved in polyamine biosynthesis and the role of exogenous polyamines in Malus hupehensis Rehd. under alkaline stress.
Hypersensitivity
Engineering a spermidine biosynthetic pathway in Clostridium thermocellum results in increased resistance to furans and increased ethanol production.
Infections
Arginase Is Essential for Survival of Leishmania donovani Promastigotes but Not Intracellular Amastigotes.
Leishmaniasis
A leishmaniasis study: Structure-based screening and molecular dynamics mechanistic analysis for discovering potent inhibitors of spermidine synthase.
Leishmaniasis
Targeting polyamine metabolism for finding new drugs against leishmaniasis: a review.
Leukemia
2-Mercaptoethylamine, a competitive inhibitor of spermidine synthase in mammalian cells.
Leukemia
Antitumor effect of dicyclohexylammonium sulfate, a potent inhibitor of spermidine synthase against P388 leukemia.
Leukemia
Synthesis of N-chlorosulfonyl dicyclohexylamine as a potent inhibitor for spermidine synthase and its effects on human leukemia Molt4B cells.
Leukemia, Lymphoid
Inhibition by polyamines of methylthiopropylamine-induced ornithine decarboxylase in human lymphoid leukemia Molt 4B cells.
Leukemia, Lymphoid
Methylthiopropylamine, a potent inhibitor of spermidine synthase and its antiproliferative effect on human lymphoid leukemia Molt 4B cells.
Lymphoma, B-Cell
Chemoprevention of B-cell lymphomas by inhibition of the Myc target spermidine synthase.
Malaria
Binding and Inhibition of Spermidine Synthase from Plasmodium falciparum and Implications for In Vitro Inhibitor Testing.
Malaria
Identification of Plasmodium falciparum spermidine synthase active site binders through structure-based virtual screening.
Malaria
Structural and mechanistic insights into the action of Plasmodium falciparum spermidine synthase.
Malaria
The spermidine synthase of the malaria parasite Plasmodium falciparum: molecular and biochemical characterisation of the polyamine synthesis enzyme.
Nematode Infections
Arabidopsis spermidine synthase is targeted by an effector protein of the cyst nematode Heterodera schachtii.
Neoplasms
Binding and Inhibition of Spermidine Synthase from Plasmodium falciparum and Implications for In Vitro Inhibitor Testing.
Neoplasms
Chain-fluorinated polyamines as tumor markers--IV. Comparison of 2-fluoroputrescine and 2,2-difluoroputrescine as substrates of spermidine synthase in vitro and in vivo.
Neoplasms
Chemoprevention of B-cell lymphomas by inhibition of the Myc target spermidine synthase.
Trypanosomiasis, African
Polyamine biosynthetic enzymes as drug targets in parasitic protozoa.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
1,4-diaminobutane
-
pH 7.4, 37ºC, partially purified enzyme; pH 8.8, 37ºC, crude extracts
0.036
1,4-diaminobutane
-
pH 7.5, 37ºC, in the presence of 2-mercaptoethylamine
0.0022
S-adenosyl-3-methylthio-1-propylamine
-
pH 8.0, 37ºC, fluorometric assay
0.0022
S-adenosyl-3-methylthio-1-propylamine
-
pH 8.2, 37ºC, spectrophotometric assay
0.0067
S-adenosyl-3-methylthio-1-propylamine
-
pH 7.4, 37ºC, partially purified enzyme; pH 8.8, 37ºC, crude extracts
0.029
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant I163A
0.032
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant wild-type enzyme
0.033
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant C159S
0.035
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P162A
0.038
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant C159A
0.05
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant T160A
0.059
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P165A
additional information
additional information
knetics of wild-type and mutant enzymes
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
S-adenosylmethioninamine
pH 7.5, 80°C, recombinant mutant D101I
0.014
S-adenosylmethioninamine
pH 7.5, 80°C, recombinant mutant D170A
0.128
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant C159A
0.135
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant T160A
0.138
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant I163A
0.14
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant wild-type enzyme
0.145
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant C159S
0.15
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P165A
0.156
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P162A
0.77
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant wild-type enzyme
1.5
S-adenosylmethioninamine
pH 7.5, 80°C, recombinant mutant D173A
8.1
S-adenosylmethioninamine
pH 7.5, 80°C, recombinant mutant Y76F
22.7
S-adenosylmethioninamine
pH 7.5, 80°C, recombinant wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P165A
2.7
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant T160A
3.4
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant C159A
4.4
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant wild-type enzyme and SPS mutant C159S
4.5
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant P162A
4.8
S-adenosylmethioninamine
pH 7.5, 37°C, recombinant SPS mutant I163A
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000051
2-phenyl-1,2-thiazol-3(2H)-one
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
0.18
2H-1,4-benzothiazin-3-amine
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
0.0091
5-[(4-methylbenzyl)oxy]quinazolin-2-amine
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
0.46
isoquinolin-1-amine
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
0.53
N-methyl-N-phenyl-2,3-dihydro-1,4-benzodioxine-2-carboxamide
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
0.83
quinolin-8-yl piperidine-1-carboxylate
Trypanosoma cruzi
Q4DA73
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
transgenic plants show 5 to 6fold increase in SPDS activity and 1.3 to 2fold increase in the free spermidine content in leaves over the wild type. Significant increase in activity upon chilling in wild type and transgenics. Slightly higher chill-induced increase in SPDS activity in transgenics. pH 8.0, 37°C
additional information
-
higher level of activity in 3 out of 4 transgenic clones. pH 7.5, 37°C
additional information
-
development of a high-throughput assay using homogeneous time-resolved fluorescence based on energy transfer from europium cryptate as a donor to crosslinked allophycocyanin XL665 as an acceptor, involving a competitive immunoassay, overview
additional information
-
assay method development using micellar electrokinetic chromatography with laser-induced fluorescence detection and 7-fluoro-4-nitrobenzo-2-oxa-1,3-diazole as a fluorescence derivatization reagent
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
-
activity is 20% higher in Tris-HCl buffer than in phosphate buffer at the same pH
10.4
additional information
additional information
-
at a given pH, the activity of the enzyme in Tris buffer is lower than in phosphate or Gly-NaOH buffers
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.8
-
about 60% of maximal activity at pH 6.5 and about 85% of maximal activity at pH 9.8
8.6 - 10.6
-
about 65% of maximal activity at pH 8.6 and about 90% of maximal activity at pH 10.6
additional information
additional information
-
rapidly inactivated at pH more than 9.0 in Gly-NaOH buffer. The activity of the enzyme is generally lower in Tris buffer than in Gly-NaOH buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
37
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 50
37 - 50
sharp drop in activity above optimal temperature 50°C, profile overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is encoded by a chimeric bifunctional gene (Spe-Sdh) that also encodes saccharopine dehydrogenase (Sdh)
-
-
brenda
gene ACL5-1; var. domestica, genes ACL5-1 and ACL5-2, and SPMS
Q4ADY4
SwissProt
brenda
gene ACL5-2; var. domestica, genes ACL5-1 and ACL5-2, and SPMS
SwissProt
brenda
gene SPMS; var. domestica, genes ACL5-1 and ACL5-2, and SPMS
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
-
nucellar-derived embryogenic callus of Valencia sweet orange is maintained on callus growth medium composed of basal Murashige and Tucker salts, partially supplemented with glycerol, alpha-difluoromethylornithine or putrescine
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs. Distinct presence in mossy fiber terminals of cerebellar cortex
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
in nucellus, integuments and inner epidermis tissues of fertilized ovules
brenda
high expression detected by RT-PCR; high expression level
brenda
-
mesencephalic raphe nucelus, highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
expression in nodule inner cortical cells, vascular bundles, and central tissues. Expression is maximal at early stages of nodule development, while at later stages, the level declines
brenda
-
highest levels of expression in nucleus accumbens, taenia tecta, cerebellar cortex, cerebral cortical layer I, hippocampus, hypothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
additional information
-
the enzyme is prominently expressed in the striatal patch compartment and in putative interneurones of the matrix compartment
brenda
-
the enzyme is prominently expressed in the striatal patch compartment and in putative interneurones of the matrix compartment
brenda
-
heterogenous expression of spermidine synthase, which primarily localizes to neurons and neuropil. Highest levels of expression in accumbens nucleus, taenia tecta, cerebellar cortx, cerebral cortical layer I, hippocamppus, hippothalamus, mesencephalic raphe nuclei, central and lateral amygdala, and the circumventricular organs
brenda
mesocarp and exocarp at all developmental stages, OeSPDS genes expression patterns during early fruit development, overview
brenda
-
protoplasts from healthy or turnip yellow mosaic virus infected leaves
brenda
-
-
brenda
high expression detected by RT-PCR, low expression detected in adventitious and hairy roots; high expression level
brenda
additional information
genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview
brenda
additional information
Q4ADY4
genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview
brenda
additional information
genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview; genes ACL5 and SPMS are differentially expressed in tissues and suspension cells, expression analysis, overview
brenda
additional information
tissue specific SPDS expression analysis, overview
brenda
additional information
tissue specific expression analysis, overview
brenda
additional information
-
immunohistochemic tissue expression analysis
brenda
additional information
immunohistochemic localization analysis, overview
brenda
additional information
-
immunohistochemic localization analysis, overview
brenda
additional information
-
immunohistochemic localization analysis, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
spermidine synthase is a key enzyme for polyamine biosynthesis
physiological function
additional information
malfunction
-
single spe-sdh mutants are isolated after sexual recombination in planta with a compatible wild-type strain. Mutants are auxotrophic for lysine and spermidine, but not for putrescine, and contain putrescine and spermidine, but not spermine. spe-sdh are were sensitive to stress, unable to carry out the yeast-to-mycelium dimorphic transition, and show attenuated virulence to maize. These phenotypic alterations are reverted by complementation with the wild-type gene
malfunction
-
microarray experiments with a spermidine synthase, spermine oxidase mutant (DELTAspe3DELTAfms1) strain are performed to investigate the responsiveness of yeast genes to supplementation with spermidine or spermine. Expression analysis identified genes responsive to the addition of either excess spermidine or spermine compared to a control culture. Results from global gene expression profiling demonstrate a more major role for spermidine in modulating gene expression in yeast than spermine
malfunction
-
an enzyme-deficient strain is auxotrophic for polyamines, requires spermidine for growth in its insect vector form, and is adversely impacted in its ability to infect mice
malfunction
-
an enzyme-deficient strain is auxotrophic for polyamines, requires spermidine for growth in its insect vector form, and is adversely impacted in its ability to infect mice
-
physiological function
-
in vitro shoots of a transgenic European pear overexpressing apple spermidine synthase (MdSPDS1) and the wild-type are subjected to long-term stress for 0.03 mM AlCl3. SPDS expression level and spermidine titer of the transgenic line are substantially higher than those of wild-type when subjected to long-term Al stress. Transgenic line show showed higher tolerance to Al stress, and its ameliorated performance is closely correlated to polyamine accumulation, especially, to a higher spermidine titer chiefly via alleviating oxidative status as well as by affecting mineral element balance
physiological function
PgSPD expression is slightly induced by mannitol and CuSO4. Salt, chilling, abscisic acid and jasmonic acid trigger a significant induction of PgSPD expression within 12-24 h post-treatment, especially PgSPD is prominently induced by salt (41.5fold)
physiological function
-
transgenic plants expressing the cyst nematode (Heterodera glycines) effector protein 10A06 exhibit elevated SPDS2 mRNA abundance, significantly higher spermidine content, and increased polyamine oxidase activity. The SPDS2 promoter is strongly activated in the nematode-induced syncytia, and transgenic plants overexpressing SPDS2 show enhanced plant susceptibility to Heterodera schachtii. These data lend strong support to a model in which the cyst nematode effector 10A06 exerts its function through the interaction with SPDS2, thereby increasing spermidine content and subsequently polyamine oxidase activity
physiological function
-
to verify whether spermidine synthase can confer long-term multi-heavy metal tolerance, in vitro shoots of a transgenic European pear overexpressing apple SPDS are subjected to stress using either CdCl2, PbCl2, ZnCl2, or a combination thereof. The results suggest that spermidine-levels are implicated in enhanced heavy metal tolerance, possibly by exerting an antioxidant activity as well as by the properties of spermidine per se including metal chelator
physiological function
-
spermidine synthhase is responsible for spermdine synthesis from putrescine, the polyamines putrescine, spermidine and spermine are cationic molecules that are found in all eukaryotic cells and are clearly essential to growth and development
physiological function
spermidine synthase is an important enzyme in the synthetic pathway of polyamines in the parasite, is an essential element for the survival of this protozoan
physiological function
-
spermidine synthase is required for virulence of Leishmania donovani
physiological function
spermidine synthase plays a crucial role in cell proliferation and differentiation
physiological function
spermidine synthase catalyses the formation of spermidine, which is an essential polyamine, spermidine is also a precursor to further polyamines, such as spermine and thermospermine, most of which contribute to tolerance against drought and salinity in plants. Thermospermine is indispensible for vascular tissue growth
physiological function
-
the parasite resists ornithine decarboxylase inhibitors by overexpression of spermidine synthase mRNA
physiological function
-
spermidine synthase is required for virulence of Leishmania donovani
-
physiological function
-
spermidine synthase catalyses the formation of spermidine, which is an essential polyamine, spermidine is also a precursor to further polyamines, such as spermine and thermospermine, most of which contribute to tolerance against drought and salinity in plants. Thermospermine is indispensible for vascular tissue growth
-
additional information
ligand docking modeling using the tertiary structure model, overview
additional information
homozygous overexpressing transgenic tomato plant lines show a high level of Md-SPDS1 mRNA expression and a 1.5 to 2fold increase in the levels of free spermidine in fruits compared to the wild-type plants. Analysis of pericarp-columella and metabolites in placenta tissues reveal distinct metabolic profiles between the wild-type and transgenic lines, particularly at the late ripening stages, phenotypes, overview. The transgenic tomato fruits also show an increase in carotenoid accumulation, especially in lycopene, and increased ethylene production compared to wild-type fruits. Genes responsible for lycopene biosynthesis, including phytoene synthase, phytoene desaturase, and deoxy-D-xylulose 5-phosphate synthase, are significantly up-regulated in ripe transgenic fruits, whereas genes involved in lycopene degradation, including lycopene-epsilon cyclase and lycopene beta cyclase, are downregulated in the transgenic fruits compared to the wild-type
additional information
-
overexpression of yeast spermidine synthase impacts ripening, senescence and decay symptoms in tomato. Constitutive expression of ySpdSyn enhances intracellular levels of Spd in the leaf, and transiently during fruit development, whereas E8-ySpdSyn expression leads to Spd accumulation early and transiently during fruit ripening. The ySpdSyn transgenic fruits have a longer shelf life, reduced shriveling and delayed decay symptom development in comparison with the wild-type fruits, crop maturity is delayed in a CaMV35S-ySpdSyn genotype, with fruits accumulating higher levels of the antioxidant lycopene. Notably, whole-plant senescence in the transgenic plants is also delayed compared with wild-type plants, phenotypes, overview
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Pseudomonas aeruginosa (strain UCBPP-PA14)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Trypanosoma cruzi (strain CL Brener)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)