2.5.1.16: spermidine synthase
This is an abbreviated version!
For detailed information about spermidine synthase, go to the full flat file.
Word Map on EC 2.5.1.16
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2.5.1.16
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polyamine
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spermine
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s-adenosylmethionine
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ornithine
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diamine
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samdc
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dicyclohexylamine
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alpha-difluoromethylornithine
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5'-methylthioadenosine
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cadaverine
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trypanothione
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adometdc
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agmatine
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4.1.1.50
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difluoromethylornithine
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medicine
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drug development
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methylthioadenosine
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thermospermine
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nutrition
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1,3-diaminopropane
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biotechnology
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norspermidine
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multisubstrate
- 2.5.1.16
- polyamine
- spermine
- s-adenosylmethionine
- ornithine
- diamine
- samdc
- dicyclohexylamine
- alpha-difluoromethylornithine
- 5'-methylthioadenosine
- cadaverine
- trypanothione
- adometdc
- agmatine
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4.1.1.50
- difluoromethylornithine
- medicine
- drug development
- methylthioadenosine
- thermospermine
- nutrition
- 1,3-diaminopropane
- biotechnology
- norspermidine
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multisubstrate
Reaction
Synonyms
aminopropyltransferase, aminopropyltransferase spermidine synthase, AtSPDS1, AtSPDS2, MdSPDS1, PAPT, PgSPD, putrescine aminopropyltransferase, Spd synthase, SPDS, SPDS2, SPDSYN, spe-sdh, spe3, SpeE, spermidine synthase, spermidine synthase 1, spermidine synthetase, Spm synthase, SpSyn, Synpcc7942_0628, synthase, spermidine
ECTree
2.5.1.16 spermidine synthaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.5.1.16 - spermidine synthase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1H-benzimidazol-5-yl(4-[(2Z)-3-phenylprop-2-en-1-yl]piperazin-1-yl)methanone
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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
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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
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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
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with 3 carbon atoms, at 0.25 mM, not at 2.5 mM substrate concentration
arginine
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98% inhibition at 0.01 mM, 95% inhibition at 0.1 mM and 84% inhibition at 1 mM
bis-cyclohexylammonium sulfate
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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
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competitive inhibition with 1,4-diaminobutane and non-competitive with decarboxy-S-adenosyl-(5')-3-methylthiopropylamine
exo-2-aminonorbornane
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potent and selective, 98% inhibition at 0.1 mM in the presence of 1 mM of putrescine
Homospermidine
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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
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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
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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
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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
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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
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uncompetitive with S-Adenosyl-3-methylthio-1-propylamine
S-Adenosyl-1,8-diamino-3-methylthiooctane
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less efficient than the thioether
S-Inosyl(5')-3-methylthiopropylamine
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not S-inosyl(5')-3-methylthiopropanol
Sulfoxide and sulfone derivatives of decarboxylated S-adenosyl-L-homocysteine
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1,3-diaminopropane
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96% inhibition at 0.01 mM and 100% inhibition at 0.1 mM
1-Aminooxy-3-aminopropane
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brain enzyme, specific, no inhibition of spermine synthase, reversible, competitive with 1,4-diaminobutane
2-mercaptoethylamine
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competitive with 1,4-diaminobutane, reversible, its removal restores the enzyme activity, the amino group is necessary to inhibit the enzyme
5'-methylthioadenosine
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83% 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
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potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
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potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
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potent inhibition, reduces the rate of spermidine synthesis by more than 90% at 0.1 mM
Cyclohexylamine
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in vitro, 50% inhibition at 0.015 mM, competitive with 1,4-diaminobutane
decarboxylated S-adenosylhomocysteine
active site binding structure, overview
S-5'-Deoxyadenosyl(5')-2-methylthioethylamine
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the most potent inhibitor, competitive with decarboxylated S-adenosylmethionine and S-5'-deoxyadenosyl-(5')-3-ethylthiopropylamine
S-adenosyl-(5')-3-methylthio-1-propylamine
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at concentrations above 0.05 mM
S-adenosyl-(5')-3-methylthio-1-propylamine
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competitive substrate inhibition
S-adenosyl-(5')-3-methylthio-1-propylamine
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complete inhibition at 0.080 mM
S-Adenosyl-1,8-diamino-3-thiooctane
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transition-state analogue, potent inhibition
S-Adenosyl-1,8-diamino-3-thiooctane
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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
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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
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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
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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
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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
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potent, 50% inhibition at 0.025 mM
trans-4-Methylcyclohexylamine
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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
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in vitro and in vivo inhibition, reduces the spermidine and spermine content in rat tissue after oral application, quantification, overview
trans-4-Methylcyclohexylamine
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potent, 50% inhibition at 0.0017 mM, competitive with 1,4-diaminobutane
trans-4-Methylcyclohexylamine
evaluation of an inhibitor activity on spermidine synthase by an NMR biochemical assay for fragment-based drug discovery
additional information
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inhibition by end products of reaction; no inhibition by phenylhydrazine, semicarbazide, sodium borohydride, NaCN, KCl, NH4Cl, MgCl2, CaCl2, NaNO3, Na2SO4, Na2HPO4
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additional information
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inhibition by end products of reaction; no inhibition by carbonyl binding reagents
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additional information
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inhibitory potency of diverse polyamine analogues on the polyamine biosynthesis in wild-type strain and strains overexpressing polyamine biosynthetic enzymes, EC50 values, overview
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additional information
not inhibitory: S-adenosylmethioninamine concentrations up to 150 microM
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additional information
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not inhibitory: S-adenosylmethioninamine concentrations up to 150 microM
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additional information
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no inhibition by 2-mercaptoethanol at 0.1 to 1 mM
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