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H2N(CH2)3NH(CH2)4NH2 + S-adenosyl 3-(methylthio)propylamine
H2N(CH2)3NH(CH2)4NH(CH2)3NH2 + S-methyl-5'-thioadenosine
-
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
S-adenosylmethioninamine + 1,8-diaminooctane
5'-methylthioadenosine + N-(3-aminopropyl)octane-1,8-diamine
-
poor substrate
-
-
?
S-adenosylmethioninamine + 6,6-difluorospermidine
5'-methylthioadenosine + 6,6-difluorospermine
-
-
-
-
?
S-adenosylmethioninamine + 6-monofluorospermidine
5'-methylthioadenosine + 6-monofluorospermine
-
-
-
-
?
S-adenosylmethioninamine + 7,7-difluorospermidine
5'-methylthioadenosine + 7,7-difluorospermine
-
-
-
-
?
S-adenosylmethioninamine + 7-monofluorospermidine
5'-methylthioadenosine + 7-monofluorospermine
-
-
-
-
?
S-adenosylmethioninamine + N-(3-aminopropyl)cadaverine
5'-methylthioadenosine + ?
-
poor substrate
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine + H+
Polyamine sythesis, addition of a second aminopropyl group to the N-10 position of spermidine. The active site with a bound spermidine molecule contains an Asp276 residue, which is in an ideal position to facilitate the deprotonation of the N-10 amino group of spermidine that attacks the C-atom of the aminopropyl group of decarboxylated S-adenosylmethionine
-
-
?
S-adenosylmethioninamine + spermidine
S-methyl-5'-thioadenosine + spermine
S-adenosylmethioninamine + sym-homospermidine
5'-methylthioadenosine + ?
-
17% of the activity with spemidine
-
-
?
S-adenosylmethioninamine + sym-norspermidine
5'-methylthioadenosine + ?
-
poor substrate
-
-
?
additional information
?
-
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
-
?
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosyl-L-methioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
the enzyme, which is involved in the polyamine biosynthetic pathway in producing the final product spermine, is not essential for plant survival under normal growth conditions
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
mono and geminal difluorinated analogues of spermidine
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
strictly specific for spermidine
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
strictly specific for spermidine
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
involved in polyamine biosynthetic pathway
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
best substrate
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
mono and geminal difluorinated analogues of spermidine
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
?
S-adenosylmethioninamine + spermidine
5'-methylthioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines
-
-
?
S-adenosylmethioninamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
-
-
-
?
S-adenosylmethioninamine + spermidine
S-methyl-5'-thioadenosine + spermine
-
decarboxylated S-adenosylmethionine is an essential intermediate in the synthesis of polyamines
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
-
S-adenosylmethionine cannot act as aminopropyl donor
-
-
?
additional information
?
-
-
levels of spermidine and spermine are not only regulated by activity of spermidine synthase and spermine synthase, but also by other factors, e.g. the level of aminopropyl donor substrate, overview
-
-
?
additional information
?
-
The predominant polyamines in mammalian cells are spermidine and spermine, these polyamines are made by the sequential addition of aminopropyl groups from decarboxylated S-adenosylmethionine.
-
-
?
additional information
?
-
-
spermine synthase is clearly essential for normal development in humans
-
-
?
additional information
?
-
-
spermine synthase is clearly essential for mammalia
-
-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
-
synthetic substrates
-
-
?
additional information
?
-
-
no substrates are putrescine, cadaverine, spermine, sym-norspermine, spermidine monoacetyl derivatives
-
-
?
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1,9-diamino-4-azanonane
-
weak
1,9-Diamino-5-azanonane
-
weak
1-aminooxy-3-N-(3-aminopropyl)-aminopropane
-
competitive inhibitor
1-aminooxy-3-N-[3-aminopropyl]-aminopropane
-
aminooxy analogue of spermidine, kinetics
3,3'-Diaminodipropylamine
-
weak
3-(RS)-(5'-deoxy-5'-carbaadenos-6'-yl)spermidine
-
IC50: 750 nM
5'-methylthiotubercidin
-
strong, in vivo and in vitro, kinetics
5-[5'-deoxy-5'-(C)-4',5'-didehydroadenosyl]-L-ornithine
-
i.e. compound A9154C, prostate
N-(3-aminopropyl)cyclohexylamine
N-butyl-1,3-diaminopropane
-
IC50: 0.4 mM
N-ethylmaleimide
-
in the absence of sulfhydryl compounds
N-[(2-aminooxyethyl)-1,4-diaminobutane]
-
competitive inhibitor
N-[2-aminooxyethyl]-1,4-diaminobutane
-
aminooxy analogue of spermidine, kinetics
PCMB
-
in the absence of sulfhydryl compounds
S-5'-Deoxyadenosyl-(5')-1-methyl-3-(methylthio)propylamine
-
-
S-adenosyl-1,12-diamino-3-thio-9-azadodecane
-
IC50: 20 nM
S-Adenosyl-1,8-diamino-3-thiooctane
-
weak, prostate
S-Adenosyl-4-methylthiobutyrate
S-Adenosyl-4-thiobutyrate methylester
-
prostate
S-adenosyl-L-ethionine
-
70-98% inhibition at 1 mm
S-adenosyl-L-homocysteine
S-Tubercidinylmethionine
-
70-98% inhibition at 1 mm
5'-ethylthioadenosine
-
-
5'-ethylthioadenosine
-
strong
5'-methylthioadenosine
-
strong
5'-methylthioadenosine
-
kinetics
5'-methylthioadenosine
-
partially reversible by adenosine
5'-methylthioadenosine
SpmSyn is strongly inhibited by 5'-methylthioadenosine. This inhibition does not have great importance in limiting spermine synthesis in vivo because 5'-methylthioadenosine is normally rapidly degraded by 5'-methylthioadenosine phosphorylase. Inhibition of this enzyme allows 5'-methylthioadenosine to accumulate with deleterious effects on polyamine content.
5'-methylthioadenosine
-
strong
7,7-Difluorospermidine
-
pH-dependent, substrate inhibition
7,7-Difluorospermidine
-
pH-dependent, substrate inhibition
7-Monofluorospermidine
-
pH-dependent, substrate inhibition
7-Monofluorospermidine
-
pH-dependent, substrate inhibition
N-(3-aminopropyl)cyclohexylamine
-
IC50: 0.2 mM
N-(3-aminopropyl)cyclohexylamine
-
strong, selective
putrescine
-
-
S-Adenosyl-4-methylthiobutyrate
-
prostate
S-Adenosyl-4-methylthiobutyrate
-
70-98% inhibition at 1 mm
S-adenosyl-D-methionine
-
-
S-adenosyl-D-methionine
-
70-98% inhibition at 1 mm
S-adenosyl-L-homocysteine
-
not
S-adenosyl-L-homocysteine
-
weak
S-adenosyl-L-methionine
-
not
S-adenosyl-L-methionine
-
prostate
spermine
-
product inhibition, weak
additional information
-
no inhibition by erythro-9-(2-hydroxy-3-nonyl)adenine, methylglyoxal-bis-(guanylhydrazone), aminoguanidine, guanethidine, L-canaline, MgCl2, KCl, diamines, polyamines, polyamine derivatives
-
additional information
-
not inhibitory: decarboxylated adenosylmethionine
-
additional information
-
-
-
additional information
-
not inhibitory: decarboxylated adenosylmethionine
-
additional information
the spermine synthase-5'-methylthioadenosine structure provides a plausible explanation for the potent inhibition of the reaction by this product and the stronger inhibition of spermine synthase compared with spermidine synthase.
-
additional information
-
not inhibitory: cyclohexylamine or dicyclohexylamine; overview on inhibitors
-
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Breast Neoplasms
Antiproliferative effect of spermine depletion by N-cyclohexyl-1,3-diaminopropane in human breast cancer cells.
Breast Neoplasms
Association between plasma diacetylspermine and tumor spermine synthase with outcome in triple negative breast cancer.
Carcinogenesis
Spermine synthase overexpression in vivo does not increase susceptibility to DMBA/TPA skin carcinogenesis or Min-Apc intestinal tumorigenesis.
Carcinoma
Independent roles of eIF5A and polyamines in cell proliferation.
Carcinoma, Hepatocellular
Fluorinated analogues of spermidine as substrates of spermine synthase.
Carcinoma, Hepatocellular
Inhibition of mammalian spermine synthase by N-alkylated-1,3-diaminopropane derivatives in vitro and in cultured rat hepatoma cells.
Carcinoma, Hepatocellular
Specific depletion of spermidine and spermine in HTC cells treated with inhibitors of aminopropyltransferases.
Colorectal Neoplasms
Spermine synthase and MYC cooperate to maintain colorectal cancer cell survival by repressing Bim expression.
Colorectal Neoplasms
Supramolecular Chemotherapy: Host-Guest Complexes of Heptaplatin-Cucurbit[7]uril toward Colorectal Normal and Tumor Cells.
Colorectal Neoplasms
Supramolecular Chemotherapy: Noncovalent Bond Synergy of Cucurbit[7]uril against Human Colorectal Tumor Cells.
Deafness
Aminopropyltransferases: function, structure and genetics.
Deafness
Spermine synthase deficiency leads to deafness and a profound sensitivity to alpha-difluoromethylornithine.
Deafness
Spermine synthase.
Hypophosphatemia
Partial deletion of both the spermine synthase gene and the Pex gene in the X-linked hypophosphatemic, gyro (Gy) mouse.
Infertility
Aminopropyltransferases: function, structure and genetics.
Infertility
Spermine synthase.
Intellectual Disability
(R,R)-1,12-Dimethylspermine can mitigate abnormal spermidine accumulation in Snyder-Robinson syndrome.
Intellectual Disability
Aminopropyltransferases: function, structure and genetics.
Intellectual Disability
Myosin Va and spermine synthase: partners in exosome transport.
Intellectual Disability
New SMS mutation leads to a striking reduction in spermine synthase protein function and a severe form of Snyder-Robinson X-linked recessive mental retardation syndrome.
Intellectual Disability
Polyamine Homeostasis in Snyder-Robinson Syndrome.
Intellectual Disability
Rational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approach.
Intellectual Disability
Snyder-Robinson syndrome.
Intellectual Disability
Snyder-Robinson syndrome: A novel nonsense mutation in spermine synthase and expansion of the phenotype.
Intellectual Disability
Spermine synthase deficiency causes lysosomal dysfunction and oxidative stress in models of Snyder-Robinson syndrome.
Intellectual Disability
Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome).
Intellectual Disability
The complete loss of function of the SMS gene results in a severe form of Snyder-Robinson syndrome.
Intellectual Disability
Whole-exome sequencing identifies a novel mutation in spermine synthase gene (SMS) associated with Snyder-Robinson Syndrome.
Leukemia
Effect of S-adenosyl-1,12-diamino-3-thio-9-azadodecane, a multisubstrate adduct inhibitor of spermine synthase, on polyamine metabolism in mammalian cells.
Mental Retardation, X-Linked
New SMS mutation leads to a striking reduction in spermine synthase protein function and a severe form of Snyder-Robinson X-linked recessive mental retardation syndrome.
Mental Retardation, X-Linked
The impact of spermine synthase (SMS) mutations on brain morphology.
Muscle Hypotonia
Aminopropyltransferases: function, structure and genetics.
Muscle Hypotonia
Polyamine Homeostasis in Snyder-Robinson Syndrome.
Neoplasm Metastasis
Association between plasma diacetylspermine and tumor spermine synthase with outcome in triple negative breast cancer.
Neoplasms
Antiproliferative effect of spermine depletion by N-cyclohexyl-1,3-diaminopropane in human breast cancer cells.
Neoplasms
Association between plasma diacetylspermine and tumor spermine synthase with outcome in triple negative breast cancer.
Neoplasms
Comparative antitumor properties in rodents of irreversible inhibitors of L-ornithine decarboxylase, used as such or as prodrugs.
Neoplasms
Spermine synthase overexpression in vivo does not increase susceptibility to DMBA/TPA skin carcinogenesis or Min-Apc intestinal tumorigenesis.
Neoplasms
Supramolecular Chemotherapy: Host-Guest Complexes of Heptaplatin-Cucurbit[7]uril toward Colorectal Normal and Tumor Cells.
Osteoporosis
Polyamine Homeostasis in Snyder-Robinson Syndrome.
Osteoporosis
Snyder-Robinson syndrome: A novel nonsense mutation in spermine synthase and expansion of the phenotype.
Seizures
Polyamine Homeostasis in Snyder-Robinson Syndrome.
spermine synthase deficiency
Diagnostic screening for spermine synthase deficiency by liquid chromatography tandem mass spectrometry.
spermine synthase deficiency
Effect of spermine synthase deficiency on polyamine biosynthesis and content in mice and embryonic fibroblasts, and the sensitivity of fibroblasts to 1,3-bis-(2-chloroethyl)-N-nitrosourea.
spermine synthase deficiency
Publisher Correction: Spermine synthase deficiency causes lysosomal dysfunction and oxidative stress in models of Snyder-Robinson syndrome.
spermine synthase deficiency
Snyder-Robinson syndrome.
spermine synthase deficiency
Spermine synthase deficiency causes lysosomal dysfunction and oxidative stress in models of Snyder-Robinson syndrome.
spermine synthase deficiency
Spermine synthase deficiency leads to deafness and a profound sensitivity to alpha-difluoromethylornithine.
spermine synthase deficiency
Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome).
Triple Negative Breast Neoplasms
Association between plasma diacetylspermine and tumor spermine synthase with outcome in triple negative breast cancer.
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DELTA1-129
0.02% activity compared to the wild-type enzyme
DELTA1-19
0.003% activity compared to the wild-type enzyme
DELTA1-43
0.0002% activity compared to the wild-type enzyme
DELTA1-82
0.00023% activity compared to the wild-type enzyme
DELTA347-366
truncation of the protein at position 346 removing the last 20 residues lead to a complete loss of activity
DELTA358-366A
smaller truncation of only 9 residues has a smaller effect but still reduced activity by 75%
F58L
the mutation is associated with the Snyder-Robinson syndrome
G191S
the mutation at a site far away from the active pocket affects the active site dynamics and thus the functionality of SpmSyn. This suggests that SpmSyn functionality is regulated by networks of interacting residues and thus expands the functional and structural importance beyond the amino acids directly involved in the catalysis
G67E
the mutation is associated with the Snyder-Robinson syndrome
M35R
the mutation is associated with the Snyder-Robinson syndrome
P112L
the mutation is associated with the Snyder-Robinson syndrome
S165D/L175E/T178H/C206R
-
the mutant shows increased activity compared to the wild type enzyme
D201A
40000fold decrease in ratio kcat/Km value
D201A
mutation of Asp201 to Ala decreases the kcat/Km for decarboxylated S-adenosylmethionine by more than 100000fold
D201N
40000fold decrease in ratio kcat/Km value
D201N
mutation of Asp201 to Asn decreases the kcat/Km for decarboxylated S-adenosylmethionine by more than 100000fold
D276N
250000fold decrease in ratio kcat/Km value
D276N
alteration of this residue reduces the kcat/Km for spermidine by more than 200000fold
E353Q
1000fold decrease in ratio kcat/Km value
E353Q
mutation of Glu353 to Gln reduces the kcat/Km by 800fold
G56S
-
point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
G56S
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
G56S
the mutation destabilizes the enzyme homodimer and thus abolishes enzymatic activity
G56S
the mutation is associated with the Snyder-Robinson syndrome
I150T
-
point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
I150T
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
V132G
-
point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
V132G
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
additional information
-
the loss-of-function mutant of gene ACAULIS5 shows a severe defect in stem elongation, isolation of a T-DNA insertion mutant of gene SPMS, i.e. spms-1, showing decreased spermine levels but no obvious phenotypic alterations, an acl5-spms-1 double mutant contains no spermine but is fully viable as the wild-type and shows no phenotypic alterations under normal growth conditions, overview
additional information
-
enzyme overexpression in transgenic mice under control of a composite CMV-IE enhancer-chicken beta-actin promotor causes no deleterious effects, the mice show normal growth, fertility, and behaviour, the content of S-adenosylmethionine in transgenic mice is important for viability, overview
additional information
deletion of the N-terminal domain leads to a complete loss of spermine synthase activity
additional information
-
deletion of the N-terminal domain leads to a complete loss of spermine synthase activity
additional information
-
mutation p.G56S in the N-terminal region of spermine synthase greatly reduces spermine synthase activity and leads to severe epilepsy and cognitive impairment related to Snyder-Robinson X-linked recessive mental retardation syndrome
additional information
enzyme is able to functionally complement spermine deficiency in yeast
additional information
-
enzyme is able to functionally complement spermine deficiency in yeast
additional information
-
enzyme null mutant, lack of spermine increases sensitivity of cells to anti-tumor agents
additional information
-
yeast does not require spermine synthase since mutants in which this enzyme is deleted are viable and grow at a normal rate
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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, Rattus norvegicus Wistar
brenda
Pajula, R.L.; Raina, A.; Eloranta, T.
Polyamine synthesis in mammalian tissues. Isolation and characterization of spermine synthase from bovine brain
Eur. J. Biochem.
101
619-626
1979
Bos taurus
brenda
Raina, A.; Pajula, R.L.; Eloranta, T.
Purification of spermidine aminopropyltransferase (spermine synthase) from bovine brain
Methods Enzymol.
94
276-279
1983
Bos taurus
brenda
Eloranta, T.; Khomutov, A.R.; Khomutov, R.M.; Hyvnen, T.
Aminooxy analogues of spermidine as inhibitors of spermine synthase and substrates of hepatic polyamine acetylating activity
J. Biochem.
108
593-598
1990
Bos taurus
brenda
Coward, J.K.; Anderson, G.L.; Tang, K.C.
Aminopropyltransferase substrates and inhibitors
Methods Enzymol.
94
286-294
1983
Bos taurus, Rattus norvegicus
-
brenda
Pegg, A.E.
Inhibition of aminopropyltransferases
Methods Enzymol.
94
294-297
1983
Bos taurus, 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
Homo sapiens
brenda
Baillon, J.G.; Mamont, P.S.; Wagner, J.; Gerhart, F.; Lux, P.
Fluorinated analogues of spermidine as substrates of spermine synthase
Eur. J. Biochem.
176
237-242
1988
Bos taurus, 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
brenda
Raina, A.; Pajula, R.L.; Eloranta, T.
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