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3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
acetyl-CoA + (S)-2-[(3-aminopropyl)amino]ethylphosphoric acid
CoA + N-acetyl-(S)-2-[(3-aminopropyl)amino]ethylphosphoric acid
-
WR-2721, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + (S)-2-[(3-aminopropyl)amino]propylphosphoric acid
CoA + N-acetyl-(S)-2-[(3-aminopropyl)amino]propylphosphoric acid
-
WR-44923, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
acetyl-CoA + 1,3-diaminopropane
CoA + ?
-
-
-
?
acetyl-CoA + 1,3-diaminopropane
CoA + N1-acetyl-1,3-diaminopropane
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
acetyl-CoA + 1,6-diaminohexane
CoA + N1-acetyl-1,6-diaminohexane
acetyl-CoA + 1,7-diaminoheptane
CoA + N1-acetyl-1,7-diaminoheptane
-
-
-
-
?
acetyl-CoA + 15-deoxyspergualin
?
-
antitumor and immunosuppressive agent 15-deoxyspergualin, about 18% of the rate with spermidine
-
-
?
acetyl-CoA + 2-[(aminopropyl)amino]ethanethiol
CoA + N-acetyl-2-[(aminopropyl)amino]ethanethiol
-
radioprotective drug WR-1065, lower affinity than for spermidine, about 10% of the rate with spermidine
-
-
?
acetyl-CoA + 6,6-difluorospermidine
CoA + N1-acetyl-6,6-difluorospermidine
-
16.6% of the rate with spermidine
-
-
?
acetyl-CoA + 7,7-difluorospermidine
CoA + N1-acetyl-7,7-difluorospermidine
-
19.7% of the rate with spermidine
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
acetyl-CoA + aminopropylcadaverine
?
-
-
-
-
?
acetyl-CoA + beta-phenylethylamine
CoA + N-acetylphenylethylamine
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
acetyl-CoA + diethylenetriamine
CoA + ?
-
-
-
?
acetyl-CoA + diethylenetriamine
CoA + N1-acetyl-diethylenetriamine
-
-
-
?
acetyl-CoA + eIF5A
CoA + acytyl-eIF5A
-
selective acetylation of the hypusine and/or deoxyhypusine residue of translation initiation factor eIF5A, resulting in loss of eIF5A activity. Hypusine or deoxyhypusine, as the free amino acid, do not act as a substrate for isoform SSAT1
-
?
acetyl-CoA + ethylenediamine
CoA + N1-acetyl-ethylenediamine
-
-
-
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
acetyl-CoA + histone
CoA + N-acetylhistone
-
-
-
-
?
acetyl-CoA + N-(n-butyl)-1,3-diaminopropane
CoA + N1-acetyl-N3-(n-butyl)-1,3-diaminopropane
-
weak substrate, lower affinity than for spermidine, 1.3% of the rate with spermidine
-
-
?
acetyl-CoA + N-acetylputrescine
CoA + N1,N4-diacetylputrescine
acetyl-CoA + N1-acetylspermidine
CoA + N1,N8-diacetylspermidine
-
low affinity
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
acetyl-CoA + N1-dansylnorspermine
CoA + N1-acetyl-N1-dansylnorspermine
-
the acetylation reaction proceeds by Bi-Bi mechanism
-
-
?
acetyl-CoA + N1-dansylspermine
CoA + N1-acetyl-N1-dansylspermine
-
-
-
-
?
acetyl-CoA + N1-methyl-1,3-diaminopropane
CoA + ?
-
-
-
?
acetyl-CoA + N8-acetylspermidine
CoA + N1,N8-diacetylspermidine
-
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
acetyl-CoA + poly-L-lysine
CoA + acetyl-poly-L-lysine
-
-
-
?
acetyl-CoA + putrescine
CoA + acetylputrescine
-
breakdown of spermidine and putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
acetyl-CoA + putrescine
CoA + N1-acetylputrescine
acetyl-CoA + spermidine
CoA + N1-acetyl-spermidine
acetyl-CoA + spermidine
CoA + N1-acetyl-sym-norspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
acetyl-CoA + spermine
CoA + N1-acetyl-spermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
acetyl-CoA + sym-norspermidine
CoA + N1-acetyl-sym-norspermidine
acetyl-CoA + sym-norspermine
CoA + N1-acetyl-sym-norspermine
acetyl-CoA + triethylenetetramine
?
chloroacetyl-CoA + spermine
N1-spermine-acetyl-CoA + ?
N1-chloroacetylation of spermine performed by hSSAT protein, pH 7.5 and 2 microM recombinant human SSAT protein at room temperature for one hour, identity of the product confirmed by mass spectrometry
-
-
?
additional information
?
-
3 acetyl-CoA + 2 spermine

3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + spermidine

3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
spermidine is preferred over spermine
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
cased on structural and docking analysis, it is expected that Glu53 and Tyr93 are key residues for recognizing spermidine
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane

?
an extremely poor substrate of human recombinant SSAT2, that is metabolized by SSAT1 in Hep-G2 cells and in wild-type primary hepatocytes
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
SSAT1 is the main acetylator of 1,12-diamino-3,6,9-triazadodecane compared to SSAT2
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
SSAT1 is the main acetylator of 1,12-diamino-3,6,9-triazadodecane compared to SSAT2
-
-
?
acetyl-CoA + 1,3-diaminopropane

CoA + N1-acetyl-1,3-diaminopropane
-
-
-
ir
acetyl-CoA + 1,3-diaminopropane
CoA + N1-acetyl-1,3-diaminopropane
-
-
-
?
acetyl-CoA + 1,3-diaminopropane
CoA + N1-acetyl-1,3-diaminopropane
-
at a low rate
-
-
?
acetyl-CoA + 1,3-diaminopropane
CoA + N1-acetyl-1,3-diaminopropane
-
-
-
-
?
acetyl-CoA + 1,5-diaminopentane

CoA + N1-acetyl-1,5-diaminopentane
-
at 39% of the rate with putrescine
-
-
?
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
-
cadaverine
-
ir
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
-
at 45% of the rate with putrescine
-
-
?
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
-
-
-
-
?
acetyl-CoA + 1,5-diaminopentane
CoA + N1-acetyl-1,5-diaminopentane
-
-
-
-
?
acetyl-CoA + 1,6-diaminohexane

CoA + N1-acetyl-1,6-diaminohexane
-
-
-
ir
acetyl-CoA + 1,6-diaminohexane
CoA + N1-acetyl-1,6-diaminohexane
-
at 50% of the rate with putrescine
-
-
?
acetyl-CoA + 1,6-diaminohexane
CoA + N1-acetyl-1,6-diaminohexane
-
at 74% of the rate with putrescine
-
-
?
acetyl-CoA + amantadine

CoA + N1-acetylamantadine
-
-
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
-
reaction occurs in vivo and in vitro, but only in presence of increased enzyme levels, amantadine may be a specific drug substrate for SSAT
-
?
acetyl-CoA + histamine

CoA + N-acetylhistamine
-
at about 30% of the rate with putrescine
-
-
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
-
at about 30% of the rate with putrescine
-
-
?
acetyl-CoA + N-acetylputrescine

CoA + N1,N4-diacetylputrescine
-
-
-
-
?
acetyl-CoA + N-acetylputrescine
CoA + N1,N4-diacetylputrescine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine

CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
reaction in vitro, but not in vivo
-
ir
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + norspermidine

CoA + N1-acetylnorspermidine
-
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + putrescine

CoA + N-acetylputrescine
-
-
-
?, ir
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
preference for putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
preference for putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
Trichosporon melibiosaceum
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
Trichosporon melibiosaceum CBS 6087
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
-
-
?
acetyl-CoA + putrescine

CoA + N1-acetylputrescine
poor substrate
-
-
?
acetyl-CoA + putrescine
CoA + N1-acetylputrescine
-
-
-
?
acetyl-CoA + spermidine

CoA + N1-acetyl-spermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetyl-spermidine
spermidine is preferred over spermine
-
-
?
acetyl-CoA + spermidine

CoA + N1-acetylspermidine
-
very poor substrate, at 2-4% of the rate with putrescine
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
N1-acetylspermidine is the major product
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
spermidine acetylation might be a strategy for inhibiting growth in response to environmental stresses
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
catabolism of spermidine and spermine
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
catabolism of spermidine and spermine
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
mimics of transition state of SSAT1 reaction analyzed
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
very poor substrate, at 2-4% of the rate with putrescine
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
physiological substrate, higher rate than with spermine
product is exclusively N1-acetylspermidine
ir
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
spermidine and spermine may be physiological substrates, enzyme may play an important role in interconversion of polyamines
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
Trichosporon melibiosaceum
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
Trichosporon melibiosaceum CBS 6087
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
+ N8-acetylspermidine, ratio N1 acetylspermidine:N8-acetylspermidine is 50:45
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
breakdown of spermidine and putrescine, key agent in the supply of nitrogen to the cell
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
+ N8-acetylspermidine, ratio N1 acetylspermidine:N8-acetylspermidine is 50:45
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
breakdown of spermidine and putrescine, key agent in the supply of nitrogen to the cell
-
-
?
acetyl-CoA + spermine

CoA + N1-acetylspermine
-
very poor substrate, at 2-4% of the rate with putrescine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
spermidine is preferred over spermine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
preferred substrate
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
about 40% of the rate with spermidine
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
catabolism of spermidine and spermine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
N1-acetylation of spermidine and spermine by spermidine/spermine acetyltransferase (SSAT) crucial for regulation of the cellular polyamine levels in eukaryotic cells
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
mimics of transition state of SSAT1 reaction analyzed
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
N1-acetylation of spermidine and spermine by spermidine/spermine acetyltransferase (SSAT) crucial for regulation of the cellular polyamine levels in eukaryotic cells, chemical and kinetic mechanism for acetyl transfer activity by recombinant human SSAT protein proposed
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
pharmacologic and genetic manipulation of keratin 6 (K6)-spermidine/spermine N1-acetyltransferase (SSAT) transgenic mice subjected to carcinogenesis
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
spermine and the enzyme and form a proton wire between the side chain of Glu92 and the N1 amine of spermine, a single water molecule forms hydrogen bonds with the side chains of Glu92, Asp93, and the N4 amine of spermine, substrate binding structure, overview
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
very poor substrate, at 2-4% of the rate with putrescine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
physiological substrate, lower rate than with spermidine
-
ir
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
spermidine and spermine may be physiological substrates, enzyme may play an important role in interconversion of polyamines
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
preferred substrate
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
preferred substrate
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
spermidine is preferred over spermine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + sym-norspermidine

CoA + N1-acetyl-sym-norspermidine
-
-
-
-
ir
acetyl-CoA + sym-norspermidine
CoA + N1-acetyl-sym-norspermidine
-
-
-
-
?
acetyl-CoA + sym-norspermidine
CoA + N1-acetyl-sym-norspermidine
-
high affinity for sym-norspermidine
-
-
?
acetyl-CoA + sym-norspermidine
CoA + N1-acetyl-sym-norspermidine
-
identical with caldine
-
-
?
acetyl-CoA + sym-norspermine

CoA + N1-acetyl-sym-norspermine
-
at a much lower rate than with sym-norspermidine
-
-
ir
acetyl-CoA + sym-norspermine
CoA + N1-acetyl-sym-norspermine
-
-
-
-
?
acetyl-CoA + triethylenetetramine

?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
acetyl-CoA + triethylenetetramine
?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
additional information

?
-
-
not: histone
-
-
?
additional information
?
-
-
not: histone
-
-
?
additional information
?
-
-
not: dopamine, serotonin
-
-
?
additional information
?
-
-
enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
-
-
?
additional information
?
-
-
important function in the degradation of diamines of lower eukaryotes
-
-
?
additional information
?
-
-
first enzyme in polyamine catabolism
-
-
?
additional information
?
-
polyamine-dependent protein synthesis is only found in isozymes Ssat1b and Ssat1c, not in Ssat1a. Also only Ssat1b and Ssat1c, but not the polyamine-insensitive Ssat1a, are able to interact with integrin alpha9 and Hif-1alpha. Substrate preferences of the isoenzymes are different. Ssat1b has similar Km values for spermidine and spermine, while Ssat1a has a smaller Km toward spermidine and Ssat1c has a smaller Km for spermine. Ssat1a and Ssatb have a better kcat/Km value for spermidine than that for spermine
-
-
?
additional information
?
-
-
polyamine-dependent protein synthesis is only found in isozymes Ssat1b and Ssat1c, not in Ssat1a. Also only Ssat1b and Ssat1c, but not the polyamine-insensitive Ssat1a, are able to interact with integrin alpha9 and Hif-1alpha. Substrate preferences of the isoenzymes are different. Ssat1b has similar Km values for spermidine and spermine, while Ssat1a has a smaller Km toward spermidine and Ssat1c has a smaller Km for spermine. Ssat1a and Ssatb have a better kcat/Km value for spermidine than that for spermine
-
-
?
additional information
?
-
spermine binding structure by X-ray diffraction scattering analysis, overview
-
-
?
additional information
?
-
the enzyme does not acetylate RcsB in vitro
-
-
-
additional information
?
-
-
the enzyme does not acetylate RcsB in vitro
-
-
-
additional information
?
-
-
not: 1-methylspermidine, WR-2822
-
-
?
additional information
?
-
-
Lys-141 is the first residue in a KRR motif that makes up part of the active site
-
-
?
additional information
?
-
-
enzyme requires a substrate with the structure H2N(CH2)3NHR and acetylates the primary amino group
-
-
?
additional information
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
stress-induced enzyme
-
-
?
additional information
?
-
-
acetylation is a physiological response to convert excess polyamines to a physiologically inert form which is readily excreted
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
first enzyme in polyamine catabolism
-
-
?
additional information
?
-
-
enzyme plays an efficient role in maintaining polyamine pool homeostasis during challenges with exogenous polyamines
-
-
?
additional information
?
-
-
rate-limiting enzyme in the degradation and interconversion of polyamines
-
-
?
additional information
?
-
-
SSAT prevents overaccumulation of higher polyamines from becoming toxic to cell and maintains a balanced ratio of polyamines according to cellular needs
-
-
?
additional information
?
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
substrate specificity of isozyme SSAT-1 in descending order: norspermidine equal spermidine, spermine, N1-acetylspermine, putrescine
-
-
?
additional information
?
-
substrate specificity of isozyme SSAT-1 in descending order: norspermidine equal spermidine, spermine, N1-acetylspermine, putrescine
-
-
?
additional information
?
-
-
substrate specificity of isozyme SSAT-1 in descending order: norspermidine equal spermidine, spermine, N1-acetylspermine, putrescine
-
-
?
additional information
?
-
substrate specificity of isozyme SSAT-2 in descending order: norspermidine, spermidine equal spermine, N1-acetylspermine equal putrescine
-
-
?
additional information
?
-
substrate specificity of isozyme SSAT-2 in descending order: norspermidine, spermidine equal spermine, N1-acetylspermine equal putrescine
-
-
?
additional information
?
-
-
substrate specificity of isozyme SSAT-2 in descending order: norspermidine, spermidine equal spermine, N1-acetylspermine equal putrescine
-
-
?
additional information
?
-
-
the enzyme functions as a coactivator for NF-kappaB and cooperates with CREB-binding protein and the p300/CBP-associated factor to enhance NF-kappaB-dependent transcription
-
-
?
additional information
?
-
-
polyamines regulate SSAT mRNA translational efficiency by inhibiting a repressor protein from binding to regions of the coding sequence of the SSAT transcript
-
-
?
additional information
?
-
roles of SSAT proteins in oxygen homeostasis, SSAT1 binding to hypoxia-inducible factor-1 (HIF-1alpha) promotes its ubiquitination/degradation, in contrast to SSAT2, SSAT1 acts by stabilizing the interaction of HIF-1alpha with RACK1
-
-
?
additional information
?
-
-
N1,N11-diethylnorspermine induces apoptosis involving increased SSAT activity and the mitochondria of the cell
-
-
?
additional information
?
-
-
simultaneous drug combination or quinoxaline pre-treatment synergistically increases SSAT expression, depletes polyamines, increases reactive oxygen species production, and produces synergistic tumor cell killing in both cell lines, overview. Cisplatin-resistant human ovarian cell line, A2780/CP cells, cannot be induced by spermidine analogues, in contrast to the sensitive counterpart A2780
-
-
?
additional information
?
-
-
SSAT binds to the HIF-1alpha subunit and promotes its ubiquitination and degradation. SSAT transcriptional regulation, regulation of SSAT protein levels by polyamines or analogues, SSAT protein turnover, overview. Upregulation of the Sat1 gene transcription is critical for the cell-specific polyamine or analog-mediated increase in SSAT content
-
-
?
additional information
?
-
-
SSAT expression causes arrest of cell cycle and cell growth in the S-phase in transfected cells through a mechanism involving the suppression of cyclin A and E2F1-expression, overview
-
-
?
additional information
?
-
-
SSAT induction increased metabolic flux by about 5fold, overview. The metabolic flux can be interrupted by inhibition of polyamine biosynthesis but not by inhibition of polyamine oxidation
-
-
?
additional information
?
-
the enzyme transforms polyamines into putrescine
-
-
?
additional information
?
-
-
the enzyme transforms polyamines into putrescine
-
-
?
additional information
?
-
human SSAT1 binds to the PAS-B (Per-ARNT-Sim) domain of HIF-1alpha, a key regulator of oxygen homeostasis in all metazoans, facilitating its degradation
-
-
?
additional information
?
-
-
human SSAT1 binds to the PAS-B (Per-ARNT-Sim) domain of HIF-1alpha, a key regulator of oxygen homeostasis in all metazoans, facilitating its degradation
-
-
?
additional information
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
SSAT catalyzes together with polyamine oxidase the back-conversion of spermine to spermidine and the latter to putrescine, a function lowering polyamine pools by facilitating their catabolism and excretion
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
enzyme plays an efficient role in maintaining polyamine pool homeostasis during challenges with exogenous polyamines
-
-
?
additional information
?
-
-
the enzyme is involved in intestinal tumorigenesis in ApcMin/+ MIN mice, enzyme is involved in catabolism of polyamines, activation of the enzyme in vivo results in suppression of tumor outgrowth in a mouse prostate cancer model
-
-
?
additional information
?
-
-
the enzyme is rate-limiting in polyamine catabolism
-
-
?
additional information
?
-
-
participates in polyamine homeostasis by regulating polyamine export and catabolism. Expression status of spermidine/spermine N1-acetyltransferase alters body fat accumulation by metabolically modulating tissue acetyl- and malonyl-CoA levels, thereby influencing fatty acid biosynthesis and oxidation
-
-
?
additional information
?
-
-
SSAT gene expression is fine-tuned by regulated unproductive splicing and translation, which is modulated by polyamine levels
-
-
?
additional information
?
-
-
regulation of SSAT protein levels by polyamines or analogues, overview
-
-
?
additional information
?
-
SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway. No activity with putrescine, cadaverine, lysine, thialysine, amantadine, substrate specificity, overview
-
-
?
additional information
?
-
-
not: histone
-
-
?
additional information
?
-
-
not: dopamine, serotonin
-
-
?
additional information
?
-
-
enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
-
-
?
additional information
?
-
-
not: histone
-
-
?
additional information
?
-
-
not: histone
-
-
?
additional information
?
-
-
enzyme requires a substrate with the structure H2N(CH2)3NHR and acetylates the primary amino group
-
-
?
additional information
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
not: putrescine
-
-
?
additional information
?
-
-
not: sym-homospermidine
-
-
?
additional information
?
-
-
regulation of SSAT protein levels by polyamines or analogues, overview
-
-
?
additional information
?
-
no substrates: glycine, glutamate, aspartate, leucine, alanine or arginine
-
-
?
additional information
?
-
spermine and spermidine are the preferential substrates, no activity with cadaverine. Conformational differences between enzyme SpeG ligand-free and liganded structures, allosteric substrate binding site structure, overview
-
-
?
additional information
?
-
-
spermine and spermidine are the preferential substrates, no activity with cadaverine. Conformational differences between enzyme SpeG ligand-free and liganded structures, allosteric substrate binding site structure, overview
-
-
?
additional information
?
-
substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
-
-
?
additional information
?
-
-
substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
-
-
?
additional information
?
-
substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
-
-
?
additional information
?
-
spermine and spermidine are the preferential substrates, no activity with cadaverine. Conformational differences between enzyme SpeG ligand-free and liganded structures, allosteric substrate binding site structure, overview
-
-
?
additional information
?
-
-
not: methylamine, dimethylamine, di-n-butylamine, L-lysine, benzylamine, semicarbazide, L-serine, glyoxylate, oxaloacetate, 4-aminobenzoate, 2-aminobenzoate
-
-
?
additional information
?
-
-
not: methylamine, dimethylamine, di-n-butylamine, L-lysine, benzylamine, semicarbazide, L-serine, glyoxylate, oxaloacetate, 4-aminobenzoate, 2-aminobenzoate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
acetyl-CoA + 1,3-diaminopropane
CoA + ?
-
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
acetyl-CoA + diethylenetriamine
CoA + ?
-
-
-
?
acetyl-CoA + eIF5A
CoA + acytyl-eIF5A
-
selective acetylation of the hypusine and/or deoxyhypusine residue of translation initiation factor eIF5A, resulting in loss of eIF5A activity. Hypusine or deoxyhypusine, as the free amino acid, do not act as a substrate for isoform SSAT1
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
acetyl-CoA + N1-methyl-1,3-diaminopropane
CoA + ?
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
acetyl-CoA + putrescine
CoA + acetylputrescine
-
breakdown of spermidine and putrescine
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
acetyl-CoA + spermine
CoA + N1-acetylspermine
acetyl-CoA + triethylenetetramine
?
additional information
?
-
3 acetyl-CoA + 2 spermine

3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
-
?
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
3 acetyl-CoA + spermidine

3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
-
?
3 acetyl-CoA + spermidine
3 CoA + N1,N4,N8-triacetylspermidine
-
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane

?
an extremely poor substrate of human recombinant SSAT2, that is metabolized by SSAT1 in Hep-G2 cells and in wild-type primary hepatocytes
-
-
?
acetyl-CoA + 1,12-diamino-3,6,9-triazadodecane
?
SSAT1 is the main acetylator of 1,12-diamino-3,6,9-triazadodecane compared to SSAT2
-
-
?
acetyl-CoA + amantadine

CoA + N1-acetylamantadine
-
-
-
-
?
acetyl-CoA + amantadine
CoA + N1-acetylamantadine
-
reaction occurs in vivo and in vitro, but only in presence of increased enzyme levels, amantadine may be a specific drug substrate for SSAT
-
?
acetyl-CoA + N1-acetylspermine

CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
?
acetyl-CoA + N1-acetylspermine
CoA + N1,N12-diacetylspermine
-
-
-
-
?
acetyl-CoA + norspermidine

CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + spermidine

CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
spermidine acetylation might be a strategy for inhibiting growth in response to environmental stresses
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
catabolism of spermidine and spermine
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
catabolism of spermidine and spermine
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
spermidine and spermine may be physiological substrates, enzyme may play an important role in interconversion of polyamines
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
breakdown of spermidine and putrescine, key agent in the supply of nitrogen to the cell
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
breakdown of spermidine and putrescine, key agent in the supply of nitrogen to the cell
-
-
?
acetyl-CoA + spermine

CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
catabolism of spermidine and spermine
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
N1-acetylation of spermidine and spermine by spermidine/spermine acetyltransferase (SSAT) crucial for regulation of the cellular polyamine levels in eukaryotic cells
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
-
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
-
spermidine and spermine may be physiological substrates, enzyme may play an important role in interconversion of polyamines
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
preferred substrate
-
-
?
acetyl-CoA + spermine
CoA + N1-acetylspermine
preferred substrate
-
-
?
acetyl-CoA + triethylenetetramine

?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
acetyl-CoA + triethylenetetramine
?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
additional information

?
-
-
enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
-
-
?
additional information
?
-
-
important function in the degradation of diamines of lower eukaryotes
-
-
?
additional information
?
-
-
first enzyme in polyamine catabolism
-
-
?
additional information
?
-
-
stress-induced enzyme
-
-
?
additional information
?
-
-
acetylation is a physiological response to convert excess polyamines to a physiologically inert form which is readily excreted
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
polyamine catabolic enzyme
-
-
?
additional information
?
-
-
first enzyme in polyamine catabolism
-
-
?
additional information
?
-
-
enzyme plays an efficient role in maintaining polyamine pool homeostasis during challenges with exogenous polyamines
-
-
?
additional information
?
-
-
rate-limiting enzyme in the degradation and interconversion of polyamines
-
-
?
additional information
?
-
-
SSAT prevents overaccumulation of higher polyamines from becoming toxic to cell and maintains a balanced ratio of polyamines according to cellular needs
-
-
?
additional information
?
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
-
isozyme SSAT-2 shows very low activity in intact wild-type cells, but is equally active to isozyme SSAT-1 in recombinantly transfected cells
-
-
?
additional information
?
-
-
the enzyme functions as a coactivator for NF-kappaB and cooperates with CREB-binding protein and the p300/CBP-associated factor to enhance NF-kappaB-dependent transcription
-
-
?
additional information
?
-
-
N1,N11-diethylnorspermine induces apoptosis involving increased SSAT activity and the mitochondria of the cell
-
-
?
additional information
?
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simultaneous drug combination or quinoxaline pre-treatment synergistically increases SSAT expression, depletes polyamines, increases reactive oxygen species production, and produces synergistic tumor cell killing in both cell lines, overview. Cisplatin-resistant human ovarian cell line, A2780/CP cells, cannot be induced by spermidine analogues, in contrast to the sensitive counterpart A2780
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SSAT binds to the HIF-1alpha subunit and promotes its ubiquitination and degradation. SSAT transcriptional regulation, regulation of SSAT protein levels by polyamines or analogues, SSAT protein turnover, overview. Upregulation of the Sat1 gene transcription is critical for the cell-specific polyamine or analog-mediated increase in SSAT content
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SSAT expression causes arrest of cell cycle and cell growth in the S-phase in transfected cells through a mechanism involving the suppression of cyclin A and E2F1-expression, overview
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SSAT induction increased metabolic flux by about 5fold, overview. The metabolic flux can be interrupted by inhibition of polyamine biosynthesis but not by inhibition of polyamine oxidation
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the enzyme transforms polyamines into putrescine
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the enzyme transforms polyamines into putrescine
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SSAT catalyzes together with polyamine oxidase the back-conversion of spermine to spermidine and the latter to putrescine, a function lowering polyamine pools by facilitating their catabolism and excretion
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polyamine catabolic enzyme
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polyamine catabolic enzyme
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polyamine catabolic enzyme
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enzyme plays an efficient role in maintaining polyamine pool homeostasis during challenges with exogenous polyamines
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the enzyme is involved in intestinal tumorigenesis in ApcMin/+ MIN mice, enzyme is involved in catabolism of polyamines, activation of the enzyme in vivo results in suppression of tumor outgrowth in a mouse prostate cancer model
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the enzyme is rate-limiting in polyamine catabolism
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participates in polyamine homeostasis by regulating polyamine export and catabolism. Expression status of spermidine/spermine N1-acetyltransferase alters body fat accumulation by metabolically modulating tissue acetyl- and malonyl-CoA levels, thereby influencing fatty acid biosynthesis and oxidation
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SSAT gene expression is fine-tuned by regulated unproductive splicing and translation, which is modulated by polyamine levels
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regulation of SSAT protein levels by polyamines or analogues, overview
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SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway. No activity with putrescine, cadaverine, lysine, thialysine, amantadine, substrate specificity, overview
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enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
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regulation of SSAT protein levels by polyamines or analogues, overview
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evolution

phylogenetic analysis of ssat-like genes dividing the genes into 3 clusters, comparison of zebrafish and human gene sequences and regulation, overview
evolution
phylogenetic analysis of ssat-like genes dividing the genes into 3 clusters, comparison of zebrafish and human gene sequences and regulation, overview. Zebrafish ssat1 homologues are paralogous genes which experience subfunctionalization in their function and regulation
evolution
the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily
evolution
the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily. The open and intermediate states of ligand-free enzyme have a unique open dodecameric ring. The SpeG dodecamer is asymmetric except for the one 2fold axis and is unlike any known dodecameric structure. The SpeG dodecamer is conserved in different bacterial species, structure analysis and comparisons, overview
evolution
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the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily. The open and intermediate states of ligand-free enzyme have a unique open dodecameric ring. The SpeG dodecamer is asymmetric except for the one 2fold axis and is unlike any known dodecameric structure. The SpeG dodecamer is conserved in different bacterial species, structure analysis and comparisons, overview
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evolution
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the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily
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malfunction

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altered expression of SAT1 in the polyamine stress response, across multiple brain regions between control individuals and depressed individuals who have died by suicide, overview
malfunction
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SSAT overexpression may be linked to the rare X-linked disease keratosis follicularis spinulosa decalvans
malfunction
acetylation of triethylenetetramine is increased in SSAT1-overexpressing mice compared with wild-type mice, but SSAT1-deficient mice metabolize TETA at the same rate as the wild-type mice, due to the activity of thialysine acetyltransferase (SSAT2)
malfunction
body weights, femur and tibia lengths and diameters, and ash weights of tibia of wild-type, SSAT overexpressing, and SSAT deficient female mice, overview. Enzyme overexpressing SSAT mice have an altered skeletal appearance with increased collagen cleavage and reduced bone strength compared to the wild-type. Engineered mice also show altered differentiation of mesenchymal stromal cells to osteoblasts. Polyamine metabolism of SSAT osteoblasts is disturbed. Osteoblasts of SSAT overexpressing mice show significantly increased SSAT enzyme activity
malfunction
enzyme inhibition also inhibits ongoing joint destruction. Enzyme inhibition or gene silencing by transfection of siRNA targeting SSAT-1 increases 5-methylcytosine levels/PMF-1 promoter methylation within 21 days
malfunction
key polyamine catabolic enzyme spermidine/spermine N1-acetyltransferase1 overexpression in HEK293T cells via adenoviral vector leads to a rapid depletion of spermidine and spermine, arrest in cell growth and a decline in cell viability. AdSAT1-transduced cells reveal morphological changes commonly associated with apoptosis, including cell shrinkage, nuclear fragmentation, mitochondrial alteration, vacuolization and membrane blebbing. As polyamine analogues, alpha-methylspermidine and N1,N12-dimethylspermine that are not substrates for SAT1 partially restore growth and prevent apoptosis of AdSAT1-transduced cells. Inhibition of polyamine oxidases does not restore the growth of AdSAT1-transduced cells or block apoptosis. AdSAT1-transduction causes apoptosis by an intrinsic mitochondrial pathway, release of cytochrome c from mitochondria to cytoplasm concomitant with a decrease in the mitochondrial fraction in AdSAT1-transduced cells
malfunction
SSAT1 knockdown leads to a dramatic reduction of N1-acetyylspermidine and N1-acetylspermine pools. Metabolism of 1,12-diamino-3,6,9-triazadodecane to N1-acetyl-1,12-diamino-3,6,9-triazadodecane is reduced with SSAT1 but not with SSAT2 shRNA. No metabolism of 1,12-diamino-3,6,9-triazadodecane detectable in SSAT1-KO cells. In wild-type cells, SSAT2 knockdown does not reduce the metabolism of 1,12-diamino-3,6,9-triazadodecane to N1-AcSpmTrien. In fact it leads to the induction of SSAT1 activity and increased metabolism of 1,12-diamino-3,6,9-triazadodecane to N1-acetyl-1,12-diamino-3,6,9-triazadodecane
malfunction
the enzyme is underexpressed in brains from suicide victims compared to controls
malfunction
enzyme knockout mice develop late-onset obesity on a high-fat diet with impaired cold-induced beige adipocyte biogenesis and energy expenditure
malfunction
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body weights, femur and tibia lengths and diameters, and ash weights of tibia of wild-type, SSAT overexpressing, and SSAT deficient female mice, overview. Enzyme overexpressing SSAT mice have an altered skeletal appearance with increased collagen cleavage and reduced bone strength compared to the wild-type. Engineered mice also show altered differentiation of mesenchymal stromal cells to osteoblasts. Polyamine metabolism of SSAT osteoblasts is disturbed. Osteoblasts of SSAT overexpressing mice show significantly increased SSAT enzyme activity
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metabolism

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role of SSAT in polyamine metabolism, overview
metabolism
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role of SSAT in polyamine metabolism, overview
metabolism
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role of SSAT in polyamine metabolism, overview
metabolism
SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway
metabolism
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SSAT is a key enzyme of polyamine catabolism
metabolism
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SSAT is the key enzyme in the catabolism of polyamines, and is turned over rapidly with only a low amount of enzyme present in the cell. Analogue-affected regulation of SSAT expression occurrs, mainly, after transcription. Depleted intracellular spermidine and spermine levels inversely correlate with the SSAT activity
metabolism
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SSAT is the rate-limiting enzyme of polyamine catabolism
metabolism
acetylation of triethylenetetramine is increased in SSAT1-overexpressing mice compared with wild-type mice, but SSAT1-deficient mice metabolize TETA at the same rate as the wild-type mice, due to the activity of thialysine acetyltransferase (SSAT2)
metabolism
spermidine/spermine N1-acetyltransferase 1 is a key enzyme in the polyamine interconversion pathway, which maintains polyamine homeostasis
metabolism
spermidine/spermine N1-acetyltransferase 1 is a key enzyme in the polyamine interconversion pathway, which maintains polyamine homeostasis
metabolism
the enzyme is involved in regulation of polyamine levels in bacteria during pathogenesis
metabolism
the enzyme acetylates and thus neutralizes toxic polyamines
metabolism
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the enzyme is involved in regulation of polyamine levels in bacteria during pathogenesis
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physiological function

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SAT1 is the rate-limiting enzyme involved in catabolism of the polyamines spermidine and spermine
physiological function
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SSAT regulates cellular polyamine content and links polyamine metabolism to lipid and carbohydrate metabolism by means of alterations in the content of acetyl-CoA and ATP. Since polyamines play critical roles in normal and neoplastic growth and in ion channel regulation, SSAT is a key enzyme in these processes. A high level of SSAT stimulates flux through the polyamine biosynthetic pathway
physiological function
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SSAT regulates cellular polyamine content and links polyamine metabolism to lipid and carbohydrate metabolism by means of alterations in the content of acetyl-CoA and ATP. Since polyamines play critical roles in normal and neoplastic growth and in ion channel regulation, SSAT is a key enzyme in these processes. A high level of SSAT stimulates flux through the polyamine biosynthetic pathway
physiological function
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SSAT regulates cellular polyamine content and links polyamine metabolism to lipid and carbohydrate metabolism by means of alterations in the content of acetyl-CoA and ATP. Since polyamines play critical roles in normal and neoplastic growth and in ion channel regulation, SSAT is a key enzyme in these processes. A high level of SSAT stimulates flux through the polyamine biosynthetic pathway
physiological function
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compared with wild-typet mice, the enzyme-deficient mice subjected to endotoxic acute kidney injury have less severe kidney damage as indicated by better preservation of kidney function. Animals treated with MDL72527, an inhibitor of both polyamine oxidase and spermine oxidase, show significant protection against endotoxin-induced acute kidney injury. Increased polyamine catabolism may contribute to kidney damage through generation of by-products of polyamine oxidation
physiological function
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silencing the expression of alternative mRNA splice variant SSATX with small interfering RNA leads to increased enzymic activity. Transfection of enzyme-deficient cells with mutated SSAT gene which produces only trace amounts of alternative mRNA splice variant SSATX yields higher enzyme activity than transfection with the natural gene which produces both SSAT and SSATX. Blocking nonsense-mediated mRNA decay in vivo by protein synthesis inhibitor cycloheximide results in accumulation of SSATX mRNA, and like in cell culture, the increase of SSATX mRNA is prevented by administration of polyamine analog N1,N11-diethylnorspermine. Although SSATX/total SSAT mRNA ratio does not correlate with polyamine levels or SSAT activity between different tissues, increasing polyamine levels by methylspermidine or zink sulfate in a given tissue leads to decreased SSATX/total SSAT mRNA ratio and vice versa
physiological function
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a key enzyme that transfers the acetyl group from acetyl-CoA to either the N-1 or N-8 position of spermidine, thereby reducing the intracellular polyamine level
physiological function
enzyme SpeG has an allosteric polyamine-binding site and acetylating polyamines regulate their intracellular concentrations