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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-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
?
-
-
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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additional information
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the enzyme transforms polyamines into putrescine
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additional information
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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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additional information
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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
physiological function
polyamines (agmatine, putrescine, spermine and spermidine) are ubiquitous molecules involved in cell growth and differentiation. They modulate neurotransmission and are responsible for the polyamine mediated stress response, a cascade of molecular events transiently activated by acute stress stimuli. Chronic stress can lead to a hyperactivation of the polyamine system, ultimately leading to cell growth inhibition and cell death. Spermidine/spermine N1-acetyltranserare 1 is the key regulator of cellular polyamine content and is involved in the catabolism of spermidine and spermine, a key step in the maintenance of polyamine homeostasis
physiological function
spermidine/spermine N1-acetyltransferase is a catabolic regulator of polyamines, ubiquitous molecules essential for cell proliferation and differentiation. Role of polyamine metabolism in bone remodeling
physiological function
Ssat1b and Ssat1c might not only be a polyamine metabolic enzyme but also simultaneously respond to polyamine levels and engage in cross-talk with other signaling pathways. They interact with a mammalian specific integrin alpha9 and Hif-1alpha, a key regulator of oxygen homeostasis in all metazoans
physiological function
the enzyme catalyzes the initial step in the degradation of polyamines and is a critical enzyme for determining the polyamine concentrations in bacteria
physiological function
the enzyme maintains polyamine homeostasis, mammalian Ssat1 is also involved in many physiological and pathological events such as hypoxia, cell migration, and carcinogenesis
physiological function
the enzyme is involved in the negative control of sporulation and degradative enzyme production
physiological function
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depletion of polyamines by the enzyme significantly inhibits cell proliferation, migration and invasion through AKT/GSK3beta/beta-catenin signaling pathway in hepatocellular carcinoma and colorectal cancer cells. The enzyme inhibits cell colony formation and proliferation rate in hepatocellular and colorectal carcinoma cells
physiological function
enzyme activation plays a key role in cold and beta3-adrenergic receptor agonist-induced beige adipocyte biogenesis and low-grade inflammation. Enzyme activation enhances hydrogen peroxide production in adipocytes. Adipose enzyme regulates beige adipocyte thermogenesis
physiological function
the enzyme is a modulator of Escherichia coli transcription through its ability to interact with the transcription factor RcsB. The enzyme interacts with the DNA-binding domain of RcsB and this interaction might be responsible for enzyme-dependent inhibition of RcsB-dependent small RNA rprA transcription
physiological function
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the enzyme plays a critical role in cell growth
physiological function
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the enzyme regulates the genes MELK and EZH2 by direct interaction with chromatin
physiological function
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the enzyme restricts chikungunya virus and Zika virus replication. The enzyme depletes spermidine and spermine to restrict RNA virus replication
physiological function
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spermidine/spermine N1-acetyltransferase is a catabolic regulator of polyamines, ubiquitous molecules essential for cell proliferation and differentiation. Role of polyamine metabolism in bone remodeling
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physiological function
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enzyme SpeG has an allosteric polyamine-binding site and acetylating polyamines regulate their intracellular concentrations
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physiological function
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the enzyme catalyzes the initial step in the degradation of polyamines and is a critical enzyme for determining the polyamine concentrations in bacteria
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additional information
enzyme SpeG forms dodecamers in solution and in crystals, three-dimensional structure in several ligand-free and liganded structures, the enzyme occurs in open and closed conformations, overview. Conserved residue Tyr134 is proposed to function as the general acid to protonate the thiolate anion of CoA after transfer of the acetyl group to the substrate
additional information
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enzyme SpeG forms dodecamers in solution and in crystals, three-dimensional structure in several ligand-free and liganded structures, the enzyme occurs in open and closed conformations, overview. Conserved residue Tyr134 is proposed to function as the general acid to protonate the thiolate anion of CoA after transfer of the acetyl group to the substrate
additional information
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enzyme SpeG forms dodecamers in solution and in crystals, three-dimensional structure in several ligand-free and liganded structures, the enzyme occurs in open and closed conformations, overview. Conserved residue Tyr134 is proposed to function as the general acid to protonate the thiolate anion of CoA after transfer of the acetyl group to the substrate
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Haywood, G.W.; Large, P.J.
The occurrence, subcellular localization and partial purification of diamine acetyltransferase in the yeast Candida boidinii grown on spermidine or putrescine as sole nitrogen source
Eur. J. Biochem.
148
277-283
1985
[Candida] boidinii, [Candida] methanosorbosa, Trichosporon melibiosaceum, [Candida] methanosorbosa CBS 6853, [Candida] boidinii CBS 5777, Trichosporon melibiosaceum CBS 6087
brenda
Della Ragione, F.; Pegg, A.E.
Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver
Biochemistry
21
6152-6158
1982
Rattus norvegicus
brenda
Della Ragione, F.; Pegg, A.E.
Spermidine N1-acetyltransferase
Methods Enzymol.
94
321-325
1983
Rattus norvegicus
brenda
Wittich, R.M.; Walter, R.D.
A novel type of putrescine (diamine)-acetylating enzyme from the nematode Ascaris suum
Biochem. J.
260
265-269
1989
Ascaris suum
brenda
Wittich, R.M.; Walter, R.D.
Putrescine N-acetyltransferase in Onchocerca volvulus and Ascaris suum, an enzyme which is involved in polyamine degradation and release of N-acetylputrescine
Mol. Biochem. Parasitol.
38
13-18
1990
Ascaris suum, Onchocerca volvulus
brenda
Seiler, N.; Al-Therib, J.
Acetyl-CoA:1,4-diaminobutane N-acetyltransferase. Occurence in vertebrate organs and subcellular localization
Biochim. Biophys. Acta
354
206-212
1974
Rattus norvegicus
brenda
Quick, D.M.; Wallace, H.M.
Induction of spermidine/spermine N1-acetyltransferase in human breast carcinoma cells. A possible role for calcium
Biochem. Pharmacol.
46
969-974
1993
Homo sapiens
brenda
Parry, L.; Lopez-Ballester, J.; Wiest, L.; Pegg, A.E.
Effect of expression of human spermidine/spermine N1-acetyltransferase in Escherichia coli
Biochemistry
34
2701-2709
1995
Homo sapiens
brenda
Ignatenko, N.A.; Fish, J.L.; Shassetz, L.R.; Woolridge, D.P.; Gerner, E.W.
Expression of the human spermidine/spermine N1-acetyltransferase in spermidine acetylation-deficient Escherichia coli
Biochem. J.
319
435-440
1996
Homo sapiens
-
brenda
Gerner, E.W.; Kurtts, T.A.; Fuller, D.J.M.; Casero, R.A., Jr.
Stress induction of the spermidine/spermine N1-acetyltransferase by a post-transcriptional mechanism in mammalian cells
Biochem. J.
294
491-495
1993
Cricetulus griseus, Homo sapiens
-
brenda
Vujcic, S.; Halmekyto, M.; Diegelman, P.; Gan, G.; Kramer, D.L.; Janne, J.; Porter, C.W.
Effects of conditional overexpression of spermidine/spermine N1-acetyltransferase on polyamine pool dynamics, cell growth, and sensitivity to polyamine analogs
J. Biol. Chem.
275
38319-38328
2000
Homo sapiens, Mus musculus
brenda
Alhonen, L.; Karppinen, A.; Uusi-Oukari, M.; Vujcic, S.; Korhonen, V.P.; Halmekyt, M.; Kramer, D.L.; Hines, R.; Jnne, J.; Porter, C.W.
Correlation of polyamine and growth responses to N1,N11-diethylnorspermine in primary fetal fibroblasts derived from transgenic mice overexpressing spermidine/spermine N1-acetyltransferase
J. Biol. Chem.
273
1964-1969
1998
Mus musculus
brenda
Coleman, C.S.; Pegg, A.E.
Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation
Biochem. J.
358
137-145
2001
Homo sapiens
brenda
Bras, A.P.M.; Jnne, J.; Porter, C.W.; Sitar, D.S.
Spermidine/spermine N1-acetyltransferase catalyzes amantadine acetylation
Drug Metab. Dispos.
29
676-680
2001
Mus musculus
brenda
Turchanowa, L.; Dauletbaev, N.; Milovic, V.; Stein, J.
Nonsteroidal anti-inflammatory drugs stimulate spermidine/spermine acetyltransferase and deplete polyamine content in colon cancer cells
Eur. J. Clin. Invest.
31
887-893
2001
Homo sapiens
brenda
Chen, Y.; Vujcic, S.; Liang, P.; Diegelman, P.; Kramer, D.L.; Porter, C.W.
Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase
Biochem. J.
373
661-667
2003
Homo sapiens (P21673), Homo sapiens (Q96F10), Homo sapiens
brenda
Tucker, J.M.; Murphy, J.T.; Kisiel, N.; Diegelman, P.; Barbour, K.W.; Davis, C.; Medda, M.; Alhonen, L.; Janne, J.; Kramer, D.L.; Porter, C.W.; Berger, F.G.
Potent modulation of intestinal tumorigenesis in Apcmin/+ mice by the polyamine catabolic enzyme spermidine/spermine N1-acetyltransferase
Cancer Res.
65
5390-5398
2005
Mus musculus
brenda
Aubel, C.; Chabanon, H.; Carraro, V.; Wallace, H.M.; Brachet, P.
Expression of spermidine/spermine N1-acetyltransferase in HeLa cells is regulated by amino acid sufficiency
Int. J. Biochem. Cell Biol.
35
1388-1398
2003
Homo sapiens
brenda
McCloskey, D.E.; Pegg, A.E.
Properties of the spermidine/spermine N1-acetyltransferase mutant L156F that decreases cellular sensitivity to the polyamine analogue N1,N11-bis(ethyl)norspermine
J. Biol. Chem.
278
13881-13887
2003
Cricetulus griseus
brenda
Pietila, M.; Pirinen, E.; Keskitalo, S.; Juutinen, S.; Pasonen-Seppanen, S.; Keinanen, T.; Alhonen, L.; Janne, J.
Disturbed keratinocyte differentiation in transgenic mice and organotypic keratinocyte cultures as a result of spermidine/spermine N-acetyltransferase overexpression
J. Invest. Dermatol.
124
596-601
2005
Mus musculus
brenda
Zahedi, K.; Bissler, J.J.; Wang, Z.; Josyula, A.; Lu, L.; Diegelman, P.; Kisiel, N.; Porter, C.W.; Soleimani, M.
Spermidine/spermine N1-acetyltransferase overexpression in kidney epithelial cells disrupts polyamine homeostasis, leads to DNA damage, and causes G2 arrest
Am. J. Physiol. Cell Physiol.
292
C1204-C1215
2007
Homo sapiens
brenda
Babbar, N.; Gerner, E.W.; Casero, R.A.
Induction of spermidine/spermine N1-acetyltransferase (SSAT) by aspirin in Caco-2 colon cancer cells
Biochem. J.
394
317-324
2006
Homo sapiens
brenda
Vogel, N.L.; Boeke, M.; Ashburner, B.P.
Spermidine/spermine N1-acetyltransferase 2 (SSAT2) functions as a coactivator for NF-kappaB and cooperates with CBP and P/CAF to enhance NF-kappaB-dependent transcription
Biochim. Biophys. Acta
1759
470-477
2006
Homo sapiens
brenda
Marverti, G.; Giuseppina Monti, M.; Pegg, A.E.; McCloskey, D.E.; Bettuzzi, S.; Ligabue, A.; Caporali, A.; DArca, D.; Moruzzi, M.S.
Spermidine/spermine N1-acetyltransferase transient overexpression restores sensitivity of resistant human ovarian cancer cells to N1,N12-bis(ethyl)spermine and to cisplatin
Carcinogenesis
26
1677-1686
2005
Homo sapiens
brenda
Forouhar, F.; Lee, I.S.; Vujcic, J.; Vujcic, S.; Shen, J.; Vorobiev, S.M.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Porter, C.W.; Tong, L.
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase
J. Biol. Chem.
280
40328-40336
2005
Bacillus subtilis
brenda
Babbar, N.; Hacker, A.; Huang, Y.; Casero, R.A.
Tumor necrosis factor alpha induces spermidine/spermine N1-acetyltransferase through nuclear factor kappaB in non-small cell lung cancer cells
J. Biol. Chem.
281
24182-24192
2006
Homo sapiens
brenda
Jell, J.; Merali, S.; Hensen, M.L.; Mazurchuk, R.; Spernyak, J.A.; Diegelman, P.; Kisiel, N.D.; Barrero, C.; Deeb, K.K.; Alhonen, L.; Patel, M.S.; Porter, C.W.
Genetically altered expression of spermidine/spermine N1-acetyltransferase affects fat metabolism in mice via acetyl-CoA
J. Biol. Chem.
282
8404-8413
2007
Mus musculus
brenda
Yarlett, N.; Wu, G.; Waters, W.R.; Harp, J.A.; Wannemuehler, M.J.; Morada, M.; Athanasopoulos, D.; Martinez, M.P.; Upton, S.J.; Marton, L.J.; Frydman, B.J.
Cryptosporidium parvum spermidine/spermine N1-acetyltransferase exhibits different characteristics from the host enzyme
Mol. Biochem. Parasitol.
152
170-180
2007
Cryptosporidium parvum
brenda
Allen, W.L.; McLean, E.G.; Boyer, J.; McCulla, A.; Wilson, P.M.; Coyle, V.; Longley, D.B.; Casero, R.A.; Johnston, P.G.
The role of spermidine/spermine N1-acetyltransferase in determining response to chemotherapeutic agents in colorectal cancer cells
Mol. Cancer Ther.
6
128-137
2007
Homo sapiens
brenda
Bewley, M.C.; Graziano, V.; Jiang, J.; Matz, E.; Studier, F.W.; Pegg, A.E.; Coleman, C.S.; Flanagan, J.M.
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target
Proc. Natl. Acad. Sci. USA
103
2063-2068
2006
Homo sapiens
brenda
Hyvoenen, M.T.; Uimari, A.; Keinaenen, T.A.; Heikkinen, S.; Pellinen, R.; Wahlfors, T.; Korhonen, A.; Naervaenen, A.; Wahlfors, J.; Alhonen, L.; Jaenne, J.
Polyamine-regulated unproductive splicing and translation of spermidine/spermine N1-acetyltransferase
RNA
12
1569-1582
2006
Mus musculus
brenda
Hegde, S.S.; Chandler, J.; Vetting, M.W.; Yu, M.; Blanchard, J.S.
Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase
Biochemistry
46
7187-7195
2007
Homo sapiens (P21673), Homo sapiens
brenda
Wang, X.; Feith, D.J.; Welsh, P.; Coleman, C.S.; Lopez, C.; Woster, P.M.; OBrien, T.G.; Pegg, A.E.
Studies of the mechanism by which increased spermidine/spermine N1-acetyltransferase activity increases susceptibility to skin carcinogenesis
Carcinogenesis
28
2404-2411
2007
Mus musculus (P48026), Mus musculus
brenda
Butcher, N.J.; Broadhurst, G.M.; Minchin, R.F.
Polyamine-dependent regulation of spermidine-spermine N1-acetyltransferase mRNA translation
J. Biol. Chem.
282
28530-28539
2007
Homo sapiens
brenda
Baek, J.H.; Liu, Y.V.; McDonald, K.R.; Wesley, J.B.; Zhang, H.; Semenza, G.L.
Spermidine/spermine N(1)-acetyltransferase-1 binds to hypoxia-inducible factor-1alpha (HIF-1alpha) and RACK1 and promotes ubiquitination and degradation of HIF-1alpha
J. Biol. Chem.
282
33358-33366
2007
Homo sapiens (P21673)
brenda
Simonian, A.; Khomutov, A.; Hyvonen, T.; Grigorenko, N.; Keinanen, T.; Vepsalainen, J.; Alhonen, L.; Janne, J.
Novel CoA-polyamine conjugates for effective inhibition of spermine/spermidine-N1-acetyltransferase
Nucleosides Nucleotides Nucleic Acids
26
1245-1248
2007
Homo sapiens (P21673)
brenda
Klempan, T.; Rujescu, D.; Mérette, C.; Himmelman, C.; Sequeira, A.; Canetti, L.; Fiori, L.; Schneider, B.; Bureau, A.; Turecki, G.
Profiling brain expression of the spermidine/spermine N1-acetyltransferase 1 (SAT1) gene in suicide
Am. J. Med. Genet. B Neuropsychiatr. Genet.
150
934-943
2009
Homo sapiens
brenda
Pegg, A.
Spermidine/spermine-N1-acetyltransferase: A key metabolic regulator
Am. J. Physiol. Endocrinol. Metab.
294
995-1010
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Takao, K.; Miyatake, S.; Fukazawa, K.; Wada, M.; Sugita, Y.; Shirahata, A.
Measurement of spermidine/spermine-N1-acetyltransferase activity by high-performance liquid chromatography with N1-dansylnorspermine as the substrate
Anal. Biochem.
376
277-279
2008
Rattus norvegicus
brenda
Uimari, A.; Keinaenen, T.A.; Karppinen, A.; Woster, P.; Uimari, P.; Jaenne, J.; Alhonen, L.
Spermine analogue-regulated expression of spermidine/spermine N1-acetyltransferase and its effects on depletion of intracellular polyamine pools in mouse fetal fibroblasts
Biochem. J.
422
101-109
2009
Mus musculus
brenda
Montemayor, E.J.; Hoffman, D.W.
The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis
Biochemistry
47
9145-9153
2008
Mus musculus (P48026)
brenda
Fiori, L.M.; Mechawar, N.; Turecki, G.
Identification and characterization of spermidine/spermine N1-acetyltransferase promoter variants in suicide completers
Biol. Psychiatry
66
460-467
2009
Homo sapiens
brenda
Liu, B.; Sun, H.; Wang, W.; Li, W.; Yan, Y.F.; Chen, S.M.; Yang, Y.P.; Xu, C.X.; Xin, J.X.; Liu, X.X.
Adenovirus vector-mediated upregulation of spermidine /spermine N1-acetyltransferase impairs human gastric cancer growth in vitro and in vivo
Cancer Sci.
100
2126-2132
2009
Homo sapiens
brenda
Holst, C.; Nevsten, P.; Johansson, F.; Carlemalm, E.; Oredsson, S.
Subcellular distribution of spermidine/spermine N1-acetyltransferase
Cell Biol. Int.
32
39-47
2008
Homo sapiens
brenda
Marverti, G.; Ligabue, A.; Guerrieri, D.; Paglietti, G.; Piras, S.; Costi, M.P.; Farina, D.; Frassineti, C.; Monti, M.G.; Moruzzi, M.S.
Spermidine/spermine N1-acetyltranferase modulation by novel folate cycle inhibitors in cisplatin-sensitive and -resistant human ovarian cancer cell lines
Gynecol. Oncol.
117
202-210
2009
Homo sapiens
brenda
Kramer, D.; Diegelman, P.; Jell, J.; Vujcic, S.; Merali, S.; Porter, C.
Polyamine acetylation modulates polyamine metabolic flux, a prelude to broader metabolic consequences
J. Biol. Chem.
283
4241-4251
2008
Homo sapiens
brenda
Sun, H.; Liu, B.; Wang, W.; Jiang, G.S.; Li, W.; Yang, Y.P.; Xu, C.X.; Yan, Y.F.; Liu, X.X.
Adenovirus-mediated expression of spermidine/spermine N1-acetyltransferase gene induces S-phase arrest in human colorectal cancer cells
Oncol. Rep.
20
1229-1235
2008
Homo sapiens
brenda
Stanic, I.; Facchini, A.; Borzi, R.; Stefanelli, C.; Flamigni, F.
The polyamine analogue N1,N11-diethylnorspermine can induce chondrocyte apoptosis independently of its ability to alter metabolism and levels of natural polyamines
J. Cell. Physiol.
219
109-116
2009
Homo sapiens
brenda
Zahedi, K.; Barone, S.L.; Xu, J.; Steinbergs, N.; Schuster, R.; Lentsch, A.B.; Amlal, H.; Wang, J.; Casero, R.A.; Soleimani, M.
Hepatocyte-specific ablation of spermine/spermidine-N1-acetyltransferase gene reduces the severity of CCl4-induced acute liver injury
Am. J. Physiol. Gastrointest. Liver Physiol.
303
G546-G560
2012
Mus musculus
brenda
Hyvoenen, M.T.; Uimari, A.; Vepsaelaeinen, J.; Khomutov, A.R.; Keinaenen, T.A.; Alhonen, L.
Tissue-specific alternative splicing of spermidine/spermine N1-acetyltransferase
Amino Acids
42
485-493
2012
Mus musculus
brenda
Lin, H.J.; Lien, Y.C.; Hsu, C.H.
A high-throughput colorimetric assay to characterize the enzyme kinetic and cellular activity of spermidine/spermine N1-acetyltransferase 1
Anal. Biochem.
407
226-232
2010
Danio rerio (Q6GQM2), Danio rerio
brenda
Lee, S.B.; Park, J.H.; Folk, J.E.; Deck, J.A.; Pegg, A.E.; Sokabe, M.; Fraser, C.S.; Park, M.H.
Inactivation of eukaryotic initiation factor 5A (eIF5A) by specific acetylation of its hypusine residue by spermidine/spermine acetyltransferase 1 (SSAT1)
Biochem. J.
433
205-213
2011
Homo sapiens (P21673)
brenda
Zhang, Y.; Zhou, J.; Chang, M.; Bai, L.; Shan, J.; Yao, C.; Jiang, R.; Guo, L.; Zhang, R.; Wu, J.; Li, Y.
Characterization of and functional evidence for Ste27 of Streptomyces sp. 139 as a novel spermine/spermidine acetyltransferase
Biochem. J.
443
727-734
2012
Streptomyces sp. (D2CFQ9)
brenda
Niiyama, M.; Sugiyama, S.; Hirose, M.; Ishikawa, S.; Tomitori, H.; Higashi, K.; Yamashita, T.; Adachi, H.; Takano, K.; Murakami, S.; Murata, M.; Inoue, T.; Mori, Y.; Kashiwagi, K.; Matsumura, H.; Igarashi, K.
Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli
Acta Crystallogr. Sect. F
69
884-887
2013
Escherichia coli
brenda
Neidhart, M.; Karouzakis, E.; Juengel, A.; Gay, R.E.; Gay, S.
Inhibition of spermidine/spermine N1-acetyltransferase activity: a new therapeutic concept in rheumatoid arthritis
Arthritis Rheumatol.
66
1723-1733
2014
Homo sapiens (P21673), Homo sapiens
brenda
Mandal, S.; Mandal, A.; Park, M.H.
Depletion of the polyamines spermidine and spermine by overexpression of spermidine/spermine N1-acetyltransferase 1 (SAT1) leads to mitochondria-mediated apoptosis in mammalian cells
Biochem. J.
468
435-447
2015
Homo sapiens (P21673)
brenda
Weigand, S.; Filippova, E.V.; Kiryukhina, O.; Anderson, W.F.
Small angle X-ray scattering data and structure factor fitting for the study of the quaternary structure of the spermidine N-acetyltransferase SpeG
Data Brief
6
47-52
2016
Escherichia coli (P0A951)
brenda
Hyvoenen, M.; Weisell, J.; Khomutov, A.; Alhonen, L.; Vepsaelaeinen, J.; Keinaenen, T.
Metabolism of triethylenetetramine and 1,12-diamino-3,6,9-triazadodecane by the spermidine/spermine-N1-acetyltransferase and thialysine acetyltransferase
Drug Metab. Dispos.
41
30-32
2013
Homo sapiens (P21673), Homo sapiens, Mus musculus (P48026)
brenda
Squassina, A.; Manchia, M.; Chillotti, C.; Deiana, V.; Congiu, D.; Paribello, F.; Roncada, P.; Soggiu, A.; Piras, C.; Urbani, A.; Robertson, G.S.; Keddy, P.; Turecki, G.; Rouleau, G.A.; Alda, M.; Del Zompo, M.
Differential effect of lithium on spermidine/spermine N1-acetyltransferase expression in suicidal behaviour
Int. J. Neuropsychopharmacol.
16
2209-2218
2013
Homo sapiens (P21673)
brenda
Filippova, E.V.; Kuhn, M.L.; Osipiuk, J.; Kiryukhina, O.; Joachimiak, A.; Ballicora, M.A.; Anderson, W.F.
A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure
J. Mol. Biol.
427
1316-1334
2015
Vibrio cholerae (Q9KL03), Vibrio cholerae, Vibrio cholerae N16961 (Q9KL03)
brenda
Filippova, E.V.; Weigand, S.; Osipiuk, J.; Kiryukhina, O.; Joachimiak, A.; Anderson, W.F.
Substrate-induced allosteric change in the quaternary structure of the spermidine N-acetyltransferase SpeG
J. Mol. Biol.
427
3538-3553
2015
Vibrio cholerae (Q9KL03), Vibrio cholerae, Vibrio cholerae N16961 (Q9KL03)
brenda
Lien, Y.C.; Ou, T.Y.; Lin, Y.T.; Kuo, P.C.; Lin, H.J.
Duplication and diversification of the spermidine/spermine N1-acetyltransferase 1 genes in zebrafish
PLoS ONE
8
e54017
2013
Homo sapiens (P21673), Homo sapiens, Danio rerio (Q6GQM2), Danio rerio
brenda
Keinanen, T.; Hyvonen, T.; Vepsalainen, J.; Alhonen, L.; Khomutov, A.; Janne, J.
Stable analogues of coenzyme-substrate complex of spermidine/spermine-N 1-acetyltransferase reaction. Synthesis and interaction with the enzyme
Russ. J. Bioorg. Chem.
40
155-161
2014
Homo sapiens (P21673)
-
brenda
Pirnes-Karhu, S.; Maeaettae, J.; Finnilae, M.; Alhonen, L.; Uimari, A.
Overexpression of spermidine/spermine N1-acetyltransferase impairs osteoblastogenesis and alters mouse bone phenotype
Transgenic Res.
24
253-265
2015
Mus musculus (P48026), Mus musculus, Mus musculus C57BL/6JOlaHsd (P48026)
brenda
Filippova, E.; Shuvalova, L.; Minasov, G.; Kiryukhina, O.; Zhang, Y.; Clancy, S.; Radhakrishnan, I.; Joachimiak, A.; Anderson, W.
Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production
Proteins
79
2566-2577
2011
Thermoplasma acidophilum (Q9HL57), Thermoplasma acidophilum
brenda
Filippova, E.V.; Weigand, S.; Kiryukhina, O.; Wolfe, A.J.; Anderson, W.F.
Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli
Acta Crystallogr. Sect. D
75
545-553
2019
Escherichia coli (P0A951), Escherichia coli
brenda
Mounce, B.C.; Poirier, E.Z.; Passoni, G.; Simon-Loriere, E.; Cesaro, T.; Prot, M.; Stapleford, K.A.; Moratorio, G.; Sakuntabhai, A.; Levraud, J.P.; Vignuzzi, M.
Interferon-induced spermidine-spermine acetyltransferase and polyamine depletion restrict Zika and chikungunya viruses
Cell Host Microbe
20
167-177
2016
Homo sapiens
brenda
Maksymiuk, A.W.; Sitar, D.S.; Ahmed, R.; Cheng, B.; Bach, H.; Bagchi, R.A.; Aroutiounova, N.; Tappia, P.S.; Ramjiawan, B.
Spermidine/spermine N1-acetyltransferase-1 as a diagnostic biomarker in human cancer
Future Sci. OA
4
FSO345
2018
Homo sapiens
brenda
Sugiyama, S.; Ishikawa, S.; Tomitori, H.; Niiyama, M.; Hirose, M.; Miyazaki, Y.; Higashi, K.; Murata, M.; Adachi, H.; Takano, K.; Murakami, S.; Inoue, T.; Mori, Y.; Kashiwagi, K.; Igarashi, K.; Matsumura, H.
Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase
Int. J. Biochem. Cell Biol.
76
87-97
2016
Escherichia coli (A0A0M3KKU5), Escherichia coli, Escherichia coli LY180 (A0A0M3KKU5)
brenda
Kobayashi, K.; Kubo, Y.; Horii, Y.; Nishiwaki, T.; Kamiyama, S.; Sone, H.; Watanabe, S.
Bacterial degradation of spermine and expression of spermidine/spermine acetyltransferase in Bacillus subtilis (natto) under liquid cultivation
J. Gen. Appl. Microbiol.
63
373-376
2017
Bacillus subtilis subsp. natto (D4FZ53), Bacillus subtilis subsp. natto BEST195 (D4FZ53)
brenda
Yuan, F.; Zhang, L.; Cao, Y.; Gao, W.; Zhao, C.; Fang, Y.; Zahedi, K.; Soleimani, M.; Lu, X.; Fang, Z.; Yang, Q.
Spermidine/spermine N1-acetyltransferase-mediated polyamine catabolism regulates beige adipocyte biogenesis
Metab. Clin. Exp.
85
298-304
2018
Mus musculus (P48026)
brenda
Li, B.; Maezato, Y.; Kim, S.H.; Kurihara, S.; Liang, J.; Michael, A.J.
Polyamine-independent growth and biofilm formation, and functional spermidine/spermine N-acetyltransferases in Staphylococcus aureus and Enterococcus faecalis
Mol. Microbiol.
111
159-175
2019
Enterococcus faecalis, Staphylococcus aureus (A0A0H2XGJ0), Staphylococcus aureus, Staphylococcus aureus USA300 (A0A0H2XGJ0)
brenda
Thakur, V.S.; Aguila, B.; Brett-Morris, A.; Creighton, C.J.; Welford, S.M.
Spermidine/spermine N1-acetyltransferase 1 is a gene-specific transcriptional regulator that drives brain tumor aggressiveness
Oncogene
38
6794-6800
2019
Homo sapiens
brenda
Wang, C.; Ruan, P.; Zhao, Y.; Li, X.; Wang, J.; Wu, X.; Liu, T.; Wang, S.; Hou, J.; Li, W.; Li, Q.; Li, J.; Dai, F.; Fang, D.; Wang, C.; Xie, S.
Spermidine/spermine N1-acetyltransferase regulates cell growth and metastasis via AKT/beta-catenin signaling pathways in hepatocellular and colorectal carcinoma cells
Oncotarget
8
1092-1109
2017
Homo sapiens
brenda
Hu, L.I.; Filippova, E.V.; Dang, J.; Pshenychnyi, S.; Ruan, J.; Kiryukhina, O.; Anderson, W.F.; Kuhn, M.L.; Wolfe, A.J.
The spermidine acetyltransferase SpeG regulates transcription of the small RNA rprA
PLoS ONE
13
e0207563
2018
Escherichia coli (P0A951), Escherichia coli
brenda