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Information on EC 2.3.1.57 - diamine N-acetyltransferase
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EC Tree
2.3.1.57 diamine N-acetyltransferaseIUBMB Comments
Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
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Word Map
- 2.3.1.57
- polyamine
- ornithine
- s-adenosylmethionine
- n1-acetylspermidine
-
denspm
- n1,n11-diethylnorspermine
- alpha-difluoromethylornithine
- pao
- n1,n12-bisethylspermine
-
superinduction
-
n1-acetylation
- medicine
-
malme-3m
- adometdc
- antizyme
-
bisguanylhydrazone
- analysis
- drug development
- pharmacology
The enzyme appears in viruses and cellular organisms
Synonyms
acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase, acetyltransferase, putrescine, bltD, CpSSAT, diamine acetyltransferase, More, N1-SAT, N1-spermidine/spermine acetyltransferase, N1SSAT, PaiA, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bltD
PaiA
SAT
SAT1
SpeG
spermidine acetyltransferase
spermidine N-acetyltransferase
spermidine/spermine acetyltransferase
spermidine/spermine N-acetyltransferase
spermidine/spermine N1-acetyltransferase
spermidine/spermine N1-acetyltransferase 1
spermidine/spermine-N1-acetyltransferase
SSAT
SSAT-1
SSAT1
VCA0947
additional information
spermidine/spermine N1-acetyltransferase
-
-
spermidine/spermine N1-acetyltransferase 1
-
SSAT
-
-
additional information
-
SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family
additional information
-
SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family
additional information
SSAT belongs to the GCN5-related N-acetyltransferase, GNAT, superfamily of acetyltransferases
additional information
-
SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
-
-
-
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
Trichosporon melibiosaceum
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
Glu92 functions as a catalytic base to drive an otherwise unfavorable deprotonation step at physiological pH. 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 + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
the acetylation proceeds by Bi-Bi mechanism
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
[Candida] methanosorbosa CBS 6853
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
[Candida] boidinii CBS 5777
-
acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
sequential mechanism
Trichosporon melibiosaceum CBS 6087
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:alkane-alpha,omega-diamine N-acetyltransferase
Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine.
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CAS REGISTRY NUMBER
COMMENTARY
54596-36-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 1,7-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 + beta-phenylethylamine
CoA + N-acetylphenylethylamine
-
-
-
-
?
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
-
-
-
?
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 + 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 + N1-acetylspermidine
CoA + N1,N8-diacetylspermidine
-
low affinity
-
-
?
acetyl-CoA + N1-dansylnorspermine
CoA + N1-acetyl-N1-dansylnorspermine
-
the acetylation reaction proceeds by Bi-Bi mechanism
-
-
?
acetyl-CoA + putrescine
CoA + acetylputrescine
-
breakdown of spermidine and putrescine
-
?
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
-
-
?
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
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
-
-
-
?
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
-
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
[Candida] boidinii CBS 5777
-
-
-
-
?
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 + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
preference for putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
-
preference for putrescine
-
?
acetyl-CoA + putrescine
CoA + N-acetylputrescine
Trichosporon melibiosaceum CBS 6087
-
-
-
?
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
-
-
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
-
-
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
-
-
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
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
[Candida] boidinii CBS 5777
-
-
+ N8-acetylspermidine, ratio N1 acetylspermidine:N8-acetylspermidine is 50:45
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
[Candida] boidinii CBS 5777
-
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
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
-
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
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
-
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 + 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 + 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
?
-
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
?
-
-
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
?
-
-
acetylation is a physiological response to convert excess polyamines to a physiologically inert form which is readily excreted
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
-
-
?
additional information
?
-
-
enzyme requires a substrate with the structure H2N(CH2)3NHR and acetylates the primary amino group
-
-
?
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
?
-
[Candida] boidinii CBS 5777
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + putrescine
CoA + acetylputrescine
-
breakdown of spermidine and putrescine
-
?
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
-
-
-
?
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
-
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 + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
acetyl-CoA + norspermidine
CoA + N1-acetylnorspermidine
-
-
-
?
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
-
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
-
breakdown of spermidine and putrescine, key agent in the supply of nitrogen to the cell
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
[Candida] boidinii CBS 5777
-
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
-
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
-
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
?
-
-
acetylation is a physiological response to convert excess polyamines to a physiologically inert form which is readily excreted
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
-
-
?
additional information
?
-
-
regulation of SSAT protein levels by polyamines or analogues, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
cofactor-binding site structure, overview. The beta-bulge formed by the beta4 and beta5 parallel strands is where the pantotheine moiety of AcCoA is located in the active site, characteristic for members of the GNAT superfamily. The pantothenate moiety forms hydrogen bonds with two conserved residues Ile87 and Ile89
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amantadine
-
competitively inhibits spermidine acetylation, at 10 mM: complete inhibition
N1-spermine-acetyl-CoA
bisubstrate analogue, bisubstrate inhibition patterns determined, linear, competitive inhibition against sperimidine and acetyl-CoA determined
Berenil
-
competitive with respect to putrescine, i.e. diminazene aceturate
additional information
-
folate cycle inhibitors, with quinoxaline moieties 3-methyl-7-trifluoromethyl-2(R)-[3,4,5-trimethoxyanilino]-quinoxaline or 3-piperazinilmethyl-2[4(oxymethyl)-phenoxy]quinoxaline, affect the enzyme, 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
-
additional information
synthetic peptide IVEMSTSKTGK50HGHAK modeled on the sequence of amino acids surrounding the hypusine residue K50, 50% inhibition of eIF5A acetylation at 0.05 mM
-
additional information
conjugates of symmetrical polyamines spermine , 1,12-diamino-4,9-diazadodecane and of nor-spermidine, 1,7-diamino-4-azaheptane, with coenzyme A, mimicking intermediate the coenzyme-substrate complex, are synthesized to inhibit the enzyme, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N1,N11-bis(ethyl)-norspermidine
increases SSAT activity, tumor regression analyzed in tumor-bearing transgenic mice expressing SSAT, tumor regression not enhanced by treatment with
N1,N11-bis(ethyl)norspermine
-
polyamine analogue, about 300fold activation of wild-type enzyme, 4fold activation of mutant L156F, the compound highly stabilizes the wild-type enzyme preventing it from degradation, while the effect on degradation of the mutant enzyme is smaller
N1,N11-bis-(ethyl)-norspermine
-
induces mRNA and activity of SSAT protein, translation proceeded by competition of a predicted RNA-binding protein
N1,N11-diethylnorspermine
-
polyamine analogue with clinical relevance as an experimental anticancer agent. Treatment of human C-28/I2 chondrocytes rapidly induces spermidine/spermine N1-acetyltransferase and spermine oxidase activities, and down-regulates ornithine decarboxylase. The treatment does not provoke cell death and caspase activation when given alone for 24 h, but causes a caspase-3 and -9 dependent apoptosis in chondrocytes further exposed to cycloheximide. The simultaneous addition of N1,N11-diethylnorspermine and cycloheximide rapidly increases caspase activity in C-28/I2 cells in the absence of spermidine/spermineN1-acetyltransferase and spermine oxidase induction or significant reduction of polyamine levels. Caspase activation induced by N1,N11-diethylnorspermine plus cycloheximide is not prevented by a N1-acetylpolyamine oxidase inhibitor
additional information
-
certain stresses induce enzyme by a spermidine-dependent post-transcriptional mechanism, e.g. heat shock, diethyldithiocarbamate and high levels of endogenous spermidine, alpha-difluoromethylornithine inhibits stress induction
-
additional information
-
indomethacin and excess polyamines induce SSAT activity
-
additional information
-
N1,N12-bis(ethyl)spermine is a potent inducer of enzyme in human tumor cells
-
additional information
-
enzyme is highly inducible by polyamine analogues such as N1,N12-bis(ethyl)spermine and N1,N11-bis(ethyl)norspermine, they prevent enzyme degradation via the Ub/proteasome pathway, mechanism
-
additional information
-
enzyme is induced by methylglyoxal bis(guanylhydrazone), potentiated by tetronasin or felodipine, tetronasin is also an active inducer, induction is related to the concentration of intracellular free calcium
-
additional information
-
enzyme is induced by isopropyl beta-D-thiogalactopyranoside
-
additional information
-
enzyme is induced by isopropyl beta-D-thiogalactopyranoside
-
additional information
-
N1,N11-diethylnorspermine induces SSAT mRNA and activity
-
additional information
-
certain stresses induce enzyme by a spermidine-dependent post-transcriptional mechanism, e.g. heat shock, diethyldithiocarbamate and high levels of endogenous spermidine, alpha-difluoromethylornithine inhibits stress induction
-
additional information
-
amino acid deprivation upregulates enzyme expression level of 2 different mRNA forms
-
additional information
-
N1,N11-diethylnorspermine induces SSAT activity by post-mRNA regulation
-
additional information
-
N1,N11-diethylnorspermine induces SSAT mRNA and activity
-
additional information
-
enzyme is induced by treatment with hepatotoxins, e.g. carbon tetrachloride
-
additional information
-
enzyme is induced by treatment with hepatotoxins, e.g. carbon tetrachloride
-
additional information
-
enzyme is induced by growth hormone, thioacetamide, dialkylnitrosamines, folic acid and spermidine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.106
1,12-diamino-3,6,9-triazadodecane
pH and temperature not specified in the publication
0.194
diethylenetriamine
measured at fixed saturating concentrations of acetyl-CoA
0.196
ethylenediamine
measured at fixed saturating concentrations of acetyl-CoA
0.083
triethylenetetramine
pH and temperature not specified in the publication
0.107
1,3-diaminopropane
measured at fixed saturating concentrations of acetyl-CoA
0.0038
acetyl-CoA
measured at fixed saturating concentration of spermidine
0.022
spermidine
measured at fixed saturating concentrations of acetyl-CoA
0.09
spermidine
isozyme ssat1b, pH and temperature not specified in the publication
0.182
spermidine
isozyme ssat1a, pH and temperature not specified in the publication
0.232
spermidine
isozyme ssat1c, pH and temperature not specified in the publication
0.0057
spermine
measured at fixed saturating concentrations of acetyl-CoA
0.055
spermine
isozyme ssat1a, pH and temperature not specified in the publication
0.091
spermine
isozyme ssat1b, pH and temperature not specified in the publication
0.139
spermine
isozyme ssat1c, pH and temperature not specified in the publication
additional information
additional information
no detectable activity for putrescine and cadaverine
-
additional information
additional information
-
no detectable activity for putrescine and cadaverine
-
additional information
additional information
-
Km value for spermine is lower than that for N1-acetylspermine
-
additional information
additional information
allosteric substrate binding, bireactant random steady-state kinetic mechanism
-
additional information
additional information
-
allosteric substrate binding, bireactant random steady-state kinetic mechanism
-
additional information
additional information
allosteric substrate binding, polyamine allosteric site structure, complex enzyme behavior, it exhibits sigmoidal curves and substrate inhibition, bireactant random steady-state kinetic mechanism, detailed non-linear regression kinetic analysis, overview
-
additional information
additional information
-
allosteric substrate binding, polyamine allosteric site structure, complex enzyme behavior, it exhibits sigmoidal curves and substrate inhibition, bireactant random steady-state kinetic mechanism, detailed non-linear regression kinetic analysis, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
spermidine
isozyme ssat1c, pH and temperature not specified in the publication
34.1
spermidine
isozyme ssat1b, pH and temperature not specified in the publication
122.2
spermidine
isozyme ssat1a, pH and temperature not specified in the publication
1.9
spermine
isozyme ssat1c, pH and temperature not specified in the publication
4.3
spermine
isozyme ssat1b, pH and temperature not specified in the publication
62.4
spermine
isozyme ssat1a, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
N1-spermine-acetyl-CoA
bisubstrate analogue, linear, competitive inhibition, structure of hSSAT with bound N1-spermine-acetyl-CoA determined
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000003 - 0.00008
-
activity in different clones of a transfected rat epidermal cell line expressing the enzyme
0.00007
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate putrescine
0.00008
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate N1-acetylspermine
0.00009
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate putrescine
0.0002
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate N1-acetylspermine
0.00023
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermine
0.00025
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate spermidine
0.0004
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate spermine
0.00068
recombinant HEK-293 cells expressing isozyme SSAT-2, substrate norspermidine
0.001
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate spermidine
0.0011
recombinant HEK-293 cells expressing isozyme SSAT-1, substrate norspermidine
0.0012
-
recombinant EGFP-tagged SSAT in cells in presence of N'-ethyl-N''-[(cyclopropyl)-methy]-4,8-diazaundecane
0.0058
-
recombinant EGFP-tagged SSAT in cells in presence of N'-ethyl-N''-[(cycloheptyl)methy]-4,8-diazaundecane
0.0106
-
recombinant EGFP-tagged SSAT in cells in presence of N',N''-diethylnorspermine
additional information
additional information
kinetic and mechanistic characterization, determination of bisubstrate inhibition patterns, three-dimensional structure of the recombinant human SSAT protein with bound bisubstrate inhibitor, acid/base assisted reaction catalyzed by SSAT involves a ternary complex, proposed on the base of kinetic properties, pH dependence and structure analysis
additional information
-
kinetic and mechanistic characterization, determination of bisubstrate inhibition patterns, three-dimensional structure of the recombinant human SSAT protein with bound bisubstrate inhibitor, acid/base assisted reaction catalyzed by SSAT involves a ternary complex, proposed on the base of kinetic properties, pH dependence and structure analysis
additional information
-
regulation of SSAT expression, de novo RNA and protein synthesis analyzed, two regions of the SSAT protein coding sequence involved in translational repression of SSAT in the absence of elevated polyamine levels, RNA-binding protein possibly interacting with stem-loop structures to block translation can be displaced by the polyamine analogue N1,N11-bis-(ethyl)-norspermine (DENSPM), allowing translation to proceed, 5' and 3' polyamine-responsive regions interact with each other in vivo, changes in either region result in translation in the absence of the polyamine analogue N1,N11-bis-(ethyl)-norspermine
additional information
SSAT1 inhibits hypoxia-inducible factor-1 (HIF-1alpha) through protein/protein interaction, effect of SSAT1 loss of function on HIF-1alpha protein levels and HIF-1 transcriptional activity, mutation of Arg101 impairs SSAT1-mediated HIF-1alpha degradation, SSAT1 promotes the ubiquitination of HIF-1alpha, involvement of SSAT1 and SSAT2 in alternative pathways for ubiquitination and degradation of HIF-1alpha, complementary roles in promoting O2-independent and O2-dependent degradation of HIF-1alpha
additional information
structure of polyamine fragment of the conjugate important for enzyme activity, existence of adenosine groups crucial for effective inhibition, since conjugates of D-N-pantothenylamidoethyl mercaptane family reveals low inhibitory activities, most exact mimic of the intermediate of N1-acetyltransferase reaction less active than analogue of the intermediate of N8-acetyltransferase reaction, significant contribution of the polyamine fragment into inhibition proven by lower activity
additional information
-
polyamine content in different clones of a transfected rat epidermal cell line expressing the enzyme, overview
additional information
tumor progression in transgenic mice expressing SSAT depends on elevated activity of ornithine decarboxylase (ODC) and on increased putrescine levels, strategy to modulate polyamine levels through the inhibition of ornithine decarboxylase (ODC) activity or polyamine uptake, but not via increased SSAT expression for cancer chemoprevention
additional information
-
tumor progression in transgenic mice expressing SSAT depends on elevated activity of ornithine decarboxylase (ODC) and on increased putrescine levels, strategy to modulate polyamine levels through the inhibition of ornithine decarboxylase (ODC) activity or polyamine uptake, but not via increased SSAT expression for cancer chemoprevention
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 9.1
activity monitored every 0.3 pH units, bell shaped pH activity profile, depending on ionization state of two groups with apparent pKa values of 7.27 and 8.87
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ssat1; three homologous ssat1 genes, named ssat1a, ssat1b, and ssat1c
UniProt
brenda
-
-
-
brenda
keratin 6 (K6)-spermidine/spermine N1-acetyltransferase (SSAT) transgenic mice, B6D2F2 background
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
brenda
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
brenda
-
TNFalpha can lead to the induction of NFkappaB signaling with a concomitant increase in spermidine/spermine N1-acetyltransferase expression
brenda
-
A549 and H157. TNFalpha can lead to the induction of NFkappaB signaling with a concomitant increase in spermidine/spermine N1-acetyltransferase expression
brenda
additional information
-
TNFalpha can lead to the induction of NFkappaB signaling with a concomitant increase in spermidine/spermine N1-acetyltransferase expression
brenda
-
enzyme expression in reduced in brain Brodmann areas,i.e. in BA4, BA8/9, and BA11, of suicide completers
brenda
-
in breast tumors, SSAT is increased contributing to an increase in acetylated polyamines
brenda
-
induction by aspirin and different non-steroidal anti-inflammatory drugs
brenda
synovial fibroblasts from patients with rheumatoid arthritis or osteoarthritis
brenda
-
the enzyme is inducible in response to 5-fluorouracil or oxaliplatin in parental and drugresistant HCT116 cell lines
brenda
-
activity of SSAT is increased 28fold in tetracycline-induced cells. Increase in SSAT levels in HEK-293 cells leads to depletion of polyamines and elevation in the enzymatic activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase, suggestive of a compensatory reaction to increased polyamine catabolism. Increased expression of SSAT also leads to DNA damage and G2 arrest
brenda
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
brenda
-
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
brenda
-
low ratio of splice variant SSATX to SSAT mRNA in syngenic rats
brenda
additional information
genes ssat1a, ssat1b, and ssat1c ares ubiquitously expressed in fish tissues st different levels, expression patterns, overview
brenda
additional information
-
genes ssat1a, ssat1b, and ssat1c ares ubiquitously expressed in fish tissues st different levels, expression patterns, overview
brenda
additional information
-
the enzyme is not detected in noncancerous human cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme, expressed in Escherichia coli DH5alpha, is present at a level of about 2% of the soluble protein
-
brenda
-
mitochondrial uptake may be regulated by the phosphorylation state of SSAT
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
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
-
the enzyme is a member of the Gcn5-related N-acetyltransferase superfamily
malfunction
-
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
-
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
-
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
metabolism
SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway
metabolism
-
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
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
-
the enzyme is involved in regulation of polyamine levels in bacteria during pathogenesis
physiological function
-
SAT1 is the rate-limiting enzyme involved in catabolism of the polyamines spermidine and spermine
physiological function
-
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
-
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
-
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
-
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