2.3.1.57: diamine N-acetyltransferase
This is an abbreviated version!
For detailed information about diamine N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.57
-
2.3.1.57
-
polyamine
-
ornithine
-
s-adenosylmethionine
-
n1-acetylspermidine
-
denspm
-
pao
-
n1,n11-diethylnorspermine
-
n1,n12-bisethylspermine
-
alpha-difluoromethylornithine
-
analysis
-
superinduction
-
antizyme
-
drug development
-
malme-3m
-
n1-acetylation
-
gcn5-related
-
pharmacology
-
bisguanylhydrazone
-
medicine
-
adometdc
- 2.3.1.57
- polyamine
- ornithine
- s-adenosylmethionine
- n1-acetylspermidine
-
denspm
- pao
- n1,n11-diethylnorspermine
- n1,n12-bisethylspermine
- alpha-difluoromethylornithine
- analysis
-
superinduction
- antizyme
- drug development
-
malme-3m
-
n1-acetylation
-
gcn5-related
- pharmacology
-
bisguanylhydrazone
- medicine
- adometdc
Reaction
Synonyms
acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase, acetyltransferase, putrescine, bltD, CpSSAT, diamine acetyltransferase, More, N1-SAT, N1-spermidine/spermine acetyltransferase, N1SSAT, PaiA, putrescine (diamine)-acetylating enzyme, putrescine acetylase, putrescine acetyltransferase, putrescine N-acetyltransferase, SAT, SAT1, SpeG, spermidine /spermine N1-acetyltransferase, spermidine acetyltransferase, spermidine N-acetyltransferase, spermidine N1-acetyltransferase, spermidine-spermine acetyltransferase, spermidine-spermine N1-acetyltransferase, spermidine/spermine acetyltransferase, spermidine/spermine N-acetyltransferase, spermidine/spermine N1-acetyltransferase, spermidine/spermine N1-acetyltransferase 1, spermidine/spermine N1-acetyltransferase 2, spermidine/spermine N1-acetyltransferase-1, spermidine/spermine-N 1-acetyltransferase, spermidine/spermine-N1-acetyltransferase, spermidine/spermine-N1-acetyltransferase activity, SSAT, SSAT-1, SSAT-2, SSAT1, SSAT2, SSATX, Ste27, Ta0374, VCA0947
ECTree
2.3.1.57 diamine N-acetyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.1.57 - diamine N-acetyltransferase
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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
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the enzyme transforms polyamines into putrescine
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the enzyme transforms polyamines into putrescine
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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
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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
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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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enzyme plays an efficient role in maintaining polyamine pool homeostasis during challenges with exogenous polyamines
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the enzyme is involved in intestinal tumorigenesis in ApcMin/+ MIN mice, enzyme is involved in catabolism of polyamines, activation of the enzyme in vivo results in suppression of tumor outgrowth in a mouse prostate cancer model
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the enzyme is rate-limiting in polyamine catabolism
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participates in polyamine homeostasis by regulating polyamine export and catabolism. Expression status of spermidine/spermine N1-acetyltransferase alters body fat accumulation by metabolically modulating tissue acetyl- and malonyl-CoA levels, thereby influencing fatty acid biosynthesis and oxidation
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SSAT gene expression is fine-tuned by regulated unproductive splicing and translation, which is modulated by polyamine levels
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regulation of SSAT protein levels by polyamines or analogues, overview
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SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway. No activity with putrescine, cadaverine, lysine, thialysine, amantadine, substrate specificity, overview
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enzyme is involved in polyamine degradation and excretion of excessive polyamines, release of N-acetylputrescine, role in the control of polyamine concentrations
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enzyme requires a substrate with the structure H2N(CH2)3NHR and acetylates the primary amino group
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regulation of SSAT protein levels by polyamines or analogues, overview
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no substrates: glycine, glutamate, aspartate, leucine, alanine or arginine
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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
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additional information
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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
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substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
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substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
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substrate-induced allosteric change of quaternary structure of spermidine N-acetyltransferase SpeG, overview
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additional information
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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
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additional information
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not: methylamine, dimethylamine, di-n-butylamine, L-lysine, benzylamine, semicarbazide, L-serine, glyoxylate, oxaloacetate, 4-aminobenzoate, 2-aminobenzoate
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[Candida] boidinii CBS 5777
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not: methylamine, dimethylamine, di-n-butylamine, L-lysine, benzylamine, semicarbazide, L-serine, glyoxylate, oxaloacetate, 4-aminobenzoate, 2-aminobenzoate
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