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Information on EC 2.3.1.57 - diamine N-acetyltransferase and Organism(s) Mus musculus and UniProt Accession P48026
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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
- pao
- n1,n11-diethylnorspermine
- n1,n12-bisethylspermine
- alpha-difluoromethylornithine
- analysis
-
superinduction
- antizyme
- drug development
-
malme-3m
-
n1-acetylation
-
gcn5-related
- pharmacology
-
bisguanylhydrazone
- medicine
- adometdc
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
spermidine/spermine n1-acetyltransferase, spermidine n1-acetyltransferase, ssat1, ssat2, spermidine acetyltransferase, spermidine/spermine acetyltransferase, spermidine/spermine-n1-acetyltransferase, ssat-1, spermidine n-acetyltransferase, ssatx, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase
-
-
-
-
acetyltransferase, putrescine
-
-
-
-
diamine acetyltransferase
-
-
-
-
N1-SAT
-
-
-
-
N1SSAT
-
-
-
-
putrescine (diamine)-acetylating enzyme
-
-
-
-
putrescine acetylase
-
-
-
-
putrescine acetyltransferase
-
-
-
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putrescine N-acetyltransferase
-
-
-
-
spermidine acetyltransferase
-
-
-
-
spermidine N1-acetyltransferase
-
-
-
-
spermidine/spermine N1-acetyltransferase
SSAT
additional information
spermidine/spermine N1-acetyltransferase
-
-
-
-
SSAT
-
-
-
-
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
54596-36-0
-
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
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
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 + triethylenetetramine
?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
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 + 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 + spermidine
CoA + N1-acetylspermidine
-
-
-
-
?
acetyl-CoA + spermidine
CoA + N1-acetylspermidine
-
-
product is exclusively N1-acetylspermidine
?
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
?
-
-
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
-
-
?
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
3 acetyl-CoA + 2 spermine
3 CoA + N1-acetylspermine + N1,N12-diacetylspermine
-
-
-
?
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 + triethylenetetramine
?
SSAT2 is the main acetylator of TETA compared to SSAT1
-
-
?
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
-
?
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
?
-
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
amantadine
-
competitively inhibits spermidine acetylation, at 10 mM: complete inhibition
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
additional information
-
N1,N11-diethylnorspermine induces SSAT activity by post-mRNA regulation
-
additional information
-
N1,N11-diethylnorspermine induces SSAT mRNA and activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0012
-
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
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
additional information
-
polyamine content in different clones of a transfected rat epidermal cell line expressing the enzyme, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
keratin 6 (K6)-spermidine/spermine N1-acetyltransferase (SSAT) transgenic mice, B6D2F2 background
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
-
high ratio of splice variant SSATX to SSAT mRNA in syngenic rats
-
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
-
low ratio of splice variant SSATX to SSAT mRNA in syngenic rats
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
metabolism
physiological function
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 knockout mice develop late-onset obesity on a high-fat diet with impaired cold-induced beige adipocyte biogenesis and energy expenditure
metabolism
SSAT catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway
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)
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
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
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
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
physiological function
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SAT1_MOUSE
171
0
20012
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SSAT in complex with coenzyme A, with and without bound spermine, hanging drop vapor diffusion method at 4°C, crystals of the binary complex between SSAT and CoA are obtained in 20% PEG 8000, 80 mM sodium acetate, 15% glycerol, 2 mM spermine, 1 mM CoA, and 85 mM sodium cacodylate, pH 6.0, 0.001 ml of the protein solution is mixed with 0.01 ml of precipitant solution containing 20% PEG 8000, 50 mM NaCl, 2 mM spermine, 1 mM coenzyme A, 15% glycerol, and 100 mM bicine buffer, pH 9.0. Crystals are obtained at pH 5.0-6.5 over a broad range of precipitant and salt concentrations. Introduction of spermine results in displacement of CoA from the enzyme active site. X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D93N
site-directed mutagenesis, the mutation affects both substrate binding and catalysis without changing the pH dependence of the enzyme
E92Q
site-directed mutagenesis, the mutation has a detrimental effect on both substrate binding and catalysis and shifts the optimal pH for enzyme activity further into alkaline solution conditions
additional information
additional information
-
crossing of ApcMin/+ MIN mice with enzyme-overexpressing transgenic mice results in mice with a 3-6fold higher development of adenomas in the small intestine and colon compared to wild-type mice, crossing of ApcMin/+ MIN mice with SSAT-knockout mice reduces the development of adenomas by 75% in the small intestine
additional information
-
enzyme overexpression in transgenic mice leads to accumulation of purtrescine and permanent hair loss at the age of 3-weeks, because the hair follicles are exchanged for dermal cysts and epidermal utriculi due to reduced expression of terminal differentiation markers such as cytokeratins 1/10, and filaggrin, and persisting expression of basal cell cytokeratins 5/14 in the suprabasal layer, hair growth can be reactivated by reduction of putrescine content
additional information
-
construction of SSAT-deficient fetal fibroblasts transiently expressing an SSAT-EGFP construct
additional information
-
mice, which have a ubiquitous SSAT overexpression due to an increase in the Sat1 gene copy number, have decreased tumor incidence in the skin in response to a two-stage tumorigenesis protocol. Pleiotropic effects of the changes associated with widespread high levels of SSAT expression in transgenic mice with increased Sat1 gene copies. Phenotype of SSAT knockout mice, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant overexpression of the enzyme in enzyme-deficient and wild-type mice using the endogenous enzyme promoter, quantitative PCR expression analysis
expression in a rat epidermal cell line, enzyme overexpression in transgenic mice
-
full-length cDNA is cloned and expressed in Escherichia coli M15, generation of a transgenic mouse line systemically overexpressing SSAT, overexpression alters polyamine pools and sensitize cells to the antiproliferative activity of N1,N11-diethylnorspermine
-
SSAT gene is cloned, tetracyclin-regulated gene lacking the 5-flanking region is expressed in MCF-7 human breast carcinoma cells, conditional overexpression lowers polyamine pools, inhibits cell growth and enhances growth sensitivity to certain analogs
-
transient expression of EGFP-tagged SSAT in SSAT-deficient mouse fetal fibroblasts in cytosol and nucleus. The presence of SSAT-EGFP leads to a 9fold induction in SSAT activity in transfected untreated cells when compared with the cells transfected with EGFP
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both cold and beta3-adrenergic receptor agonist CL-316,243 increase the expression of the enzyme in inguinal white adipose tissue and brown adipose tissue
induction of enzyme SSAT with alpha-methylspermidine disturbs wild-type osteoblastogenesis
N',N''-diethylnorspermine, N'-ethyl-N''-[(cyclopropyl)-methy]-4,8-diazaundecane, and N'-ethyl-N''-[(cycloheptyl)methy]-4,8-diazaundecane treatments lead to high, moderate, or low induction of SSAT activity, respectively
-
spermidine/spermine N1-acetyltransferase SSAT, has an alternative mRNA splice variant SSATX which undergoes degradation via nonsense-mediated mRNA decay (NMD) pathway, and the intracellular polyamine level regulates the ratio of the SSATX and SSAT splice variants
-
SSAT mRNA expression peaks at threefold 24 h following lipopolysaccharide injection and returns to background levels by 48 h. The activity of SSAT correlates with its mRNA levels
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
tumor progression in transgenic mouse lines overexpressing SSAT protein and susceptibility to skin carcinogenesis analyzed
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
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
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)
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
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
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)
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)
EXTERNAL LINKS (specific for EC-Number 2.3.1.57)
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Release 2023.1 (January 2023)
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