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Literature summary extracted from

  • Pegg, A.
    Spermidine/spermine-N1-acetyltransferase: A key metabolic regulator (2008), Am. J. Physiol. Endocrinol. Metab., 294, 995-1010.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.57 additional information kainate-induced seizures increase SSAT activity Homo sapiens

Application

EC Number Application Comment Organism
2.3.1.57 drug development SSAT may also be a useful target in diseases other than cancer Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.57 gene Sat1, located on the X chromosome at Xp22.1, DNA and amino acid sequence analysis, genetic structure, overview Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.57 SSAT bound to a bisubstrate analogue N1-spermine-acetyl-CoA Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.57 K87R the mutant has a longer half-life than wild type or any of the other mutants Rattus norvegicus
2.3.1.57 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 Mus musculus
2.3.1.57 additional information transgenic overexpression of SSAT protects from kainate and epilepsy-like seizure activity induction by pentylenetetrazol Homo sapiens
2.3.1.57 S82D/T83A inactive mutant Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.57 additional information
-
 additional information Km value for spermine is lower than that for N1-acetylspermine Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.57 cytosol
-
 Homo sapiens 5829
-
2.3.1.57 mitochondrion mitochondrial uptake may be regulated by the phosphorylation state of SSAT Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.57 acetyl-CoA + N1-acetylspermine Mus musculus
-
 CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine Homo sapiens
-
 CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine Rattus norvegicus
-
 CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermidine Mus musculus
-
 CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermidine Homo sapiens
-
 CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermidine Rattus norvegicus
-
 CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermine Mus musculus
-
 CoA + N1-acetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermine Homo sapiens
-
 CoA + N1-acetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermine Rattus norvegicus
-
 CoA + N1-acetylspermine
-
 ?
2.3.1.57 additional information Mus musculus regulation of SSAT protein levels by polyamines or analogues, overview ?
-
 ?
2.3.1.57 additional information Rattus norvegicus regulation of SSAT protein levels by polyamines or analogues, overview ?
-
 ?
2.3.1.57 additional information Homo sapiens 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.57 Homo sapiens
-
 gene SAT1
-
2.3.1.57 Mus musculus
-
 C57BL/6J and CD2F1 mice
-
2.3.1.57 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.57 phosphoprotein
-
 Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.57 breast cancer cell in breast tumors, SSAT is increased contributing to an increase in acetylated polyamines Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.57 acetyl-CoA + N1-acetylspermine
-
 Mus musculus CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine
-
 Homo sapiens CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + N1-acetylspermine
-
 Rattus norvegicus CoA + N1,N12-diacetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermidine
-
 Mus musculus CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermidine
-
 Homo sapiens CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermidine
-
 Rattus norvegicus CoA + N1-acetylspermidine
-
 ?
2.3.1.57 acetyl-CoA + spermine
-
 Mus musculus CoA + N1-acetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermine
-
 Homo sapiens CoA + N1-acetylspermine
-
 ?
2.3.1.57 acetyl-CoA + spermine
-
 Rattus norvegicus CoA + N1-acetylspermine
-
 ?
2.3.1.57 additional information regulation of SSAT protein levels by polyamines or analogues, overview Mus musculus ?
-
 ?
2.3.1.57 additional information regulation of SSAT protein levels by polyamines or analogues, overview Rattus norvegicus ?
-
 ?
2.3.1.57 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 Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.57 homodimer structure analysis, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.3.1.57 More SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family Mus musculus
2.3.1.57 More SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family Homo sapiens
2.3.1.57 More SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family Rattus norvegicus
2.3.1.57 spermidine/spermine-N1-acetyltransferase
-
 Mus musculus
2.3.1.57 spermidine/spermine-N1-acetyltransferase
-
 Homo sapiens
2.3.1.57 spermidine/spermine-N1-acetyltransferase
-
 Rattus norvegicus
2.3.1.57 SSAT
-
 Mus musculus
2.3.1.57 SSAT
-
 Homo sapiens
2.3.1.57 SSAT
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.57 acetyl-CoA
-
 Mus musculus
2.3.1.57 acetyl-CoA
-
 Homo sapiens
2.3.1.57 acetyl-CoA
-
 Rattus norvegicus

Expression

EC Number Organism Comment Expression
2.3.1.57 Rattus norvegicus the SSAT activity in carbon tetrachloride-treated rats declined rapidly after treatment with cycloheximide down
2.3.1.57 Homo sapiens treatment of some human cancer cells, such as NCI H157 human lung carcinoma cells, with polyamine analogues N1,N12-bis(ethyl)spermine or N1,N11-bis-(ethyl)norspermine leads to a very high induction of SSAT. SSAT activity is induced via a variety of other stimuli, including toxins, hormones, cytokines, nonsteroidal anti-inflammatory agents, natural products, and stress pathways, and by ischemia-reperfusion injury. Effects of increased SSAT activity include death of pancreatic cells, blockage of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans, and hair loss. Polyamine analogs such as BE-3-3-3 or BE-3-4-3 cause a huge increase in Sat1 gene expression in certain tumor cells up

General Information

EC Number General Information Comment Organism
2.3.1.57 malfunction SSAT overexpression may be linked to the rare X-linked disease keratosis follicularis spinulosa decalvans Homo sapiens
2.3.1.57 metabolism role of SSAT in polyamine metabolism, overview Mus musculus
2.3.1.57 metabolism role of SSAT in polyamine metabolism, overview Homo sapiens
2.3.1.57 metabolism role of SSAT in polyamine metabolism, overview Rattus norvegicus
2.3.1.57 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 Mus musculus
2.3.1.57 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 Homo sapiens
2.3.1.57 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 Rattus norvegicus