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Literature summary for 2.3.1.57 extracted from
- Spermidine/spermine-N1-acetyltransferase: A key metabolic regulator (2008), Am. J. Physiol. Endocrinol. Metab., 294, 995-1010.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | kainate-induced seizures increase SSAT activity | Homo sapiens |
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | SSAT may also be a useful target in diseases other than cancer | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Sat1, located on the X chromosome at Xp22.1, DNA and amino acid sequence analysis, genetic structure, overview | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| SSAT bound to a bisubstrate analogue N1-spermine-acetyl-CoA | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K87R | the mutant has a longer half-life than wild type or any of the other mutants | Rattus norvegicus |
| 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 |
| additional information | transgenic overexpression of SSAT protects from kainate and epilepsy-like seizure activity induction by pentylenetetrazol | Homo sapiens |
| S82D/T83A | inactive mutant | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km value for spermine is lower than that for N1-acetylspermine | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Homo sapiens | 5829 | - |
| mitochondrion | mitochondrial uptake may be regulated by the phosphorylation state of SSAT | Homo sapiens | 5739 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + N1-acetylspermine | Mus musculus | - |
CoA + N1,N12-diacetylspermine | - |
? |  |
| acetyl-CoA + N1-acetylspermine | Homo sapiens | - |
CoA + N1,N12-diacetylspermine | - |
? | |
| acetyl-CoA + N1-acetylspermine | Rattus norvegicus | - |
CoA + N1,N12-diacetylspermine | - |
? | |
| acetyl-CoA + spermidine | Mus musculus | - |
CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermidine | Homo sapiens | - |
CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermidine | Rattus norvegicus | - |
CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermine | Mus musculus | - |
CoA + N1-acetylspermine | - |
? | |
| acetyl-CoA + spermine | Homo sapiens | - |
CoA + N1-acetylspermine | - |
? | |
| acetyl-CoA + spermine | Rattus norvegicus | - |
CoA + N1-acetylspermine | - |
? | |
| additional information | Mus musculus | regulation of SSAT protein levels by polyamines or analogues, overview | ? | - |
? | |
| additional information | Rattus norvegicus | regulation of SSAT protein levels by polyamines or analogues, overview | ? | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
gene SAT1 | - |
| Mus musculus | - |
C57BL/6J and CD2F1 mice | - |
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | - |
Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| breast cancer cell | in breast tumors, SSAT is increased contributing to an increase in acetylated polyamines | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-CoA + N1-acetylspermine | - |
Mus musculus | CoA + N1,N12-diacetylspermine | - |
? | |
| acetyl-CoA + N1-acetylspermine | - |
Homo sapiens | CoA + N1,N12-diacetylspermine | - |
? | |
| acetyl-CoA + N1-acetylspermine | - |
Rattus norvegicus | CoA + N1,N12-diacetylspermine | - |
? | |
| acetyl-CoA + spermidine | - |
Mus musculus | CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermidine | - |
Homo sapiens | CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermidine | - |
Rattus norvegicus | CoA + N1-acetylspermidine | - |
? | |
| acetyl-CoA + spermine | - |
Mus musculus | CoA + N1-acetylspermine | - |
? | |
| acetyl-CoA + spermine | - |
Homo sapiens | CoA + N1-acetylspermine | - |
? | |
| acetyl-CoA + spermine | - |
Rattus norvegicus | CoA + N1-acetylspermine | - |
? | |
| additional information | regulation of SSAT protein levels by polyamines or analogues, overview | Mus musculus | ? | - |
? | |
| additional information | regulation of SSAT protein levels by polyamines or analogues, overview | Rattus norvegicus | ? | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | structure analysis, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family | Mus musculus |
| More | SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family | Homo sapiens |
| More | SSAT is a member of the GCN5-related N-acetyltransferase, GNAT, family | Rattus norvegicus |
| spermidine/spermine-N1-acetyltransferase | - |
Mus musculus |
| spermidine/spermine-N1-acetyltransferase | - |
Homo sapiens |
| spermidine/spermine-N1-acetyltransferase | - |
Rattus norvegicus |
| SSAT | - |
Mus musculus |
| SSAT | - |
Homo sapiens |
| SSAT | - |
Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Mus musculus | |
| acetyl-CoA | - |
Homo sapiens | |
| acetyl-CoA | - |
Rattus norvegicus | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Rattus norvegicus | the SSAT activity in carbon tetrachloride-treated rats declined rapidly after treatment with cycloheximide | down |
| 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
| General Information | Comment | Organism |
|---|---|---|
| malfunction | SSAT overexpression may be linked to the rare X-linked disease keratosis follicularis spinulosa decalvans | Homo sapiens |
| metabolism | role of SSAT in polyamine metabolism, overview | Mus musculus |
| metabolism | role of SSAT in polyamine metabolism, overview | Homo sapiens |
| metabolism | role of SSAT in polyamine metabolism, overview | Rattus norvegicus |
| 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 |
| 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 |
| 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 |
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