Spermidine/spermine N-acetyltransferase

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<StructureSection load='2jev' size='450' side='right' scene='48/486363/Cv/2' caption='Human SSAT1 dimer complex with acetyl-spermine-S-CoA, [[2jev]]'>
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<StructureSection load='' size='350' side='right' scene='48/486363/Cv/2' caption='Human SSAT1 dimer complex with acetyl-spermine-S-CoA, [[2jev]]'>
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__TOC__
== Function ==
== Function ==
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'''Spermidine/spermine N-acetyltransferase''' (SSAT) catalyzes the acetylation of spermidine and spermine. SSAT regulates cellular polyamine homeostasis by degrading polyamines via their acetylation. SSAT activity is regulated by polyamine concentration and various toxins, hormones and natural products<ref>PMID:18349109</ref>.
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'''Spermidine/spermine N-acetyltransferase''' (SSAT) or '''Spermidine N-acetyltransferase''' or '''diamine acetyltransferase''' catalyzes the acetylation of spermidine and spermine. SSAT regulates cellular polyamine homeostasis by degrading polyamines via their acetylation. SSAT activity is regulated by polyamine concentration and various toxins, hormones and natural products<ref>PMID:18349109</ref>.
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*'''Spermidine/spermine N-acetyltransferase SpeG''' is a bacterial SSAT with a unique dodecameric structure and allosteric site<ref>PMID:37508494</ref>.
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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The active site of SSAT contains a bisubstrate inhibitor. In catalysis, residues Tyr140 act as general acid and Glu92 as general base<ref>PMID:17516632</ref>.
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The <scene name='48/486363/Cv/7'>active site of SSAT contains a bisubstrate inhibitor</scene>. In <scene name='48/486363/Cv/8'>catalysis, residues Tyr140 act as general acid and Glu92 as general base</scene><ref>PMID:17516632</ref> (colored in cyan). Water molecules are shown as red spheres.
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</StructureSection>
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==3D structures of SSAT==
==3D structures of SSAT==
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{{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[Spermidine/spermine N-acetyltransferase 3D structures]]
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Spermidine/spermine N-acetyltransferase
 
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**[[2q4v]], [[2bei]] – hSSAT2 – human<br />
 
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**[[2f5i]], [[2b5g]], [[2g3t]] – hSSAT1<br />
 
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**[[2b3u]] – hSSAT1 (mutant)<br />
 
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**[[5cnp]] – VcSSAT – ''Vibrio cholerae''<br />
 
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**[[4r9m]] – SSAT – ''Escherichia coli''<br />
 
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*Spermidine/spermine N-acetyltransferase complexes
 
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**[[2b3v]] - hSSAT1 (mutant) + acetyl-CoA<br />
 
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**[[2fxf]] - hSSAT1 + acetyl-CoA<br />
 
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**[[2b4b]] - hSSAT1 (mutant) + BE3 + CoA<br />
 
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**[[2b4d]], [[2b58]], [[3bj7]] - hSSAT1 + CoA<br />
 
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**[[2jev]] - hSSAT1 + acetylspermine-S-CoA<br />
 
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**[[3bj8]] - hSSAT1 + spermine + CoA<br />
 
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**[[4mi4]] – VcSSAT + spermine <br />
 
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**[[4mj8]] – VcSSAT + polyamine <br />
 
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**[[4r87]] – VcSSAT + spermine + CoA <br />
 
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**[[4ncz]] – VcSSAT + sulfonate derivative<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human SSAT1 dimer complex with acetyl-spermine-S-CoA, 2jev

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Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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