Spermidine/spermine N-acetyltransferase

spinqualitylabelsall models Human SSAT1 dimer complex with acetyl-spermine-S-CoA, 2jev Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function 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. Spermidine/spermine N-acetyltransferase SpeG is a bacterial SSAT with a unique dodecameric structure and allosteric site. Relevance Several types of cancer are accompanied by increased level of cellular polyamine and compounds which affect SSAT activity are explored as possible anti-cancer drugs. Structural highlights The active site of SSAT contains a bisubstrate inhibitor. In catalysis, residues Tyr140 act as general acid and Glu92 as general base (colored in cyan). Water molecules are shown as red spheres. 3D structures of SSAT Spermidine/spermine N-acetyltransferase 3D structures

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Michal Harel, Alexander Berchansky, Joel L. Sussman