Spermidine/spermine N-acetyltransferase

From Proteopedia

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{{STRUCTURE_2jev| PDB=2jev | SIZE=400| SCENE= |right|CAPTION=Human SSAT1 complex with CoA and spermine, [[2jev]] }}
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{{STRUCTURE_2jev| PDB=2jev | SIZE=400| SCENE= |right|CAPTION=Human SSAT1 dimer complex with acetyl-spermine-S-CoA, [[2jev]] }}
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Revision as of 10:33, 15 November 2012

Template:STRUCTURE 2jev

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. 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.

3D structures of SSAT

2q4v, 2bei – hSSAT2 – human
2f5i, 2b5g, 2g3t – hSSAT1
2b3u – hSSAT1 (mutant)

SSAT complexes

2b3v - hSSAT1 (mutant) + acetyl-CoA
2fxf - hSSAT1 + acetyl-CoA
2b4b - hSSAT1 (mutant) + BE3 + CoA
2b4d, 2b58, 3bj7 - hSSAT1 + CoA
2jev - hSSAT1 + acetylspermine-S-CoA
3bj8 - hSSAT1 + spermine + CoA

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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