Literature summary for 2.3.1.57 extracted from

Bewley, M.C.; Graziano, V.; Jiang, J.; Matz, E.; Studier, F.W.; Pegg, A.E.; Coleman, C.S.; Flanagan, J.M.
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target (2006), Proc. Natl. Acad. Sci. USA, 103, 2063-2068.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
precipitation with polyethylene glycol, high resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA, spermine, and the inhibitor N1,N11-bis-(ethyl)-norspermine	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
N1,N11-bis-(ethyl)-norspermine	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	selfacetylation of Lys26 in the presence of acetyl-cCoA and in absence of substrate	Homo sapiens

Subunits

Subunits	Comment	Organism
dimer	two dimer conformations are observed: a symmetric form with two open surface channels capable of binding substrate or cofactor, and an asymmetric form in which only one of the surface channels appears capable of binding and acetylating polyamines	Homo sapiens

Synonyms

Synonyms	Comment	Organism
spermidine/spermine N1-acetyltransferase	-	Homo sapiens
SSAT	-	Homo sapiens

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Release 2023.1 (January 2023)