Literature summary for 2.3.1.B43 extracted from

Schuetz, A.; Min, J.; Antoshenko, T.; Wang, C.L.; Allali-Hassani, A.; Dong, A.; Loppnau, P.; Vedadi, M.; Bochkarev, A.; Sternglanz, R.; Plotnikov, A.N.
Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin (2007), Structure, 15, 377-389.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor-diffusion method at 20°C. Crystal structures of SIRT5 in complex with ADP-ribose, and crystal structures of SIRT5 bound to suramin	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
suramin	suramin binds into the NAD+-, the product-, and the substrate-binding site	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NXA8	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NAD+ + [chicken histone]-N6-acetyl-L-lysine	chemically acetylated chicken histone. Less activity toward chemically acetylated bovine serum albumin and monoacetylated histone H4 (K16 and K8). No activity is observed with monoacetylated histone K5 and K12 histone H4 peptides	Homo sapiens	nicotinamide + [chicken histone]-L-lysine + 2'-O-acetyl-ADP-ribose	-	?

Synonyms

Synonyms	Comment	Organism
SIRT5	-	Homo sapiens

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.022	-	pH and temperature not specified in the publication	Homo sapiens	suramin

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Release 2023.1 (January 2023)