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Literature summary for 2.3.1.286 extracted from

  • Jackson, M.D.; Schmidt, M.T.; Oppenheimer, N.J.; Denu, J.M.
    Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases (2003), J. Biol. Chem., 278, 50985-50998 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-acetylpyridine 16.8% inhibition at 30 mM Saccharomyces cerevisiae
3-bromopyridine 19.1% inhibition at 30 mM Saccharomyces cerevisiae
3-chloropyridine 9% inhibition at 30 mM Saccharomyces cerevisiae
3-fluoropyridine less than 2% inhibition at 30 mM Saccharomyces cerevisiae
3-hydroxypyridine 83.9% inhibition at 15 mM Saccharomyces cerevisiae
3-methoxypyridine 10.8% inhibition at 30 mM Saccharomyces cerevisiae
3-pyridine-carboxyaldehyde 10.6% inhibition at 30 mM Saccharomyces cerevisiae
3-Pyridinemethanol 22.5% inhibition at 30 mM Saccharomyces cerevisiae
nicotinamide noncompetitive inhibitor versus NAD+ Homo sapiens
nicotinamide noncompetitive inhibitor versus NAD+. 95% inhibition at 1.5 mM Saccharomyces cerevisiae
nicotinic acid 18.3% inhibition at 15 mM Saccharomyces cerevisiae
Pyridine 6.4% inhibition at 30 mM Saccharomyces cerevisiae
Thionicotinamide 58.3% inhibition at 15 mM Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[protein]-N6-acetyl-L-lysine + NAD+ + H2O Homo sapiens overall reaction [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O Saccharomyces cerevisiae overall reaction [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O the rates with beta-2'-deoxy-2'-fluororibo-NAD+ are about 200fold slower than the exchange rates determined with NAD+ under similar conditions Saccharomyces cerevisiae ?
-
?
KSTGGK(Ac)APRKQ + beta-2'-deoxy-2'-fluororibo-NAD+ + H2O the rates with beta-2'-deoxy-2'-fluororibo-NAD+ are about 1200fold slower than the exchange rates determined with NAD+ under similar conditions Homo sapiens ?
-
?
KSTGGK(Ac)APRKQ + NAD+ + H2O an 11-mer histone H3 peptide Homo sapiens KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?
KSTGGK(Ac)APRKQ + NAD+ + H2O an 11-mer histone H3 peptide Saccharomyces cerevisiae KSTGGKAPRKQ + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O overall reaction Homo sapiens [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O overall reaction Saccharomyces cerevisiae [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
?

Synonyms

Synonyms Comment Organism
HST2
-
Saccharomyces cerevisiae
silent information regulator 2
-
Homo sapiens
silent information regulator 2
-
Saccharomyces cerevisiae
Sir2
-
Homo sapiens
Sir2
-
Saccharomyces cerevisiae
SIRT2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens
NAD+
-
Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0339
-
nicotinamide at pH 7.5 and 37°C Homo sapiens
0.298
-
nicotinamide at pH 7.5 and 37°C Saccharomyces cerevisiae