EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.3.1.286 | acetyl-cytochrome c + NAD+ + H2O |
the enzyme does not deacetylate native acetyl-cytochrome c but does deacetylate the heat-denatured substrate |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | acetyl-poly-L-lysine + NAD+ + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | fluorogenic acetyl-L-lysine + NAD+ + H2O |
- |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | 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 |
? |
- |
? |
2.3.1.286 | 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 |
? |
- |
? |
2.3.1.286 | more |
no activity with the crotonylated histone H3 peptide QTAR(N6-crotonyl)KSTGG |
Homo sapiens |
? |
- |
? |
2.3.1.286 | more |
no activity with the succinylated histone H3 peptide QTAR(N6-succinyl)KSTGG |
Homo sapiens |
? |
- |
? |
2.3.1.286 | more |
Sirt3 has almost no activity against acetylated cytochrome c |
Homo sapiens |
? |
- |
? |
2.3.1.286 | more |
the enzyme is specific for acetyl-lysine within proteins. It does not deacetylate small polycations such as acetyl-spermine or acetyl-protamine or acetylated amino termini of proteins. Furthermore, the enzyme displays conformational rather than sequence specificity, preferentially deacetylating acetyl-lysine within unstructured regions of proteins |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.286 | more |
the enzyme preferentially hydrolyzes medium and long chain fatty acyl lysine. The deacetylase activity of the enzyme is weak |
Plasmodium falciparum |
? |
- |
? |