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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.3.1.286
757557
Identification of novel protein lysine acetyltransferases in Escherichia coli
mBio
9
e01905-18
2018
Escherichia coli
30352934
2.3.1.286
749528
Increased expression of Drosophila Sir2 extends life span in a dose-dependent manner
Aging
5
682-691
2013
Drosophila melanogaster
24036492
2.3.1.286
751013
Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
J. Biol. Chem.
278
50985-50998
2003
Saccharomyces cerevisiae
14522996
2.3.1.286
751013
Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
J. Biol. Chem.
278
50985-50998
2003
Homo sapiens
14522996
2.3.1.286
749884
Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
Biochemistry
46
14478-14486
2007
Saccharomyces cerevisiae
18027980
2.3.1.286
749884
Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
Biochemistry
46
14478-14486
2007
Homo sapiens
18027980
2.3.1.286
749886
Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase
Biochemistry
47
10227-10239
2008
Plasmodium falciparum
18729382
2.3.1.286
749470
Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
ACS Chem. Biol.
7
155-159
2012
Plasmodium falciparum
21992006
2.3.1.286
752056
SIR proteins create compact heterochromatin fibers
Proc. Natl. Acad. Sci. USA
115
12447-12452
2018
Saccharomyces cerevisiae
30455303
2.3.1.286
750369
SIR2 the biochemical mechanism of NAD+-dependent protein deacetylation and ADP-ribosyl enzyme intermediates
Curr. Med. Chem.
11
807-826
2004
Saccharomyces cerevisiae
15078167
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