Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28597

for references in articles please use BRENDA:EC2.3.1.286
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O28597
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sirt1, sirt3, sirtuin, sirt2, sirtuin 1, sirtuin 3, sir2p, silent information regulator 2, sir2alpha, nad-dependent histone deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD+-dependent protein deacetylase
-
-
-
-
NAD-dependent protein deacetylase
-
-
protein lysine deacetylase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2''-O-acetyl-ADP-D-ribose-forming)
The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2''-O-acetyl-ADP-D-ribose converts non-enzymically to 3''-O-acetyl-ADP-D-ribose.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
overall reaction
-
-
?
HLKSKKGQSTSRHK(K-Ac)LMFK + NAD+ + H2O
HLKSKKGQSTSRHKKLMFK + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
p53A peptide
-
-
?
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
r
KKGQSTSRHKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + nicotinamide
KKGQSTSRHKKAcLMFKTEG + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
[bovine serum albumin]-N6-acetyl-L-lysine + NAD+ + H2O
[bovine serum albumin]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
show the reaction diagram
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
overall reaction
-
-
?
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
show the reaction diagram
-
-
-
-
r
[protein]-N6-acetyl-L-lysine + NAD+
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
show the reaction diagram
-
-
-
-
?
[protein]-N6-acetyl-L-lysine + NAD+ + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O
[protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
contains zinc
Zn2+
-
the small domain of the enzyme contains a three-stranded zinc ribbon motif. No exogenous added Zn ions are needed for in vitro deacetylase and nicotinamide-NAD+ exchange activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Benzamide
-
5% inhibition at 5 mM
Isonicotinamide
-
4% inhibition at 5 mM
o-phenanthroline
-
-
Pyrazinamide
-
4% inhibition at 5 mM
Thionicotinamide
-
4% inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 0.16
nicotinamide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in a productive complex with NAD+, in a nonproductive NAD+ complex and in the unliganded state, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.4), 1.8 M ammonium sulfate, and 1% (w/v) PEG400 at 20°C
-
isoform SIR2-Af1 in complex with NAD+, hanging drop vapor diffusion method, using 100 mM MES (pH 6.0), and 12% (w/v) PEG-10K
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E186A
-
inactive
H135A
-
inactive
Q115A
-
the mutant shows very weak deacetylation activity compared to the wild type enzyme
S36A
-
inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, Mono S column chromatography, and Superdex S200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli XL1Blue cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sauve, A.A.; Schramm, V.L.
Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
Biochemistry
42
9249-9256
2003
Archaeoglobus fulgidus, Saccharomyces cerevisiae, Mus musculus
Manually annotated by BRENDA team
Min, J.; Landry, J.; Sternglanz, R.; Xu, R.M.
Crystal structure of a SIR2 homolog-NAD complex
Cell
105
269-279
2001
Archaeoglobus fulgidus
Manually annotated by BRENDA team
North, B.J.; Verdin, E.
Sirtuins Sir2-related NAD-dependent protein deacetylases
Genome Biol.
5
224
2004
Archaeoglobus fulgidus (O28597), Saccharomyces cerevisiae (P53686), Homo sapiens (Q8IXJ6), Homo sapiens, Archaeoglobus fulgidus ATCC 49558 (O28597)
Manually annotated by BRENDA team
Cen, Y.; Sauve, A.A.
Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approaches
J. Am. Chem. Soc.
132
12286-12298
2010
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Avalos, J.L.; Boeke, J.D.; Wolberger, C.
Structural basis for the mechanism and regulation of Sir2 enzymes
Mol. Cell
13
639-648
2004
Archaeoglobus fulgidus
Manually annotated by BRENDA team