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Information on EC 2.3.1.286 - protein acetyllysine N-acetyltransferase and Organism(s) Thermotoga maritima and UniProt Accession Q9WYW0

for references in articles please use BRENDA:EC2.3.1.286
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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.
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Thermotoga maritima
UNIPROT: Q9WYW0
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The taxonomic range for the selected organisms is: Thermotoga maritima
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
silent information regulator 2
-
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+
[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
overall reaction
-
-
?
[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
-
-
-
?
2 KKGQSTSRHKKAcLMFKTEG + 2 NAD+ + 2 H2O
KKGQSTSRHKKLMFKTEG + 2''-O-acetyl-ADP-D-ribose + 3''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
K382azaKAc-containing p53 peptide + NAD+ + H2O
K382azaK-containing p53 peptide + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
K382KAc-containing p53 peptide + NAD+ + H2O
K382K-containing p53 peptide + 2''-O-acetyl-ADP-D-ribose + nicotinamide
show the reaction diagram
-
-
-
-
?
[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
-
overall reaction
-
-
?
[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+
[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
overall reaction
-
-
?
[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
-
-
-
?
[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
-
overall reaction
-
-
?
[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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0109
K382azaKAc-containing p53 peptide
-
at 37°C, pH not specified in the publication
-
0.0718
K382KAc-containing p53 peptide
-
at 37°C, pH not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
K382azaKAc-containing p53 peptide
-
at 37°C, pH not specified in the publication
-
0.18
K382KAc-containing p53 peptide
-
at 37°C, pH not specified in the publication
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101N
the mutation affects the deacetylation activity of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sauve, A.A.; Celic, I.; Avalos, J.; Deng, H.; Boeke, J.D.; Schramm, V.L.
Chemistry of gene silencing the mechanism of NAD+-dependent deacetylation reactions
Biochemistry
40
15456-15463
2001
Thermotoga maritima
Manually annotated by BRENDA team
Hu, P.; Wang, S.; Zhang, Y.
Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations
J. Am. Chem. Soc.
130
16721-16728
2008
Thermotoga maritima (Q9WYW0), Thermotoga maritima ATCC 43589 (Q9WYW0)
Manually annotated by BRENDA team
Dancy, B.C.; Ming, S.A.; Papazyan, R.; Jelinek, C.A.; Majumdar, A.; Sun, Y.; Dancy, B.M.; Drury, W.J.; Cotter, R.J.; Taverna, S.D.; Cole, P.A.
Azalysine analogues as probes for protein lysine deacetylation and demethylation
J. Am. Chem. Soc.
134
5138-5148
2012
Thermotoga maritima
Manually annotated by BRENDA team