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Information on EC 2.3.1.B43 - protein-lysine desuccinylase (NAD+) and Organism(s) Escherichia coli and UniProt Accession P75960
for references in articles please use BRENDA:EC2.3.1.B43preliminary BRENDA-supplied EC number
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EC Tree
2.3.1.B43 protein-lysine desuccinylase (NAD+)Specify your search results
Word Map
- 2.3.1.B43
- sirtuins
- sirt3
-
deacetylation
- deacetylases
-
desuccinylation
-
malonylation
-
nad-dependent
-
sirt1-7
-
glutarylation
- diagnostics
- medicine
- drug development
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
Synonyms
sirt5, sirtuin 5, nad+-dependent protein deacetylase, nad+ dependent deacetylase, nicotinamide adenine dinucleotide-dependent protein deacetylase, sirtuin deacylase, histone desuccinylase, nad+-dependent protein deacylase, sirt5iso1, lysine desuccinylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
-
the rate of desuccinylation is 5.8fold faster than the rate of deburyrylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
-
the rate of desuccinylation is 3.8fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
-
the rate of desuccinylation is 2.3fold faster than the rate of deacetylation
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
-
-
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme can deacetylate acetyllysine independently whether the acetyl donor is acetyl-Coenzyme A or acetyl phosphate. Linear sequences alone are inadequate to predict CobB substrates and that structural analyses are necessary. CobB substrate acetyllyines appear to be located near the surface of the protein on a
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
?
additional information
?
-
-
global identification of CobB substrates using an Escherichia coli proteome microarray
-
-
?
additional information
?
-
-
the enzyme shows dual enzymatic activities to catalyze the removal of two structurally different lysine acyl groups, acetyl and succinyl, from the modified lysine residues
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + [protein]-N6-acetyl-L-lysine
nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
-
-
?
NAD+ + [N-hydroxyarylamine O-acetyltransferase]-N6-acetyl-L-lysine
nicotinamide + [N-hydroxyarylamine O-acetyltransferase]-L-lysine + 2'-O-acetyl-ADP-ribose
-
-
-
-
?
NAD+ + [RcsB protein]-N6-acetyl-L-lysine180
nicotinamide + [RcsB protein]-L-lysine180 + 2'-O-acetyl-ADP-ribose
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
-
-
?
NAD+ + [response regulator CheY]-N6-acetyl-L-lysine
nicotinamide + [response regulator CheY]-L-lysine + 2'-O-acetyl-ADP-ribose
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
-
-
?
additional information
?
-
-
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the zinc-binding domain of the sirtuin proteins may play a similar role in substrate-specific recognition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.0147
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.0151
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.02
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.242
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.052
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
0.059
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.135
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
3.5
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
8.9
[histone H3 K9 peptide]-N6-acetyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
0.022
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme R95M
-
0.067
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, mutant enzyme Y92F
-
2.8
[histone H3 K9 peptide]-N6-succinyl-L-lysine
-
pH 8.0, 37°C, wild-type enzyme
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
reversible Nepsilon-Lys acetylation of transcription factors is a mode of regulation of gene expression used by all cells
physiological function
the enzyme regulates protein function in diverse and often essential cellular processes, most notably translation. CobB is the predominate deacetylase in Escherichia coli loop or a helix that protrudes into the solution and thus in position to be an easily accessible target
malfunction
metabolism
physiological function
malfunction
-
CobB knockout cells show slightly increased acetylation levels and succinylation levels relative to the wild type cells
malfunction
-
RcsB protein isolated from a cobB deletion mutation strain is hyperacetylated
metabolism
-
overexpression of CobB reduces the 6fold glucose-dependent induction to a more modest 3fold induction
metabolism
-
sirtuin deacetylase CobB deficiency leads to both site-specific and global changes in protein acetylation stoichiometry, affecting central metabolism
metabolism
-
the Gcn5-like acetyltransferase YfiQ and the sirtuin deacetylase CobB play crucial roles in the transcription regulation of the periplasmic stress-responsive promoter cpxP when cells of Escherichia coli grow in the presence of glucose, an environment that induces protein acetylation
physiological function
-
acetylation of the response regulator RcsB controls transcription from the small RNA promoter rprA
physiological function
-
the enzyme regulates chemotaxis of Escherichia coli by deacetylating CheY
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40274) in complex with an 11-residue peptide containing residues 1219 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R95M
-
desuccinylation decreases about 100fold, deacetylation decreases about 3fold
Y92F
-
desuccinylation decreases about 42fold, deacetylation decreases about 3fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Q.F.; Gu, J.; Gong, P.; Wang, X.D.; Tu, S.; Bi, L.J.; Yu, Z.N.; Zhang, Z.P.; Cui, Z.Q.; Wei, H.P.; Tao, S.C.; Zhang, X.E.; Deng, J.Y.
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferase
FEBS J.
280
1966-1979
2013
Escherichia coli, Escherichia coli AD494
Hu, L.I.; Chi, B.K.; Kuhn, M.L.; Filippova, E.V.; Walker-Peddakotla, A.J.; Bsell, K.; Becher, D.; Anderson, W.F.; Antelmann, H.; Wolfe, A.J.
Acetylation of the response regulator RcsB controls transcription from a small RNA promoter
J. Bacteriol.
195
4174-4186
2013
Escherichia coli
Baeza, J.; Dowell, J.A.; Smallegan, M.J.; Fan, J.; Amador-Noguez, D.; Khan, Z.; Denu, J.M.
Stoichiometry of site-specific lysine acetylation in an entire proteome
J. Biol. Chem.
289
21326-21338
2014
Escherichia coli
Zhao, K.; Chai, X.; Marmorstein, R.
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
J. Mol. Biol.
337
731-741
2004
Escherichia coli (P75960), Escherichia coli
AbouElfetouh, A.; Kuhn, M.L.; Hu, L.I.; Scholle, M.D.; Sorensen, D.J.; Sahu, A.K.; Becher, D.; Antelmann, H.; Mrksich, M.; Anderson, W.F.; Gibson, B.W.; Schilling, B.; Wolfe, A.J.
The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites
Microbiologyopen
4
66-83
2015
Escherichia coli (P75960)
Colak, G.; Xie, Z.; Zhu, A.Y.; Dai, L.; Lu, Z.; Zhang, Y.; Wan, X.; Chen, Y.; Cha, Y.H.; Lin, H.; Zhao, Y.; Tan, M.
Identification of lysine succinylation substrates and the succinylation regulatory enzyme CobB in Escherichia coli
Mol. Cell. Proteomics
12
3509-3520
2013
Escherichia coli
Li, R.; Gu, J.; Chen, Y.Y.; Xiao, C.L.; Wang, L.W.; Zhang, Z.P.; Bi, L.J.; Wei, H.P.; Wang, X.D.; Deng, J.Y.; Zhang, X.E.
CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY
Mol. Microbiol.
76
1162-1174
2010
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Lima, B.P.; Antelmann, H.; Gronau, K.; Chi, B.K.; Becher, D.; Brinsmade, S.R.; Wolfe, A.J.
Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
Mol. Microbiol.
81
1190-1204
2011
Escherichia coli
Thao, S.; Chen, C.S.; Zhu, H.; Escalante-Semerena, J.C.
Nepsilon-lysine acetylation of a bacterial transcription factor inhibits its DNA-binding activity
PLoS One
5
e15123
2010
Escherichia coli (P75960)
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