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Literature summary for 2.3.1.B43 extracted from

  • 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 (2013), Mol. Cell. Proteomics, 12, 3509-3520.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.B43

Cloned(Commentary)

Cloned (Comment) Organism
wild-type enzyme and active site mutants Y92F and R95M Escherichia coli

Protein Variants

Protein Variants Comment Organism
R95M desuccinylation decreases about 100fold, deacetylation decreases about 3fold Escherichia coli
Y92F desuccinylation decreases about 42fold, deacetylation decreases about 3fold Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0147
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme Y92F Escherichia coli
0.0151
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli
0.02
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme R95M Escherichia coli
0.086
-
 [histone H3 K9 peptide]-N6-succinyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Escherichia coli ?
-
 ?
NAD+ + [histone H3 K9 peptide]-N6-acetyl-L-lysine
-
 Escherichia coli nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-acetyl-ADP-ribose
-
 ?
NAD+ + [histone H3 K9 peptide]-N6-succinyl-L-lysine
-
 Escherichia coli nicotinamide + [histone H3 K9 peptide]-L-lysine + 2'-O-succinyl-ADP-ribose
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.052
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme Y92F Escherichia coli
0.059
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme R95M Escherichia coli
0.135
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli
0.242
-
 [histone H3 K9 peptide]-N6-succinyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
malfunction CobB knockout cells show slightly increased acetylation levels and succinylation levels relative to the wild type cells Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.022
-
 [histone H3 K9 peptide]-N6-succinyl-L-lysine pH 8.0, 37°C, mutant enzyme R95M Escherichia coli
0.067
-
 [histone H3 K9 peptide]-N6-succinyl-L-lysine pH 8.0, 37°C, mutant enzyme Y92F Escherichia coli
2.8
-
 [histone H3 K9 peptide]-N6-succinyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli
3
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme R95M Escherichia coli
3.5
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, mutant enzyme Y92F Escherichia coli
8.9
-
 [histone H3 K9 peptide]-N6-acetyl-L-lysine pH 8.0, 37°C, wild-type enzyme Escherichia coli