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Literature summary for 2.3.3.16 extracted from

  • Venkat, S.; Chen, H.; McGuire, P.; Stahman, A.; Gan, Q.; Fan, C.
    Characterizing lysine acetylation of Escherichia coli type II citrate synthase (2019), FEBS J., 286, 2799-2808 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADH 0.1 M, 92% inhibition of wild-type, 25% inhibition of K283 acetylated variant, 88% inhibition of K295 acetylated variant, 7% inhibition of K168 acetylated variant Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.021
-
oxaloacetate wild-type, pH 7.8, 25°C Escherichia coli
0.023
-
oxaloacetate K283 acetylated variant, pH 7.8, 25°C Escherichia coli
0.025
-
oxaloacetate K168 acetylated variant, pH 7.8, 25°C Escherichia coli
0.032
-
acetyl-CoA K283 acetylated variant, pH 7.8, 25°C Escherichia coli
0.032
-
oxaloacetate K295 acetylated variant, pH 7.8, 25°C Escherichia coli
0.098
-
acetyl-CoA wild-type, pH 7.8, 25°C Escherichia coli
0.145
-
acetyl-CoA K168 acetylated variant, pH 7.8, 25°C Escherichia coli
0.478
-
acetyl-CoA K295 acetylated variant, pH 7.8, 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + H2O + oxaloacetate
-
Escherichia coli citrate + CoA
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
56
-
oxaloacetate K295 acetylated variant, pH 7.8, 25°C Escherichia coli
89
-
oxaloacetate K168 acetylated variant, pH 7.8, 25°C Escherichia coli
92
-
oxaloacetate wild-type, pH 7.8, 25°C Escherichia coli
114
-
oxaloacetate K283 acetylated variant, pH 7.8, 25°C Escherichia coli

General Information

General Information Comment Organism
metabolism recombinant wild-type CS has no detectable acetylation. Acetylation of lysine residues does not result in significantly different activities with that of the wild-type, except for residues K283 and K295. Acetylation at K283 increases the activity by nearly twofold, while acetylation at K295 decreased the activity by about 10fold. CS can be acetylated by acetyl-phosphate chemically, and be deacetylated by the CobB deacetylase Escherichia coli