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Literature summary extracted from

  • Knorr, S.; Sinn, M.; Galetskiy, D.; Williams, R.; Wang, C.; Mueller, N.; Mayans, O.; Schleheck, D.; Hartig, J.
    Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate (2018), Nat. Commun., 9, 5071 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.64 in complex with glutarate, succinate, and the inhibitor N-oxalyl-glycine Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.64 (S)-2-hydroxyglutarate weak product inhibition Escherichia coli
1.14.11.64 N-oxalyl-glycine
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.64 0.1
-
 2-oxoglutarate pH 7.2, 30°C Escherichia coli
1.14.11.64 0.65
-
 Glutarate pH 7.2, 30°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.13 cytoplasmic membrane
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.13 L-2-hydroxyglutarate + a quinone Escherichia coli
-
 2-oxoglutarate + a quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.13 Escherichia coli
-
-
-
1.14.11.64 Escherichia coli P76621
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.13 Ni-NTA column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.11.64 0.053
-
 pH 7.2, 30°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.13 L-2-hydroxyglutarate + a quinone
-
 Escherichia coli 2-oxoglutarate + a quinol
-
 ?
1.1.5.13 L-2-hydroxyglutarate + menaquinone-4
-
 Escherichia coli 2-oxoglutarate + menaquinol-4
-
 ?
1.1.5.13 L-2-hydroxyglutarate + ubiquinone-1
-
 Escherichia coli 2-oxoglutarate + ubiquinol-1
-
 ?
1.14.11.64 glutarate + 2-oxoglutarate + O2
-
 Escherichia coli (S)-2-hydroxyglutarate + succinate + CO2
-
 ?
1.14.11.64 additional information no substrates: oxalate, malonate, succinate, adipate, and pimelate Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.13 L-2-hydroxyglutarate dehydrogenase
-
 Escherichia coli
1.1.5.13 L2HG dehydrogenase
-
 Escherichia coli
1.1.5.13 L2HG:quinone oxidoreductase
-
 Escherichia coli
1.1.5.13 lhgO
-
 Escherichia coli
1.14.11.64 csiD
-
 Escherichia coli
1.14.11.64 GlaH
-
 Escherichia coli
1.14.11.64 glutarate 2-hydroxylase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.13 FAD dependent on Escherichia coli

General Information

EC Number General Information Comment Organism
1.14.11.64 physiological function during catabolism of lysine to succinate, CsiD acts as an 2-oxoglutarate-dependent dioxygenase catalysing hydroxylation of glutarate to L-2-hydroxyglutarate. Repression of the pathway by CsiR is relieved upon glutarate binding. In a knockout strain, with carbon starvation and entry into the stationary phase, the intracellular concentration of glutarate accumulates to much higher levels than compared to the wild-type Escherichia coli