Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.11.64 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)

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

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P76621
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutarate + 2-oxoglutarate + O2
-
Escherichia coli (S)-2-hydroxyglutarate + succinate + CO2
-
?
additional information no substrates: oxalate, malonate, succinate, adipate, and pimelate Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
csiD
-
Escherichia coli
GlaH
-
Escherichia coli
glutarate 2-hydroxylase
-
Escherichia coli

General Information

General Information Comment Organism
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