Requires iron(II). The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, participates in L-lysine degradation in many bacteria. It provides an alternative route for L-glutarate degradation that does not proceed via CoA-activated intermediates.
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The enzyme appears in viruses and cellular organisms
Requires iron(II). The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, participates in L-lysine degradation in many bacteria. It provides an alternative route for L-glutarate degradation that does not proceed via CoA-activated intermediates.
GntR family protein, CsiR, and LysR family protein, GcdR, regulate the catabolism of glutarate by repressing the transcription of csiD and lhgO, two key genes in the glutarate hydroxylation pathway, and by activating the transcription of gcdH and gcoT, two key genes in the glutaryl-CoA dehydrogenation pathway, respectively
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
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Enzyme Nomenclature
1.14.11.64 glutarate dioxygenase
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