EC Number |
General Information |
Reference |
---|
4.1.3.25 | evolution |
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases) |
727258 |
4.1.3.25 | evolution |
the itaconate degradation and detoxification pathways of Yersinia and Pseudomonas, both possessing three genes for itaconate degradation, i.e. itaconate coenzyme A (CoA) transferase, itaconyl-CoA hydratase and (S)-citramalyl-CoA lyase, encoded in the rip operon, are the result of convergent evolution |
728354 |
4.1.3.25 | metabolism |
the enzyme catalyzes the last step of the itaconate degradation pathway |
728354 |
4.1.3.25 | metabolism |
the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway |
727258 |
4.1.3.25 | metabolism |
the enzyme is involved in the catabolic pathway of itaconic acid |
-, 746855 |
4.1.3.25 | metabolism |
the enzyme is involved in the degradation of itaconate |
-, 746828 |
4.1.3.25 | metabolism |
the enzyme is involved in the itaconic acid degrading pathway in itaconic acid producing Aspergillus terreus |
-, 746855 |
4.1.3.25 | more |
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview |
727258 |
4.1.3.25 | physiological function |
the enzyme is crucial for survival of the pathogen in host macrophages |
728354 |
4.1.3.25 | physiological function |
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus |
-, 727258 |