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Results 1 - 10 of 10
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25metabolism the enzyme catalyzes the last step of the itaconate degradation pathway 728354
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25metabolism 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25metabolism the enzyme is involved in the catabolic pathway of itaconic acid -, 746855
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25metabolism the enzyme is involved in the degradation of itaconate -, 746828
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25metabolism the enzyme is involved in the itaconic acid degrading pathway in itaconic acid producing Aspergillus terreus -, 746855
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25more 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25physiological function the enzyme is crucial for survival of the pathogen in host macrophages 728354
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.25physiological function the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus -, 727258
Results 1 - 10 of 10