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Results 1 - 7 of 7
EC Number General Information Commentary Reference
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24evolution 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
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24metabolism Mcl1 and Mcl2 together catalyze the apparent malate synthase activity during acetyl-CoA assimilation via the ethylmalonyl-CoA pathway. Mcl1 is a true (3S)-malyl-CoA lyase, catalyzing the Claisen condensation of acetyl-CoA with glyoxylate. Activity of the mcl1::kan mutant is not detected in cell extracts grown on succinate plus acetate. Apparent malate synthase activity is very low in cell extracts of the mcl1::kan and mcl2::kan mutants when grown on acetate or acetate plus succinate 704322
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24metabolism the enzyme belongs to a group of organisms that lack isocitrate lyase. Therefore, they are unable to use the glyoxylate bypass to assimilate acetyl-CoA or other substrates that enter central carbon metabolism at the level of acetyl-CoA. Instead, they use the ethylmalonyl-CoA pathway for the assimilation of acetyl-CoA with the bifunctional enzyme catalyzing the cleavage of beta-methylmalyl-CoA and the synthesis of malyl-CoA 727258
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24metabolism 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
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24more 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
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24physiological function the enzyme from Rhodobacter sphaeroides is involved in the ethylmalonyl-CoA pathway for acetate assimilation 727258
Show all pathways known for 4.1.3.24Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.24physiological function the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus -, 727258
Results 1 - 7 of 7