EC Number |
General Information |
Reference |
---|
4.1.3.24 | 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 |
4.1.3.24 | metabolism |
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 |
4.1.3.24 | metabolism |
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 |
4.1.3.24 | 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 |
4.1.3.24 | 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 |
4.1.3.24 | physiological function |
the enzyme from Rhodobacter sphaeroides is involved in the ethylmalonyl-CoA pathway for acetate assimilation |
727258 |
4.1.3.24 | physiological function |
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus |
-, 727258 |