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EC Number
General Information
the enzyme belongs to the class I-CoA-transferases, which, typified by mitochondrial succinyl-CoA:3-oxoacid CoA-transferase, form multiple covalent adducts involving an essential glutamate residue. Arg228 is found in only AarC and several closely allied SCACT group sequences, EC 6.2.1
the nucleophilic glutamate is held at a near-ideal angle for attack as the thioester oxygen is forced into an oxyanion hole composed of Gly388 NH and CoA N2''. CoA is nearly immobile along its entire length during all stages of the enzyme reaction. Spatial and sequence conservation of key residues indicates that this mechanism is general among class I CoA-transferases, structural model for the AarC mechanism, overview. An auxiliary carboxylate binding site, located just outside the AarC catalytic pocket, contributes to the efficient recognition and conversion of the physiological carboxylate substrates. Protein conformational dynamics, overview. Arg228 has an important kinetic role in carboxylate substrate binding. Regulation of carboxylate access to the active-site glutamate, overview
physiological function
enzyme AarC is succinyl-coenzyme A:acetate CoA-transferase, which replaces succinyl-CoA synthetase in a variant citric acid cycle. This bypass appears to reduce metabolic demand for free CoA, reliance upon nucleotide pools, and the likely effect of variable cytoplasmic pH upon citric acid cycle flux
physiological function
low concentrations of succinate stimulate the anaerobic pyruvate metabolism of hydrogenosomes. A major function of succinate may be the intraorganellar shuttling of CoA from acetate to succinate as complied by acetate/succinate CoA-transferase
physiological function
the enzyme is an acetic acid resistance factor AarC that is required for acetate resistance by vinegar factory strain Acetobacter aceti 1023. The enzyme acts in a variant citric acid cycle that overoxidizes acetic acid to CO2, which then diffuses into the acidic culture medium
Results 1 - 5 of 5