6.2.1.13	D212betaE	site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced	693061	
6.2.1.13	D674A	site-directed mutagenesis, the mutation does not eliminate the ability of ACD to be phosphorylated from either direction, although phosphorylation by ATP is reduced	744911	
6.2.1.13	D674A	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	D674E	the variant retains about 45% activity compared to wild type enzyme	744911	
6.2.1.13	D674N	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	E213A	site-directed mutagenesis, the mutant variant is not phosphorylated by acetyl-CoA and phosphate	744911	
6.2.1.13	E213A	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	E213D	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	E213Q	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	E218A	site-directed mutagenesis, the mutant variant is not phosphorylated by acetyl-CoA and phosphate	744911	
6.2.1.13	E218alphaD	site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced	693061	
6.2.1.13	E218alphaQ	site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced	693061	
6.2.1.13	E218Dalpha	1-10% of wild-type activity	693061	
6.2.1.13	G266S	the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme	716267	
6.2.1.13	H252A	site-directed mutagenesis, alteration of His252 in EhACD effectively eliminate overall enzymatic activity as well as phosphorylation in either direction of the reaction	744911	
6.2.1.13	H252A	the variant has no detectable activity in either direction of the reaction	744911	
6.2.1.13	H257alphaD	site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit	693061	
6.2.1.13	H257Dalpha	mutant shows no activity in either direction	693061	
6.2.1.13	H533D	the variant retains about 3% activity compared to wild type enzyme	744911	
6.2.1.13	H533E	the variant retains about 1% activity compared to wild type enzyme	744911	
6.2.1.13	H533K	the variant retains about 10% activity compared to wild type enzyme	744911	
6.2.1.13	H533N	the variant retains about 5% activity compared to wild type enzyme	744911	
6.2.1.13	H533Q	the variant retains about 5% activity compared to wild type enzyme	744911	
6.2.1.13	H533R	the variant retains about 10% activity compared to wild type enzyme	744911	
6.2.1.13	H533R	the variant retains less than 25% activity compared to wild type enzyme	744911	
6.2.1.13	H71betaA	site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit	693061	
6.2.1.13	additional information	gradual ACS gene silencing (49-93%) significantly decreases the acetate flux without affecting the levels of glycolytic metabolites and ATP in trophozoites. Amoebae lacking ACS activity are unable to reestablish the acetyl-CoA/CoA ratio after an oxidative stress challenge	744414