EC Number |
Protein Variants |
Reference |
---|
2.3.3.8 | D1026N |
mutant enzyme has 2% activity compared to wild-type enzyme |
757803 |
2.3.3.8 | H274A |
mutation abolishes both the catalytic activity and phosphorylation of the enzyme by ATP |
488225 |
2.3.3.8 | H305A |
inactive mutant of isoform Acl1 |
-, 736591 |
2.3.3.8 | H760A |
the turnover number of the mutant is similar to that of wild type in the absence of citrate and CoA, yet significantly less than that of wild type enzyme in the presence of both citrate and CoA |
718938 |
2.3.3.8 | H975A |
mutant enzyme has 25% activity compared to wild-type enzyme |
757803 |
2.3.3.8 | more |
decreased enzyme activity by use of antisense RNA, even plants with moderately reduced enzyme activity have a complex, bonsai phenotype with miniaturized organs, smaller cells, aberrant plastid morphology, reduced cuticular wax deposition and hyperaccumulation of starch, anthocyanin, and stress-related mRNAs in vegetative tissue. Exogenous malonate complements phenotype |
660133 |
2.3.3.8 | more |
enzyme knockout mutant leads to a significant impairment of glucose-dependent lipid synthesis and an elevation of mitochondrial membrane potential. Cells lacking ATP citrate synthase display decreased cytokine-stimulated cell proliferation. In contrast, these cells resist cell death induced by either cytokine or glucose withdrawal. The mutation significantly impairs Akt-mediated tumorigenesis in vivo |
676255 |
2.3.3.8 | more |
expression of holo-ATP citrate synthase as well as its two individual subunits in Escherichia coli. Purified recombinant subunits are able to reconstitute the holo-enzyme in vitro, with activity levels similar to that of recombinant holo-enzyme prepared from coexpressed genes. Residues of each subunit contribute to different aspects of the catalytic mechanism, so both proteins contribute to the active site |
674301 |