PMID:16667268

Citation	Roessler, PG (1990) Purification and Characterization of Acetyl-CoA Carboxylase from the Diatom Cyclotella cryptica. Plant Physiol. 92:73-8
Abstract	Acetyl-CoA carboxylase from the diatom Cyclotella cryptica has been purified to near homogeneity by the use of ammonium sulfate fractionation, gel filtration chromatography, and affinity chromatography with monomeric avidin-agarose. The specific activity of the final preparation was as high as 14.6 micromoles malonyl-CoA formed per milligram protein per minute, indicating a 600-fold purification. Native acetyl-CoA carboxylase has a molecular weight of approximately 740 kilodaltons and appears to be composed of four identical biotin-containing subunits. The enzyme has maximal activity at pH 8.2, but enzyme stability is greater at pH 6.5. K(m) values for MgATP, acetyl-CoA, and HCO(3)- were determined to be 65, 233, and 750 micromolar, respectively. The purified enzyme is strongly inhibited by palmitoyl-CoA, and is inhibited to a lesser extent by malonyl-CoA, ADP, and phosphate. Pyruvate stimulates enzymatic activity to a slight extent. Acetyl-CoA carboxylase from Cyclotella cryptica is not inhibited by cyclohexanedione or aryloxyphenoxypropionic acid herbicides as strongly as monocot acetyl-CoA carboxylases; 50% and 0% inhibition was observed in the presence of 23 micromolar clethodim and 100 micromolar haloxyfop, respectively.
Links	PubMed PMC1062250
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
9STRA:Q39478		GO:0003989: acetyl-CoA carboxylase activity	ECO:0000314:		F		Figure 1	complete CACAO 6267
9STRA:Q39478	enables	GO:0003989: acetyl-CoA carboxylase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

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