Acyl coenzyme A carboxylase (acyl-CoA carboxylase) was purified from Acidianus brierleyi. The purified enzyme showed a unique subunit structure (three subunits with apparent molecular masses of 62, 59, and 20 kDa) and a molecular mass of approximately 540 kDa, indicating an alpha(4)beta(4)gamma(4) subunit structure. The optimum temperature for the enzyme was 60 to 70 degrees C, and the optimum ...

barley belongs to the poaceae which is the largest monocotyledon family. plastid single-copy gene acetyl-coa carboxylase (accase) is the first step in the biosynthesis of fatty acids and therefore, it is used to study the phylogenetic relationships, evolutionary and systematic of grasses. in this study, for the first time, phylogenetic relationship of eight species of hordeum genus from iran in...

Rat liver acetyl-CoA carboxylase has been purified to homogeneity by a new method involving polyethylene glycol precipitation, and DEAE and Sepharose 4B chromatography. The final product displays a single band on SDS polyacrylamide gel electrophoresis of estimated molecular weight 240,000. This material contains 5.5 +/- 0.3 moles of alkali-labile phosphate per subunit and has a specific activit...

A high molecular weight protein (approximately 1.5--2 x 10(6) daltons) has been found in rat liver cytosol to inhibit acetyl CoA carboxylase activity. The protein inhibitor was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography and gel filtration. The inactivation of the carboxylase is not attributable to either phosphorylation of the enzyme or to action on substrates or ...

The activity of the biotin-dependent enzyme pyruvate carboxylase from many organisms is highly regulated by the allosteric activator acetyl-CoA. A number of X-ray crystallographic structures of the native pyruvate carboxylase tetramer are now available for the enzyme from Rhizobium etli and Staphylococcus aureus. Although all of these structures show that intersubunit catalysis occurs, in the c...

The activities of two lipogenic enzymes, acetyl-CoA carboxylase and fatty acid synthase, were determined in two transplantable mammary adenocarcinomas (13762 and R3230AC) carried by non-pregnant, pregnant and lactating rats, and in mammary tissue of control animals (non-tumour-carrying) of comparable physiological states. During mammary-gland differentiation of control or tumour-carrying animal...

23 Holloway, P. J., Wong, W. W. C., Partridge, H. J., Seaman, D. and Perry, R. B. (1992) Pestic. Sci. 34, 109-118 24 Silcox, D. and Holloway, P. J. (1989) in Adjuvants and Agrochemicals (Chow, P. N. P., Grant, C. A,, Hinshalwood, A. M. and Simundsson, E., eds.), pp. 115-128, CRC Press Inc., Boca Raton, FL 25 Coret, J., Garnbonnet, B., Brabet, F. and Charnel, A. R. (1993) Pestic. Sci. 38, 201-20...

Acetyl-CoA carboxylase [acetyl-CoA-carbon dioxide ligase (ADP forming), EC 6.4.1.2] is a biotin-containing enzyme catalyzing the formation of malonyl-CoA. The tissue distribution of this enzyme was determined for leaves of C(3)- and C(4)-plants. The mesophyll tissues of the C(3)-plants Pisum sativum and Allium porrum contained 90% of the leaf acetyl-CoA carboxylase activity, with the epidermal ...