The total cytosol activity of acetyl-CoA carboxylase (acetyl-CoA:CO(2) ligase (ADP), EC 6.4.1.2) in the liver is known to be 6- to 10-fold higher in genetically obese hyperglycemic mice (C57BL/6J-ob) than in nonobese mice. The results of immunochemical titrations, Ouchterlony double-diffusion analysis, and kinetic and heat inactivation studies indicated that this rise in the level of carboxylas...

The mammalian target of rapamycin (mTOR) has been shown to play a central role in regulating cell growth and metabolism. However, little is known about the function mTOR nutrient metabolism bivalve mollusks. In this study, regulation was investigated Sinonovacula constricta. First, activation assayed after starvation refeeding. Afterwards, using an activator (MHY1485) or inhibitor (rapamycin) m...

A technique is described for the non-recirculating perfusion of inguinal/abdominal mammary tissue in situ in anaesthetized lactating rats. Tissue viability was maintained, without resort to infusion of vasoactive chemicals which may also be effectors of cellular metabolism, for at least 90 min. Total tissue adenine nucleotides (per mg of DNA) were somewhat decreased in perfused relative to non-...

AccD6 (acetyl coenzyme A (CoA) carboxylase), plays an important role in mycolic acid synthesis of Mycobacterium tuberculosis (Mtb). Induced gene expression by isoniazid (isonicotinylhydrazine - INH), anti-tuberculosis drug) shows the expression of accD6. It is our interest to study the binding of activated INH with the AccD6 model using molecular docking procedures. The study predicts a primary...

Mycobacterium tuberculosis H37Ra and M. bovis BCG produce multiple methyl-branched fatty acids called mycocerosic acids, presumably from methylmalonyl coenzyme A (CoA). An acyl-CoA carboxylase was isolated from these organisms at a 30 to 50%fo yield by a purification procedure involving ammonium sulfate fractionation, gel ifitration, and affinity chromatography with a monomeric avidin-Sepharose...

The isolation of acetyl-CoA carboxylase from lactating rat mammary glands is described. A procedure was used which differs significantly from those employed by others who have isolated this enzyme from animal tissues. The purified enzyme catalyzes the carboxylation of 5.5 pmoles of acetylCoA per min per mg of protein under optimum assay conditions. Apparent K, values were determined for acetyl-...