acetyl CoA carboxylase

acetyl CoA carboxylase

a biotin-containing enzyme which participates in the synthesis of fatty acids by catalyzing the carboxylation reaction in which acetyl-CoA is converted to malonyl-CoA. It has the important effect of regulating the rate of fatty acid synthesis and is itself influenced in its activity by the local concentration of magnesium, citrate, palmitylcarnitine and ATP and is stimulated by the action of insulin.
References in periodicals archive ?
First, we examined whether protein restriction affected expression of acetyl CoA carboxylase (ACC), a major lipogenic enzyme.
The mRNAs encoding several yield-related enzymes including acetyl CoA carboxylase, glucosyltransferase, phosphate translocator, and lipoxygenase were reprogrammed by nucleotide solutions with concomitant changes in the accumulation of cellulosic biomass and vegetable oil in peanut [11, 12, 14].
The cDNA inserts that were used as probes were those homologous to rRNA, and to mRNAs encoding acetyl CoA carboxylase (ACC), lipoxygenase (LO), glucosyltransferase, inorganic phosphate translocator, nitrate reductase, and glycinamide ribonucleotide (GAR) synthetase/GAR transformylase.
Molecular biology of GDH-based biotechnology: Some of the GDH-synthesized RNAs that were used as probes were those homologous to mRNAs encoding glucosyltransferase, phosphate translocator [14]; acetyl CoA carboxylase (ACC), lipoxygenase (LO) [12]; probes #1 for nitrate reductase (NR) and probe #2 for glycinamide ribonucleotide transformylase/glycinamide ribonucleotide synthetases (GART/GARS) (Table 1).
Phosphorylation of both acetyl CoA carboxylase and AMP-activated protein kinase was increased, thus explaining the increase in fatty acid oxidation.
These include acetyl CoA carboxylase, the rate limiting enzyme that initiates fatty acid synthesis.
that show that the company has identified a series of novel, highly potent, and highly selective Acetyl CoA Carboxylase (ACC)1/2 allosteric inhibitors.
2004) also indicated that reduced lipogenesis in the mammary gland of lactating mice was caused by reducing acetyl CoA carboxylase activity and mRNA abundance of acetyl CoA carboxylase, the critical enzyme in de novo fatty acid synthesis, and also inhibited mammary desaturation by reducing mammary stearoyl-CoA desaturase activity and mRNA abundance.