Acetyl CoA carboxylase (ACC) Activity Assay Kit (Enzymatic method) , 100T/96S

Acetyl-CoA Carboxylase (ACC) is a critical biotin-dependent enzyme that sits at the crossroads of lipid metabolism, playing an irreplaceable role in biological systems. Its core biological function is to catalyze the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA—a reaction that serves as the rate-limiting step in de novo fatty acid synthesis, making it a key regulator of lipid biosynthesis and energy homeostasis.

The structural and functional characteristics of ACC vary across different organisms, adapting to their unique metabolic needs:

In most prokaryotes, as well as in the chloroplasts of plants and algae, ACC exists as a multi-subunit enzyme complex, where distinct subunits work together to drive the carboxylation reaction.
In eukaryotes, ACC takes the form of a large, multi-domain enzyme localized in the endoplasmic reticulum. Each domain of this enzyme is specialized for specific functions, such as biotin binding, carboxylation catalysis, and regulatory interactions, ensuring efficient and precise control of its activity.

The activity of ACC is tightly regulated through multiple layers of mechanisms to maintain metabolic balance:

Transcriptional and translational control: Long-term regulation occurs at the gene expression level, where factors like nutrient availability, hormonal signals (e.g., insulin and glucagon), and cellular energy status modulate the synthesis of ACC proteins. For example, in times of high nutrient intake, insulin promotes the transcription of ACC genes, increasing enzyme levels to support fatty acid synthesis.
Covalent modification: Short-term regulation is primarily achieved through phosphorylation and dephosphorylation of specific serine residues on the ACC protein. Kinases (e.g., AMP-activated protein kinase, AMPK) phosphorylate ACC under conditions of energy stress (e.g., low ATP levels), inhibiting its activity and shifting metabolism toward energy production. Conversely, phosphatases dephosphorylate ACC, restoring its activity to promote fatty acid synthesis.
Allosteric regulation: Small molecules act as allosteric modulators to fine-tune ACC activity. Citrate, a key intermediate in the tricarboxylic acid (TCA) cycle, binds to ACC and activates it, signaling abundant energy and carbon sources to drive fatty acid synthesis. In contrast, palmitoyl-CoA, the end product of fatty acid synthesis, acts as a feedback inhibitor, preventing excessive accumulation of lipids.

Given its central role in lipid metabolism, measuring ACC activity is of great significance in various research fields:

Metabolic disease research: Abnormal ACC activity is closely associated with metabolic disorders such as obesity, type 2 diabetes, and non-alcoholic fatty liver disease (NAFLD). For instance, overactivation of ACC in the liver leads to excessive fatty acid synthesis and accumulation, contributing to the development of NAFLD. By quantifying ACC activity, researchers can gain insights into the pathogenesis of these diseases and identify potential therapeutic targets.
Lipid biosynthesis studies: In plant and microbial research, ACC activity determines the rate of fatty acid synthesis and the accumulation of oils. Studying ACC activity helps optimize strategies for enhancing oil production in crops (e.g., soybeans, rapeseed) or microbial systems (e.g., yeast) for industrial applications like biofuel production.
Drug discovery: ACC has emerged as a promising therapeutic target for metabolic diseases. Inhibitors of ACC are being developed to reduce fatty acid synthesis and treat conditions such as NAFLD and hypertriglyceridemia. Accurate measurement of ACC activity is essential for screening and evaluating the efficacy of these potential drug candidates.

Our Acetyl CoA Carboxylase (ACC) Activity Assay Kit (Enzymatic Method) is designed to specifically detect and quantify ACC activity in biological samples. Based on the enzymatic reaction principle, the kit measures the production of inorganic phosphorus (a byproduct of the ACC-catalyzed reaction: acetyl-CoA + ATP + HCO₃⁻ → malonyl-CoA + ADP + Pi) to calculate ACC activity. This method ensures high specificity and reliability, providing researchers with a powerful tool to advance their studies in lipid metabolism and related fields.