ACACB: A Potential Drug Target for Obesity and Diabetes (G32)

Target Name: ACACB

NCBI ID: G32

ACACB

ACACB: A Potential Drug Target for Obesity and Diabetes

Acetyl-CoA carboxylase (ACC) is a enzyme that plays a crucial role in the metabolism of fatty acids in the body. It is a key enzyme in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is responsible for producing energy in the form of ATP from the food we consume. ACC is found in all eukaryotic cells and is involved in the production of a variety of molecules, including fatty acids, ketones, and amino acids.

Recent studies have identified ACACB as a potential drug target or biomarker for various diseases, including obesity, diabetes, and neurodegenerative disorders. In this article, we will explore the biology of ACACB and its potential as a drug target.

Biochemistry

ACACB is a 26-kDa protein that consists of 235 amino acids. It is a member of the superfamily of Coa-AAS transmembrane proteins, which include enzymes involved in various cellular processes, including metabolism, neurotransmitter synthesis, and signaling.

The ACACB enzyme has a single substrate, acetyl-CoA, which is a key intermediate step in the citric acid cycle. The catalytic center of the ACACB enzyme consists of a substrate-binding site, a catalytic domain, and a carboxylic acid-binding site.

Substrate binding

The ACACB enzyme has a specific substrate requirement, which is acetyl-CoA. This substrate is held by a unique aromatic ring structure, which is the only portion of the protein that is involved in substrate binding. The aromatic ring is a hydrophobic region that is able to interact with the acetyl-CoA molecule and allows the enzyme to bind to it with high affinity.

Catalytic domain

The catalytic domain of ACACB is responsible for the catalytic activity of the enzyme. It consists of a Rossmann-fold, a parallel beta-sheet, and a beta-helix. The Rossmann-fold is the site of the substrate binding and is the starting point for the catalytic cycle. The parallel beta-sheet is the extension of the Rossmann-fold and is involved in the formation of the active site. The beta-helix is a structural element that is involved in the stability and stability of the enzyme.

Carboxylic acid-binding site

The carboxylic acid-binding site is the final step in the ACACB enzyme's catalytic cycle. It is a parallel beta-sheet that is involved in the formation of the active site. The site is held by the acetyl-CoA molecule and is the substrate for the enzyme's active site catalyst.

Drug targeting

Recent studies have identified ACACB as a potential drug target for various diseases, including obesity, diabetes, and neurodegenerative disorders. The high-affinity nature of the ACACB enzyme for acetyl-CoA makes it an attractive target for drugs that are designed to inhibit the activity of the enzyme.

Obesity

Obesity is a growing public health problem that is associated with a variety of health conditions, including cardiovascular disease, diabetes, and certain cancers. Several studies have identified ACACB as a potential drug target for obesity. These studies have shown that inhibiting the activity of ACACB can lead to a decrease in the amount of acetyl-CoA produced and, in turn, a decrease in the rate of fatty acid oxidation, which is a key contributor to obesity.

Diabetes

Diabetes is a chronic metabolic disorder that is characterized by high levels of blood sugar. The production of fatty acids is a key contributor to diabetes, and recent studies have identified ACACB as a potential drug target

Protein Name: Acetyl-CoA Carboxylase Beta

Functions: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (PubMed:16854592, PubMed:19236960, PubMed:20457939, PubMed:20952656, PubMed:19900410, PubMed:26976583). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:19236960, PubMed:20457939, PubMed:20952656, PubMed:26976583). Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (By similarity). Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (By similarity)

The "ACACB Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ACACB comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets