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sitekebche.com serves as a valuable platform for accessing important biomedical and scientific information, particularly regarding human butyrylcholinesterase (BChE). As a critical enzyme in the human body, BChE has been widely studied for its role in various biochemical processes, including lipid metabolism and drug metabolism. For researchers and professionals in the field, understanding BChE's function, structure, and genetic variants is essential. In this article, we will explore the key features and insights from databases like UniProtKB and NCBI, as well as the latest research on BChE's roles, mutations, and inhibitors.
Overview of Butyrylcholinesterase (BChE)
Butyrylcholinesterase, also known as BCHE, is an enzyme that hydrolyzes ester bonds in certain compounds, including neurotransmitters like acetylcholine. While acetylcholinesterase (AChE) is primarily involved in neurotransmitter degradation in the central nervous system, BChE is mainly found in plasma and is involved in the hydrolysis of choline-based esters. It plays a significant role in lipid metabolism, drug detoxification, and in the breakdown of certain lipid-soluble molecules that might otherwise accumulate and pose a risk to health.
Amino Acid Sequence and Structure
The amino acid sequence of human BChE can be retrieved from the UniProtKB database under accession number P06276. The sequence provides essential information about the enzyme's structure and allows researchers to understand its functional domains and active sites. These insights are crucial for the development of targeted therapies and drug interventions that may involve the modulation of BChE activity.
Moreover, the NCBI (National Center for Biotechnology Information) database holds valuable genetic data regarding BChE, including polymorphisms, mutations, and related phenotypes. The sequence data available on these platforms serves as a foundation for both basic and clinical research into BChE’s function and its relevance in various diseases.
BChE in Lipid Metabolism: A New Outlook
Recent studies have brought new perspectives on BChE’s involvement in lipid metabolism. BChE is thought to play a role in breaking down lipids such as phospholipids, which are essential components of cell membranes. These lipids contribute significantly to various cellular processes, including signal transduction and membrane trafficking.
By hydrolyzing certain lipid substrates, BChE influences lipid signaling pathways, which may have downstream effects on metabolic disorders such as obesity, diabetes, and cardiovascular disease. While much of the focus on BChE has been on its role in neurotransmission and drug metabolism, recent evidence suggests that its role in lipid homeostasis is equally important and warrants further exploration.
This new outlook on BChE’s involvement in lipid metabolism may lead to the identification of potential therapeutic targets for diseases linked to lipid dysregulation. As the understanding of BChE expands, new interventions could be developed to modulate its activity in order to correct metabolic imbalances.
Review of Human Butyrylcholinesterase Structure and Function
A comprehensive review of the structure and function of human BChE is vital for advancing biomedical knowledge, particularly in the context of drug development and genetic research. BChE is a serine hydrolase enzyme with a complex tertiary structure that allows it to interact with a variety of substrates. Its functional domains are primarily responsible for its enzymatic activity, which involves the hydrolysis of ester bonds in molecules like acetylcholine and other choline esters.
The enzyme’s active site is composed of a serine residue, a histidine residue, and an acidic residue, which work together to facilitate the breakdown of substrates. Additionally, the glycosylation patterns on the enzyme can influence its activity and stability. Advances in structural biology, particularly through techniques like X-ray crystallography and cryogenic electron microscopy (Cryo-EM), have allowed for a more detailed understanding of BChE’s structural components.
Researchers have also focused on the variations in BChE function across different populations and how genetic differences may impact enzyme activity. These variations can help explain why certain individuals may have altered drug responses or susceptibility to diseases linked to impaired BChE function.
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