Obesity-related Enzymes
InquiryHighly Specific, Highly Pure Enzymes for Your Needs
Protheragen, as a professional obesity research company, focuses on providing high-quality enzyme products to meet the diversified needs of our clients in the field of obesity research. For example, lipase, fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MAGL), and diacylglycerol lipase (DAGL). In the obesity mechanism, lipase is involved in the lipolysis process, hydrolyzing triglycerides into free fatty acids and glycerol, products that can be absorbed and utilized as a source of energy. However, when lipase activity is too high or fat intake is too high, the accumulation of free fatty acids may lead to the development of fat accumulation and obesity.
Fig.1 Enzymes are involved in biosynthesis and degradation in vivo. (Matheson, et al., 2021)
Our company offers a comprehensive range of obesity-related enzymes designed to help clients delve deeper into the mysteries of fat metabolism and its central role in the regulation of body weight and energy balance. To elucidate the structure and function of lipases and metabolic enzymes that are critical to the obesity mechanism, we offer a range of highly efficient tools. We aim to help our clients advance their research and discoveries in a variety of fields, including nutrition, metabolic disease research, drug discovery, and basic biology, by providing a range of enzymes that are closely related to obesity research.
Lipases
Fig.2 Lipase lid structure. (Yao, et al., 2021)
Lipase belongs to the class of carboxylester hydrolases that progressively hydrolyze triglycerides into glycerol and fatty acids. Lipases are found in the tissues of fat-containing animals, plants, and microorganisms and include phosphodiesterases, sterolases, and carboxylesterases. We offer lipase from different sources and in different concentrations to meet our clients' needs.
- Lipase from Candida rugosa, ≥2 U/mg
- Lipase from porcine pancreas, Type II
- Lipase from wheat germ, Type I
Metabolic Enzymes/Proteases
Fig.3 Structure of phospholipase D. (Wang, et al., 2021)
Obesity is strongly associated with the activity and expression levels of several metabolic enzymes and proteases. Our researchers improve fat metabolism by regulating the activity and expression levels of these enzymes. Our high-quality and highly specific metabolic enzymes/proteases are an excellent choice for your obesity research.
- Phospholipase D from Streptomyces chromofuscus
- Phospholipase D from peanut
- Phosphoglycerate kinase from yeast
- Glycerol 3-phosphate oxidase from Aerococcus viridans
- Glycerol kinase from Cellulomonas sp.
Obesity-related Tool Enzymes
Fig.4 Rabbit muscle pyruvate kinase. (Swint-Kruse, et al., 2023)
The physiological and pathological processes of obesity involve the action of a variety of instrumental enzymes. The high-quality tool enzymes provided by our company play a key role in the regulation of fat metabolism, energy homeostasis, and inflammatory responses.
- Lactate oxidase from the microorganism
- Glutathione peroxidase from bovine erythrocytes
- Butyrylcholinesterase (BCHE) from horse serum
- Pyruvate kinase from the microorganism
- Pyruvate kinase (PK) from rabbit muscle
- L-Lactate dehydrogenase from the microorganism
- Lactate dehydrogenase (LDH) from bovine heart
Enzyme Substrates
Fig.5 Indoxyl acetate position forecast. (Valek, et al., 2019)
Enzyme substrates are key substances in enzyme-catalyzed reactions, and their metabolic status directly affects the onset and development of obesity. Our high-purity enzyme substrates help our clients to deeply analyze the metabolic pathways and regulatory mechanisms of obesity.
- Lipase substrate
- 4-Nitrophenyl stearate
- Fluorescein dilaurate
Applications
- Our enzymes can be used in the development and screening of enzyme inhibitors, further becoming a potential drug for the treatment of obesity and related metabolic diseases.
- Our enzymes affect the body's energy metabolism and weight control by regulating the processes of fatty acid synthesis, transport, and oxidation.
- Our enzymes can be used not only to study the mechanisms of obesity onset and progression, but are also closely related to the inflammatory response and the onset and progression of a variety of metabolic diseases.
Advantages of Us
- Our enzymes are carefully screened and optimized to ensure the best catalytic efficiency under specific conditions.
- Our enzymes have excellent stability and durability. They remain active under a variety of environmental conditions and continue to function over a long time.
- We have a professional biological research team to provide clients with professional technical support on enzyme selection and use.
Frequently Asked Questions
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Does Protheragen support the customization of special enzymes?
Sure! Our company provides a wide range of production systems to meet the needs of our clients in different areas of research.
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How are enzymes modified?
In order to improve enzyme stability, reduce antigenicity, and extend half-life, our company uses various modification methods to modify the enzyme molecular structure in order to create certain excellent properties (e.g., higher stability, no antigenicity, resistance to protease hydrolysis, etc.) that natural enzymes do not possess.
The enzyme Protheragen provides not only important tools for obesity research but also potential targets for the development of novel therapies against obesity and related metabolic diseases. Through an in-depth study of the functions and regulatory mechanisms of these enzymes, it is expected to open up new avenues for obesity treatment. Please feel free to contact us for more enzyme-related information.
References
- Matheson, J.; et al. Potential of fatty acid amide hydrolase (FAAH), monoacylglycerol lipase (MAGL), and diacylglycerol lipase (DAGL) enzymes as targets for obesity treatment: a narrative review. Pharmaceuticals. 2021, 14(12): 1316. (CC BY 4.0)
- Kumar, A.; et al. Industrial applications of fungal lipases: a review. Frontiers in Microbiology. 2023, 14: 1142536. (CC BY 4.0)
- Yao, W.; et al. A valuable product of microbial cell factories: Microbial lipase. Frontiers in Microbiology. 2021, 12: 743377. (CC BY 4.0)
- Wang, F.; et al. Crystal structure of a phospholipase D from the plant-associated bacteria Serratia plymuthica strain AS9 reveals a unique arrangement of catalytic pocket. International Journal of Molecular Sciences. 2021, 22(6): 3219. (CC BY 4.0)
- Swint-Kruse, L.; et al. PYK-SubstitutionOME: an integrated database containing allosteric coupling, ligand affinity and mutational, structural, pathological, bioinformatic and computational information about pyruvate kinase isozymes. Database. 2023, baad030. (CC BY 4.0)
- Valek, T.; et al. Indoxyl acetate as a substrate for analysis of lipase activity. International Journal of Analytical Chemistry. 2019, 8538340. (CC BY 4.0)