In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.
A highly branched glucan in starch.
An unbranched glucan in starch.
An enzyme that catalyzes the transfer of glucose from ADPglucose to glucose-containing polysaccharides in 1,4-alpha-linkages. EC 2.4.1.21.
An autosomal recessive metabolic disorder due to a deficiency in expression of glycogen branching enzyme 1 (alpha-1,4-glucan-6-alpha-glucosyltransferase), resulting in an accumulation of abnormal GLYCOGEN with long outer branches. Clinical features are MUSCLE HYPOTONIA and CIRRHOSIS. Death from liver disease usually occurs before age 2.
Any of a group of polysaccharides of the general formula (C6-H10-O5)n, composed of a long-chain polymer of glucose in the form of amylose and amylopectin. It is the chief storage form of energy reserve (carbohydrates) in plants.
Enzymes that catalyze the transfer of glucose from a nucleoside diphosphate glucose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
A genus of obligately aerobic, thermophilic, gram-negative bacteria in the family Crenotrichaceae. They were isolated from submarine alkaline HOT SPRINGS in Iceland.
Glycogen is a multibranched polysaccharide of glucose serving as the primary form of energy storage in animals, fungi, and bacteria, stored mainly in liver and muscle tissues. (Two sentences combined as per your request)
Glucose polymers consisting of a backbone of beta(1->3)-linked beta-D-glucopyranosyl units with beta(1->6) linked side chains of various lengths. They are a major component of the CELL WALL of organisms and of soluble DIETARY FIBER.
An enzyme that hydrolyzes 1,6-alpha-glucosidic branch linkages in glycogen, amylopectin, and their beta-limit dextrins. It is distinguished from pullulanase (EC 3.2.1.41) by its inability to attack pullulan and by the feeble action of alpha-limit dextrins. It is distinguished from amylopectin 6-glucanohydrolase (EC 3.2.1.69) by its action on glycogen. With EC 3.2.1.69, it produces the activity called "debranching enzyme". EC 3.2.1.68.
An ATP-dependent enzyme that catalyzes the addition of ADP to alpha-D-glucose 1-phosphate to form ADP-glucose and diphosphate. The reaction is the rate-limiting reaction in prokaryotic GLYCOGEN and plant STARCH biosynthesis.
Polysaccharides composed of repeating glucose units. They can consist of branched or unbranched chains in any linkages.
Serves as the glycosyl donor for formation of bacterial glycogen, amylose in green algae, and amylopectin in higher plants.
An enzyme that catalyzes the transfer of D-glucose from UDPglucose into 1,4-alpha-D-glucosyl chains. EC 2.4.1.11.
A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A group of inherited metabolic disorders involving the enzymes responsible for the synthesis and degradation of glycogen. In some patients, prominent liver involvement is presented. In others, more generalized storage of glycogen occurs, sometimes with prominent cardiac involvement.
Annual cereal grass of the family POACEAE and its edible starchy grain, rice, which is the staple food of roughly one-half of the world's population.
Polysaccharides are complex carbohydrates consisting of long, often branched chains of repeating monosaccharide units joined together by glycosidic bonds, which serve as energy storage molecules (e.g., glycogen), structural components (e.g., cellulose), and molecular recognition sites in various biological systems.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
An endocellulase with specificity for the hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans including laminarin, paramylon, and pachyman.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An exocellulase with specificity for 1,3-beta-D-glucasidic linkages. It catalyzes hydrolysis of beta-D-glucose units from the non-reducing ends of 1,3-beta-D-glucans, releasing GLUCOSE.
A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.
The threadlike, vascular projections of the chorion. Chorionic villi may be free or embedded within the DECIDUA forming the site for exchange of substances between fetal and maternal blood (PLACENTA).
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A genus of ascomycetous fungi, family Sordariaceae, order SORDARIALES, comprising bread molds. They are capable of converting tryptophan to nicotinic acid and are used extensively in genetic and enzyme research. (Dorland, 27th ed)
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

1,4-Alpha-Glucan Branching Enzyme (GBE) is an enzyme that plays a crucial role in the synthesis of glycogen, a complex carbohydrate that serves as the primary form of energy storage in animals and fungi. GBE catalyzes the transfer of a segment of a linear glucose chain (alpha-1,4 linkage) to an alpha-1,6 position on another chain, creating branches in the glucan molecule. This branching process enhances the solubility and compactness of glycogen, allowing it to be stored more efficiently within cells.

Defects in GBE are associated with a group of genetic disorders known as glycogen storage diseases type IV (GSD IV), also called Andersen's disease. This autosomal recessive disorder is characterized by the accumulation of abnormally structured glycogen in various tissues, particularly in the liver and muscles, leading to progressive liver failure, muscle weakness, cardiac complications, and sometimes neurological symptoms.

Amylopectin is a type of complex carbohydrate molecule known as a polysaccharide. It is a component of starch, which is found in plants and is a major source of energy for both humans and other animals. Amylopectin is made up of long chains of glucose molecules that are branched together in a bush-like structure.

Amylopectin is composed of two types of glucose chain branches: outer chains, which are made up of shorter, highly branched chains of glucose molecules; and inner chains, which are made up of longer, less branched chains. The branching pattern of amylopectin allows it to be digested and absorbed more slowly than other types of carbohydrates, such as simple sugars. This slower digestion and absorption can help to regulate blood sugar levels and provide sustained energy.

Amylopectin is found in a variety of plant-based foods, including grains, legumes, vegetables, and fruits. It is an important source of calories and energy for humans and other animals that consume these types of plants as part of their diet.

Amylose is a component of starch, which is a complex carbohydrate found in plants. Amylose is a long, straight chain polymer made up of thousands of glucose molecules linked together by α-1,4 glycosidic bonds. It is less abundant than the other major component of starch, amylopectin, which has branched chains due to α-1,6 glycosidic bonds.

Amylose is relatively resistant to digestion by human enzymes, making it less easily absorbed and providing a slower release of glucose into the bloodstream compared to amylopectin. This property has led to its use in some low-glycemic index foods and as a dietary supplement for people with diabetes.

In addition to its role in food, amylose has industrial applications, such as in the production of adhesives, textiles, and paper. It is also used in medical research as a material for drug delivery and tissue engineering.

Starch synthase is an enzyme involved in the synthesis of starch, which is a complex carbohydrate that serves as an important energy storage molecule in plants. Specifically, starch synthase catalyzes the transfer of glucose from activated donor molecules, such as ADP-glucose, to the non-reducing end of a growing linear chain or branch of an amylopectin molecule, resulting in the formation of starch.

There are several isoforms of starch synthase that have been identified in plants, including granule-bound starch synthase (GBSS), which is responsible for synthesizing the highly branched and crystalline amylose component of starch, and soluble starch synthases (SSI, SSII, SSIII, and SSIV), which contribute to the synthesis of the more branched and less crystalline amylopectin component.

Defects in starch synthase activity have been associated with various genetic disorders in humans, such as glycogen storage disease type II (Pompe disease) and transient infantile hyperammonemia, which are caused by mutations in the genes encoding for the enzymes involved in the synthesis of glycogen and starch, respectively.

Glycogen Storage Disease Type IV (GSD IV), also known as Andersen's disease, is a rare inherited metabolic disorder that affects the body's ability to break down glycogen, a complex carbohydrate that serves as a source of energy for the body.

In GSD IV, there is a deficiency in the enzyme called glycogen branching enzyme (GBE), which is responsible for adding branches to the glycogen molecule during its synthesis. This results in an abnormal form of glycogen that accumulates in various organs and tissues, particularly in the liver, heart, and muscles.

The accumulation of this abnormal glycogen can lead to progressive damage and failure of these organs, resulting in a variety of symptoms such as muscle weakness, hypotonia, hepatomegaly (enlarged liver), cardiomyopathy (heart muscle disease), and developmental delay. The severity of the disease can vary widely, with some individuals experiencing milder symptoms while others may have a more severe and rapidly progressing form of the disorder.

Currently, there is no cure for GSD IV, and treatment is focused on managing the symptoms and slowing down the progression of the disease. This may include providing nutritional support, addressing specific organ dysfunction, and preventing complications.

I'm happy to help! However, it seems there might be a bit of confusion here. Starch is not typically considered a medical term, but rather a nutritional and biochemical concept. Here's a brief explanation:

Starch is a complex carbohydrate that serves as the primary form of energy storage in plants. It is made up of long chains of glucose molecules and can be found in various foods such as grains, legumes, fruits, and vegetables. Amylase, an enzyme present in our saliva and digestive system, helps break down starch into simpler sugars during the digestion process so that our bodies can absorb them for energy.

I hope this clarifies any confusion! If you have any other questions or need further information on a medical topic, please don't hesitate to ask.

Glucosyltransferases (GTs) are a group of enzymes that catalyze the transfer of a glucose molecule from an activated donor to an acceptor molecule, resulting in the formation of a glycosidic bond. These enzymes play crucial roles in various biological processes, including the biosynthesis of complex carbohydrates, cell wall synthesis, and protein glycosylation. In some cases, GTs can also contribute to bacterial pathogenesis by facilitating the attachment of bacteria to host tissues through the formation of glucans, which are polymers of glucose molecules.

GTs can be classified into several families based on their sequence similarities and catalytic mechanisms. The donor substrates for GTs are typically activated sugars such as UDP-glucose, TDP-glucose, or GDP-glucose, which serve as the source of the glucose moiety that is transferred to the acceptor molecule. The acceptor can be a wide range of molecules, including other sugars, proteins, lipids, or small molecules.

In the context of human health and disease, GTs have been implicated in various pathological conditions, such as cancer, inflammation, and microbial infections. For example, some GTs can modify proteins on the surface of cancer cells, leading to increased cell proliferation, migration, and invasion. Additionally, GTs can contribute to bacterial resistance to antibiotics by modifying the structure of bacterial cell walls or by producing biofilms that protect bacteria from host immune responses and antimicrobial agents.

Overall, Glucosyltransferases are essential enzymes involved in various biological processes, and their dysregulation has been associated with several human diseases. Therefore, understanding the structure, function, and regulation of GTs is crucial for developing novel therapeutic strategies to target these enzymes and treat related pathological conditions.

"Rhodothermus" is not a medical term, but rather a genus name in the domain Bacteria. It belongs to the family Rhodothermaceae and is characterized by its ability to thrive in high-temperature environments, with an optimum growth temperature of around 65-70°C. These bacteria are typically found in marine hot springs and deep-sea hydrothermal vents. They play a role in the global carbon cycle by breaking down complex organic matter into simpler compounds, which can then be used by other organisms.

Therefore, "Rhodothermus" is not directly related to medical terminology or human health. However, understanding the biology and ecology of these extremophilic bacteria can provide insights into the fundamental principles of life and may have potential applications in biotechnology and industrial processes.

Glycogen is a complex carbohydrate that serves as the primary form of energy storage in animals, fungi, and bacteria. It is a polysaccharide consisting of long, branched chains of glucose molecules linked together by glycosidic bonds. Glycogen is stored primarily in the liver and muscles, where it can be quickly broken down to release glucose into the bloodstream during periods of fasting or increased metabolic demand.

In the liver, glycogen plays a crucial role in maintaining blood glucose levels by releasing glucose when needed, such as between meals or during exercise. In muscles, glycogen serves as an immediate energy source for muscle contractions during intense physical activity. The ability to store and mobilize glycogen is essential for the proper functioning of various physiological processes, including athletic performance, glucose homeostasis, and overall metabolic health.

Beta-glucans are a type of complex carbohydrate known as polysaccharides, which are found in the cell walls of certain cereals, bacteria, and fungi, including baker's yeast, mushrooms, and algae. They consist of long chains of glucose molecules linked together by beta-glycosidic bonds.

Beta-glucans have been studied for their potential health benefits, such as boosting the immune system, reducing cholesterol levels, and improving gut health. They are believed to work by interacting with immune cells, such as macrophages and neutrophils, and enhancing their ability to recognize and destroy foreign invaders like bacteria, viruses, and tumor cells.

Beta-glucans are available in supplement form and are also found in various functional foods and beverages, such as baked goods, cereals, and sports drinks. However, it is important to note that the effectiveness of beta-glucans for these health benefits may vary depending on the source, dose, and individual's health status. Therefore, it is recommended to consult with a healthcare professional before taking any dietary supplements or making significant changes to your diet.

Isoamylase is not a medical term per se, but rather a biochemical term used to describe an enzyme. Medically, it may be relevant in the context of certain medical conditions or treatments that involve carbohydrate metabolism. Here's a general definition:

Isoamylase (EC 3.2.1.68) is a type of amylase, a group of enzymes that break down complex carbohydrates, specifically starch and glycogen, into simpler sugars. Isoamylase is more precisely defined as an enzyme that hydrolyzes (breaks down) alpha-1,6 glucosidic bonds in isomaltose, panose, and dextrins, yielding mainly isomaltose and limit dextrin. It is found in various organisms, including bacteria, fungi, and plants. In humans, isoamylase is involved in the digestion of starch in the small intestine, where it helps convert complex carbohydrates into glucose for energy absorption.

Glucose-1-phosphate adenylyltransferase, also known as ADP-glucose pyrophosphorylase or AGPase, is an enzyme that plays a crucial role in carbohydrate metabolism, specifically in the synthesis of starch. It catalyzes the reaction between ATP and glucose-1-phosphate to produce ADP-glucose and pyrophosphate. This reaction is the first committed step in the biosynthetic pathway of starch in plants, algae, and some bacteria. In humans, defects in this enzyme can lead to a rare genetic disorder called glycogen storage disease type Ib.

Glucans are polysaccharides (complex carbohydrates) that are made up of long chains of glucose molecules. They can be found in the cell walls of certain plants, fungi, and bacteria. In medicine, beta-glucans derived from yeast or mushrooms have been studied for their potential immune-enhancing effects. However, more research is needed to fully understand their role and effectiveness in human health.

Adenosine diphosphate glucose (ADP-glucose) is a key intermediate in the biosynthesis of glycogen, which is a complex carbohydrate that serves as a primary form of energy storage in animals, fungi, and bacteria. In this process, ADP-glucose is formed from glucose-1-phosphate and adenosine triphosphate (ATP) through the action of the enzyme ADP-glucose pyrophosphorylase. Once synthesized, ADP-glucose is then used as a substrate for the enzyme glycogen synthase, which catalyzes the addition of glucose units to an existing glycogen molecule, leading to its growth and expansion. This pathway plays a crucial role in regulating cellular energy metabolism and maintaining glucose homeostasis within the body.

Glycogen synthase is an enzyme (EC 2.4.1.11) that plays a crucial role in the synthesis of glycogen, a polysaccharide that serves as the primary storage form of glucose in animals, fungi, and bacteria. This enzyme catalyzes the transfer of glucosyl residues from uridine diphosphate glucose (UDP-glucose) to the non-reducing end of an growing glycogen chain, thereby elongating it.

Glycogen synthase is regulated by several mechanisms, including allosteric regulation and covalent modification. The activity of this enzyme is inhibited by high levels of intracellular glucose-6-phosphate (G6P) and activated by the binding of glycogen or proteins that bind to glycogen, such as glycogenin. Phosphorylation of glycogen synthase by protein kinases, like glycogen synthase kinase-3 (GSK3), also reduces its activity, while dephosphorylation by protein phosphatases enhances it.

The regulation of glycogen synthase is critical for maintaining glucose homeostasis and energy balance in the body. Dysregulation of this enzyme has been implicated in several metabolic disorders, including type 2 diabetes and non-alcoholic fatty liver disease (NAFLD).

'Zea mays' is the biological name for corn or maize, which is not typically considered a medical term. However, corn or maize can have medical relevance in certain contexts. For example, cornstarch is sometimes used as a diluent for medications and is also a component of some skin products. Corn oil may be found in topical ointments and creams. In addition, some people may have allergic reactions to corn or corn-derived products. But generally speaking, 'Zea mays' itself does not have a specific medical definition.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Glycogen storage disease (GSD) is a group of rare inherited metabolic disorders that affect the body's ability to break down and store glycogen, a complex carbohydrate that serves as the primary form of energy storage in the body. These diseases are caused by deficiencies or dysfunction in enzymes involved in the synthesis, degradation, or transport of glycogen within cells.

There are several types of GSDs, each with distinct clinical presentations and affected organs. The most common type is von Gierke disease (GSD I), which primarily affects the liver and kidneys. Other types include Pompe disease (GSD II), McArdle disease (GSD V), Cori disease (GSD III), Andersen disease (GSD IV), and others.

Symptoms of GSDs can vary widely depending on the specific type, but may include:

* Hypoglycemia (low blood sugar)
* Growth retardation
* Hepatomegaly (enlarged liver)
* Muscle weakness and cramping
* Cardiomyopathy (heart muscle disease)
* Respiratory distress
* Developmental delays

Treatment for GSDs typically involves dietary management, such as frequent feedings or a high-protein, low-carbohydrate diet. In some cases, enzyme replacement therapy may be used to manage symptoms. The prognosis for individuals with GSDs depends on the specific type and severity of the disorder.

"Oryza sativa" is the scientific name for Asian rice, which is a species of grass and one of the most important food crops in the world. It is a staple food for more than half of the global population, providing a significant source of calories and carbohydrates. There are several varieties of Oryza sativa, including indica and japonica, which differ in their genetic makeup, growth habits, and grain characteristics.

Oryza sativa is an annual plant that grows to a height of 1-2 meters and produces long slender leaves and clusters of flowers at the top of the stem. The grains are enclosed within a tough husk, which must be removed before consumption. Rice is typically grown in flooded fields or paddies, which provide the necessary moisture for germination and growth.

Rice is an important source of nutrition for people around the world, particularly in developing countries where it may be one of the few reliable sources of food. It is rich in carbohydrates, fiber, and various vitamins and minerals, including thiamin, riboflavin, niacin, iron, and magnesium. However, rice can also be a significant source of arsenic, a toxic heavy metal that can accumulate in the grain during growth.

In medical terms, Oryza sativa may be used as a component of nutritional interventions for individuals who are at risk of malnutrition or who have specific dietary needs. It may also be studied in clinical trials to evaluate its potential health benefits or risks.

Polysaccharides are complex carbohydrates consisting of long chains of monosaccharide units (simple sugars) bonded together by glycosidic linkages. They can be classified based on the type of monosaccharides and the nature of the bonds that connect them.

Polysaccharides have various functions in living organisms. For example, starch and glycogen serve as energy storage molecules in plants and animals, respectively. Cellulose provides structural support in plants, while chitin is a key component of fungal cell walls and arthropod exoskeletons.

Some polysaccharides also have important roles in the human body, such as being part of the extracellular matrix (e.g., hyaluronic acid) or acting as blood group antigens (e.g., ABO blood group substances).

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

N-Acetylglucosaminyltransferases (GlcNAc transferases) are a group of enzymes that play a crucial role in the post-translational modification of proteins by adding N-acetylglucosamine (GlcNAc) to specific amino acids in a protein sequence. These enzymes catalyze the transfer of GlcNAc from a donor molecule, typically UDP-GlcNAc, to acceptor proteins, which can be other glycoproteins or proteins without any prior glycosylation.

The addition of N-acetylglucosamine by these enzymes is an essential step in the formation of complex carbohydrate structures called N-linked glycans, which are attached to asparagine residues within the protein sequence. The process of adding GlcNAc can occur in different ways, leading to various types of N-glycan structures, such as oligomannose, hybrid, and complex types.

There are several classes of N-Acetylglucosaminyltransferases (GnTs) based on their substrate specificity and the type of glycosidic linkage they form:

1. GnT I (MGAT1): Transfers GlcNAc to the α1,6 position of the mannose residue in the chitobiose core of N-linked glycans, initiating the formation of complex-type structures.
2. GnT II (MGAT2): Adds a second GlcNAc residue to the β1,4 position of the mannose residue at the non-reducing end of the chitobiose core, forming bi-antennary N-glycans.
3. GnT III (MGAT3): Transfers GlcNAc to the β1,4 position of the mannose residue in the chitobiose core, creating a branching point for further glycosylation and leading to tri- or tetra-antennary N-glycans.
4. GnT IV (MGAT4): Adds GlcNAc to the β1,4 position of the mannose residue at the non-reducing end of antennae, forming multi-branched complex-type structures.
5. GnT V (MGAT5): Transfers GlcNAc to the β1,6 position of the mannose residue in the chitobiose core, leading to hybrid and complex-type N-glycans with bisecting GlcNAc.
6. GnT VI (MGAT6): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
7. GnT VII (MGAT7): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
8. GnT VIII (MGAT8): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
9. GnT IX (MGAT9): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
10. GnT X (MGAT10): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
11. GnT XI (MGAT11): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
12. GnT XII (MGAT12): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
13. GnT XIII (MGAT13): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
14. GnT XIV (MGAT14): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
15. GnT XV (MGAT15): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
16. GnT XVI (MGAT16): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
17. GnT XVII (MGAT17): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
18. GnT XVIII (MGAT18): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
19. GnT XIX (MGAT19): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
20. GnT XX (MGAT20): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
21. GnT XXI (MGAT21): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
22. GnT XXII (MGAT22): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
23. GnT XXIII (MGAT23): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
24. GnT XXIV (MGAT24): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
25. GnT XXV (MGAT25): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
26. GnT XXVI (MGAT26): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
27. GnT XXVII (MGAT27): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
28. GnT XXVIII (MGAT28): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
29. GnT XXIX (MGAT29): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
30. GnT XXX (MG

Glucan Endo-1,3-beta-D-Glucosidase is an enzyme that catalyzes the hydrolysis of 1,3-beta-D-glycosyl links in glucans, which are polysaccharides composed of D-glucose units joined by beta-linkages. This enzyme specifically cleaves internal beta-1,3 bonds, resulting in the production of shorter glucan chains with reducing and non-reducing ends.

Glucan Endo-1,3-beta-D-Glucosidase is found in various organisms, including bacteria, fungi, and higher plants. It has attracted significant interest in biotechnological applications due to its potential role in the degradation of cell walls in pathogenic fungi and its ability to generate bioactive glucooligosaccharides with potential health benefits.

In medical contexts, Glucan Endo-1,3-beta-D-Glucosidase has been studied for its potential role in the treatment of fungal infections, as well as its diagnostic value in detecting and measuring specific types of glucans in biological samples.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Glucan 1,3-beta-Glucosidase is an enzyme that breaks down 1,3-beta-D-glucans, which are polysaccharides made up of chains of beta-D-glucose molecules linked together by 1,3-beta-glycosidic bonds. This enzyme catalyzes the hydrolysis of these glycosidic bonds, releasing individual glucose molecules or smaller oligosaccharides.

Glucan 1,3-beta-Glucosidase is found in various organisms, including bacteria, fungi, and higher plants. It has potential applications in biotechnology, such as in the production of biofuels and the degradation of plant material for use in animal feed. Additionally, it has been studied for its potential role in the treatment of certain medical conditions, such as fungal infections, where it can help to break down the cell walls of pathogenic fungi.

"Geobacillus stearothermophilus" is a species of gram-positive, rod-shaped bacteria that is thermophilic, meaning it thrives at relatively high temperatures. It is commonly found in soil and hot springs, and can also be found in other environments such as compost piles, oil fields, and even in some food products.

The bacterium is known for its ability to form endospores that are highly resistant to heat, radiation, and chemicals, making it a useful organism for sterility testing and bioprotection applications. It has an optimum growth temperature of around 60-70°C (140-158°F) and can survive at temperatures up to 80°C (176°F).

In the medical field, "Geobacillus stearothermophilus" is not typically associated with human disease or infection. However, there have been rare cases of infections reported in immunocompromised individuals who have come into contact with contaminated medical devices or materials.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

In medical terms, "seeds" are often referred to as a small amount of a substance, such as a radioactive material or drug, that is inserted into a tissue or placed inside a capsule for the purpose of treating a medical condition. This can include procedures like brachytherapy, where seeds containing radioactive materials are used in the treatment of cancer to kill cancer cells and shrink tumors. Similarly, in some forms of drug delivery, seeds containing medication can be used to gradually release the drug into the body over an extended period of time.

It's important to note that "seeds" have different meanings and applications depending on the medical context. In other cases, "seeds" may simply refer to small particles or structures found in the body, such as those present in the eye's retina.

Chorionic villi are finger-like projections of the chorion, which is the outermost extraembryonic membrane in a developing embryo. These structures are composed of both fetal and maternal tissues and play a crucial role in the early stages of pregnancy by providing a site for exchange of nutrients and waste products between the mother and the developing fetus.

Chorionic villi contain fetal blood vessels that are surrounded by stromal cells, trophoblasts, and connective tissue. They are formed during the process of implantation, when the fertilized egg attaches to the uterine wall. The chorionic villi continue to grow and multiply as the placenta develops, eventually forming a highly vascular and specialized organ that supports fetal growth and development throughout pregnancy.

One important function of chorionic villi is to serve as the site for the production of human chorionic gonadotropin (hCG), a hormone that can be detected in the mother's blood and urine during early pregnancy. This hormone plays a critical role in maintaining pregnancy by signaling the corpus luteum to continue producing progesterone, which helps to prevent menstruation and support fetal growth.

Abnormalities in chorionic villi can lead to various pregnancy complications, such as miscarriage, stillbirth, or intrauterine growth restriction. For this reason, chorionic villus sampling (CVS) is a diagnostic procedure that may be performed during early pregnancy to obtain fetal cells for genetic testing and diagnosis of chromosomal abnormalities or other genetic disorders.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Morphogenesis is a term used in developmental biology and refers to the process by which cells give rise to tissues and organs with specific shapes, structures, and patterns during embryonic development. This process involves complex interactions between genes, cells, and the extracellular environment that result in the coordinated movement and differentiation of cells into specialized functional units.

Morphogenesis is a dynamic and highly regulated process that involves several mechanisms, including cell proliferation, death, migration, adhesion, and differentiation. These processes are controlled by genetic programs and signaling pathways that respond to environmental cues and regulate the behavior of individual cells within a developing tissue or organ.

The study of morphogenesis is important for understanding how complex biological structures form during development and how these processes can go awry in disease states such as cancer, birth defects, and degenerative disorders.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Neurospora is not a medical term, but a genus of fungi commonly found in the environment. It is often used in scientific research, particularly in the fields of genetics and molecular biology. The most common species used in research is Neurospora crassa, which has been studied extensively due to its haploid nature, simple genetic structure, and rapid growth rate. Research using Neurospora has contributed significantly to our understanding of fundamental biological processes such as gene regulation, metabolism, and circadian rhythms.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Q-enzyme, alpha-glucan-branching glycosyltransferase, amylose isomerase, enzymatic branching factor, branching ... This connection is catalyzed by a branching enzyme, generally given the name α-glucan branching enzyme. A branching enzyme ... Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a ... and branching enzyme. Shown by x-ray crystallography, glycogen branching enzyme has four marginally asymmetric units each that ...
It is found in a range of enzymes that act on branched substrates i.e. isoamylase, pullulanase and branching enzyme. Isoamylase ... Carbohydrate-binding module family 25 (CBM25) binds alpha-glucooligosaccharides, particularly those containing alpha-1,6 ... 3-mixed linked glucans only bind in cleft B. Carbohydrate-binding module family 9 (CBM9) binds to crystalline cellulose. CBM4 ... 6-alpha-D-glucosidic branch linkages in glycogen, amylopectin and dextrin; 1,4-alpha-glucan branching enzyme functions in the ...
The GBE1 gene provides instructions for making the glycogen branching enzyme. This enzyme is involved in the production of a ... A person inherits loss-of-function mutations in the GBE1 gene from each parent, and the lack of glycogen branching enzyme (the ... Whether or not a person is making sufficient amounts of functional glycogen branching enzyme can be determined by taking a skin ... Most GBE1 gene mutations result in a shortage (deficiency) of the glycogen branching enzyme, which leads to the production of ...
... cholesterol 7 alpha-hydroxylase MeSH D08.811.682.690.708.783.212 - cholesterol side-chain cleavage enzyme MeSH D08.811.682.690. ... glucan 1,4-beta-glucosidase MeSH D08.811.277.450.420.200.600 - glucan endo-1,3-beta-d-glucosidase MeSH D08.811.277.450.420.375 ... cholesterol 7 alpha-hydroxylase MeSH D08.244.453.915.212 - cholesterol side-chain cleavage enzyme MeSH D08.244.453.915.400 - 25 ... cholesterol 7 alpha-hydroxylase MeSH D08.811.682.690.708.170.915.212 - cholesterol side-chain cleavage enzyme MeSH D08.811. ...
... is an enzyme that catalyzes the chemical reaction that transfers an alpha-D-glucosyl residue in a 1,4-alpha-D-glucan to the ... 6-alpha-D-glucosyltransferase. Other names in common use include oligoglucan-branching glycosyltransferase, 1,4-alpha-D-glucan ... 6-alpha-D-glucosyltransferase, T-enzyme, and D-glucosyltransferase. Abdullah M; Whelan WJ (1960). "Synthesis of alpha-1:6- ... This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this ...
While most alpha-amylase enzymes only cleave alpha-1,4-linkages in their substrates, neopullulanase additionally cleaves alpha- ... also known as glycogen branching enzyme). Like these enzymes, each monomer contains an active site at the carboxyl-terminus ... The enzyme first selectively hydrolyzes alpha-1,4-glucosidic bonds on the nonreducing side of pullulan's alpha-1,6-glucosidic ... This results in narrower active site than the other alpha-amylase enzymes, which do not dimerize, and likely contributes to its ...
... α-glucan can be comparably synthesized via the maltosyl transferase GlgE and branching enzyme GlgB. This alternative pathway is ... α-Glucans (alpha-glucans) are polysaccharides of D-glucose monomers linked with glycosidic bonds of the alpha form. α-Glucans ... Alpha-glucan is also commonly found in bacteria, yeasts, plants, and insects. Whereas the main pathway of α-glucan synthesis is ... 6-glucan (including amylopectin) Shimomura, Shoji; Fukui, Toshio (1980). "A comparative study on .alpha.-glucan phosphorylases ...
... highly branched starch chains have to be phosphorylated in order to be accessible for degrading enzymes. The enzyme glucan, ... the other enzyme-potato alpha-glucan phosphorylase can add a glucose unit from glucose 1-phosphorylase to the non-reducing ends ... The starch debranching enzyme isoamylase removes some of these branches. Several isoforms of these enzymes exist, leading to a ... 6-alpha branching bonds. A second enzyme, phosphoglucan, water dikinase (PWD) phosphorylates the glucose molecule at the C-3 ...
"Amylase, Alpha - Worthington Enzyme Manual". worthington-biochem.com. Archived from the original on 14 October 2016. Valls, ... but compound hydrolysis requires an enzyme that acts on branched products. Salivary amylase is inactivated in the stomach by ... The alpha-Amylase Protein alpha-Amylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article ... Digestive enzyme Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ (May 1996). "Structure of human salivary α-amylase at 1.6 Å ...
These extracellular homopolysaccharides are called α-glucan polymers. Glucansucrase enzymes can synthesize a variety of glucans ... "A circularly permuted alpha-amylase-type alpha/beta-barrel structure in glucan-synthesizing glucosyltransferases". FEBS Letters ... University of Texas Medical Branch at Galveston. 1996. ISBN 978-0-9631172-1-2. Colby SM, McLaughlin RE, Ferretti JJ, Russell RR ... This glucose is added to a growing glucan chain. Glucansucrase uses the energy released from bond cleavage to drive glucan ...
Glucans are noted in two forms: alpha glucans and beta glucans. Many beta-glucans are medically important. They represent a ... 3-glucan Properties of glucans include resistance to oral acids/enzyme and water insolubility. Glucans extracted from grains ... 3-branches floridean starch, α-1,4- and α-1,6-glucan glycogen, α-1,4- and α-1,6-glucan pullulan, α-1,4- and α-1,6-glucan starch ... Glucans serve a diverse set of functions. Within the cell, certain glucans store energy, fortify cellular structure, behave in ...
They contain no enzymes. ASBC 50-165/EBC 90-320; the typical British crystal malt used in pale ale and bitter is around ASBC 70 ... Unconverted starch becomes sugar during the last steps of mashing, through the action of alpha and beta amylases. The oldest ... and contains large quantities of beta-glucans compared to other grains; these long-chain sugars can leach out during a mash, ... not fully modified requires mashing in multiple steps rather than at simply one temperature as the starches must be de-branched ...
Varieties that contain a slightly higher amylopectin content, which is a highly branched molecule, help the potato retain its ... Potato starch contains two types of glucan, amylose and amylopectin, the latter of which is most industrially useful. Waxy ... Carotenoid compounds include provitamin A alpha-carotene and beta-carotene, which are converted to the essential nutrient, ... an enzyme which catalyzes the formation of amylose. 'Amflora' potatoes therefore produce starch consisting almost entirely of ...
Usually β-glucan is solubilized in the extraction process with residual starch, which is then removed by hydrolysis with alpha- ... Additionally, studies suggest that it increases the activity of CYP7A1, a key enzyme in the synthesis of bile acids, thus ... Sciences, Government of Canada, Health Canada, Health Products and Food Branch, Food Directorate, Bureau of Nutritional (25 ... In oats, β-glucan makes up the majority of the soluble fibre; however, oat β-glucans do become insoluble above a certain ...
They inhibit the enzyme 14-alpha-sterol demethylase, a microsomal CYP, which is required for biosynthesis of ergosterol for the ... Echinocandins inhibit the creation of glucan in the fungal cell wall by inhibiting 1,3-Beta-glucan synthase: Anidulafungin ... University of Texas Medical Branch at Galveston, ISBN 978-0-9631172-1-2, PMID 21413319, retrieved 2 December 2022 PubChem. " ... This leads to the accumulation of 14-alpha-methylsterols resulting in impairment of function of certain membrane-bound enzymes ...
The fungal cell wall is made of a chitin-glucan complex; while glucans are also found in plants and chitin in the exoskeleton ... Harris SD (2008). "Branching of fungal hyphae: regulation, mechanisms and comparison with other branching systems". Mycologia. ... Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The alpha-aminoadipate pathway for lysine biosynthesis in fungi". Cell ... Pereira JL, Noronha EF, Miller RN, Franco OL (June 2007). "Novel insights in the use of hydrolytic enzymes secreted by fungi ...
Ability to form branching chains of cells, known as pseudohyphae is also sometimes said to be associated with virulence, though ... At first, this was thought to increase RLS by up-regulating the sir2 enzyme, however it was later discovered that this effect ... Yeast has two mating types, a and α (alpha), which show primitive aspects of sex differentiation. As in many other eukaryotes, ... After AMR constriction is complete, two secondary septums are formed by glucans. How the AMR ring dissembles remains poorly ...
GNAI3: G protein subunit alpha i3. *GNAQ: G protein subunit alpha q ... GNPTAB: N-acetylglucosamine-1-phosphate transferase subunits alpha and beta. *GNPTG: N-acetylglucosamine-1-phosphate ...
... is a rare autosomal recessive disorder caused by a deficiency of glycogen branching enzyme. Glycogen storage disease type IV ... is a rare autosomal recessive disorder caused by a deficiency of glycogen branching enzyme. Glycogen storage disease type IV ... Sing-Chung Li 1 , Wuh-Liang Hwu, Ju-Li Lin, Deeksha S Bali, Chen Yang, Shih-Ming Chu, Yin-Hsiu Chien, Hung-Chieh Chou, Chien-Yi ... 1 School of Nutrition and Health Science, Taipei Medical University, Taipei, Taiwan. ...
Q-enzyme, alpha-glucan-branching glycosyltransferase, amylose isomerase, enzymatic branching factor, branching ... This connection is catalyzed by a branching enzyme, generally given the name α-glucan branching enzyme. A branching enzyme ... Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a ... and branching enzyme. Shown by x-ray crystallography, glycogen branching enzyme has four marginally asymmetric units each that ...
Lee, Y. C., Chang, C. J., Bali, D., Chen, Y. T., and Yan, Y. T. (2011). Glycogen-branching enzyme deficiency leads to abnormal ... Ward, T. L., Valberg, S. J., Adelson, D. L., Abbey, C. A., Binns, M. M., and Mickelson, J. R. (2004). Glycogen branching enzyme ... Animals of a specific breed clustering outside the expected breed branch were removed. In the case of multiple clusters for a ... Individuals of the same breed were collapsed to a branch labelled with the breeds name. One auroch (Bos primigenius) was added ...
HALLMARK_INTERFERON_ALPHA_RESPONSE HALLMARK_INTERFERON_GAMMA_RESPONSE HALLMARK_KRAS_SIGNALING_DN HALLMARK_KRAS_SIGNALING_UP ... branched chain amino acid transaminase 1.... BHLHE40. 8553. BHLHE40. basic helix-loop-helix family member e40.... ... malic enzyme 1 [Source:HGNC Symbol;Acc:H.... MLLT11. 10962. MLLT11. MLLT11 transcription factor 7 cofactor [.... ... MODULE_1 MODULE_100 MODULE_104 MODULE_11 MODULE_112 MODULE_117 MODULE_118 MODULE_12 MODULE_128 MODULE_129 MODULE_13 MODULE_137 ...
Branching Enzyme. 1,4-alpha-Glucosidase, Exo use Glucan 1,4-alpha-Glucosidase ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 1-Sar-8-Ile Angiotensin II use 1-Sarcosine-8-Isoleucine Angiotensin II ...
Branching Enzyme. 1,4-alpha-Glucosidase, Exo use Glucan 1,4-alpha-Glucosidase ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 1-Sar-8-Ile Angiotensin II use 1-Sarcosine-8-Isoleucine Angiotensin II ...
Branching Enzyme. 1,4-alpha-Glucosidase, Exo use Glucan 1,4-alpha-Glucosidase ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ...
Branching Enzyme. 1,4-alpha-Glucosidase, Exo use Glucan 1,4-alpha-Glucosidase ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 1-Sar-8-Ile Angiotensin II use 1-Sarcosine-8-Isoleucine Angiotensin II ...
Branching Enzyme. 1,4-alpha-Glucosidase, Exo use Glucan 1,4-alpha-Glucosidase ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 1-Sar-8-Ile Angiotensin II use 1-Sarcosine-8-Isoleucine Angiotensin II ...
Glycyl-tRNA synthetase alpha chain. 160.44. 0.5440. 135. sll0849 Photosystem II reaction center D2 protein. 161.76. 0.5375. ... Type 4 pilin-like protein, essential for motility. 3.46. 0.8142. 3. slr1377 Leader peptidase I (signal peptidase I). 4.47. ... 1,4-alpha-glucan branching enzyme. 24.27. 0.7068. 18. slr2017 Type 4 pilin-like protein, essential for motility. 24.33. 0.7253 ... Probable 4-hydroxyphenylpyruvate dioxygenase. 102.22. 0.5562. 84. slr2019 ATP-binding protein of ABC transporter. 102.83. ...
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the ... starch branching enzyme III [Zea mays]. RefSeq. NP_001154629.1. 0. 74. 899. 68. 899. alpha-amylase/ catalytic/ cation binding [ ... The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on ... A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L. ...
Hereditary branching enzyme dysfunction in adult polyglucosan body disease: A possible metabolic cause in two patients. Lossos ... Gomori, J. M., Steiner, I., Melamed, E. & Cooper, G., Jan 1984, In: Neuroradiology. 26, 1, p. 21-24 4 p.. Research output: ... Steiner, I., Gomori, J. M. & Melamed, E., 1984, In: Stroke. 15, 2, p. 279-282 4 p.. Research output: Contribution to journal › ... Wirguin, I., Steiner, I., Brenner, T. & Abramsky, O., Aug 1991, In: Annals of Neurology. 30, 2, p. 227 1 p.. Research output: ...
... branching enzyme 1. 3p12.3. CV:PGCnp. DEG:Sanders_2013. DMG:Jaffe_2016. GSMA_IIA. GSMA_IIE. ... gap junction protein alpha 1. 6q22.31. CV:PGCnp. DMG:Wockner_2014. Network. ION BALANCE. G2Cdb.human_BAYES-COLLINS-HUMAN-PSD- ... glucan (1,4-alpha-), ... lysyl oxidase like 1. 15q22. CV:PGCnp. CV:PheWAS. 6457. SH3GL3 ... peptidylglycine alpha-amidating monooxygenase. 5q14-q21. CV:GWASdb. CV:PGCnp. Expression. GR_Ng. PMID:cooccur. ...
Please cite Turkarslan et al., 2017 Mol. Sys. Biol. if you find Syntrophy Portal useful.. Acknowledgement: "This material by ENIGMA- Ecosystems and Networks Integrated with Genes and Molecular Assemblies (http://enigma.lbl.gov), a Scientific Focus Area Program at Lawrence Berkeley National Laboratory is based upon work supported by the U.S. Department of Energy, Office of Science, Office of Biological & Environmental Research under contract number DE-AC02-05CH11231" ...
glucosidase, alpha; acid. Felis catus. domestic cat. protein-coding. GBE1. glucan (1,4-alpha-), branching enzyme 1. Felis catus ... apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C. Felis catus. domestic cat. protein-coding. ... iduronidase, alpha-L-. Felis catus. domestic cat. protein-coding. ITGA2B. integrin, alpha 2b (platelet glycoprotein IIb of IIb/ ... collagen, type V, alpha 1. Felis catus. domestic cat. protein-coding. COLQ. collagen-like tail subunit (single strand of ...
Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer ... Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose ... The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local ... suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity. ...
ubiquitin conjugating enzyme E2 M [Sou.... UBE2S. 27338. UBE2S. ubiquitin conjugating enzyme E2 S [Sou.... ... mannosidase alpha class 2A member 1 [S.... MAPKAPK2. 9261. MAPKAPK2. MAPK activated protein kinase 2 [Sourc.... ... GSE17721_4_VS_24H_GARDIQUIMOD_BMDC_UP GSE17721_4H_VS_24H_POLYIC_BMDC_DN GSE17721_4H_VS_24H_POLYIC_BMDC_UP GSE17721_ALL_VS_24H_ ... BENPORATH_ES_1 BENPORATH_ES_2 BENPORATH_ES_CORE_NINE BENPORATH_ES_CORE_NINE_CORRELATED BENPORATH_ES_WITH_H3K27ME3 BENPORATH_MYC ...
Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli. Download Prime PubMed ... Branching enzyme belongs to the alpha-amylase family, which includes enzymes that catalyze hydrolysis or transglycosylation at ... Limited proteolysis of branching enzyme from Escherichia coli.. *The N-terminal region of the starch-branching enzyme from ... Branching enzyme belongs to the alpha-amylase family, which includes enzymes that catalyze hydrolysis or transglycosylation at ...
Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in ... 6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Bacterial isoamylases are ... alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as ... is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase ( ...
glucan- branching. enzyme. Maltase-. glucoamylase,. intestinal. Alpha-amylase 1. Maltase-. glucoamylase,. intestinal. Glycogen ... enzyme. Maltase-. glucoamylase,. intestinal. Glycogen. debranching. enzyme. UDP-glucose. 6-dehydrogenase. Glycogen. ... 1-phosphate. Isovalerylglucuronide. Uridine. 5-diphosphate. H. 2. O. D-Glucuronic acid. Magnesium. Magnesium. Calcium. ... 1,6-bisphosphate. 3-Phosphoglyceric. acid. Uridine. triphosphate. Uridine. diphosphate. glucose. PP. i. Amylose. Uridine. 5- ...
Alteration of amylopectin branching patterns in opaque2 starch could contribute to generation of the soft, starchy endosperm. ... Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme. Arch Biochem Biophys. 1997, 342: 92- ... Amylopectin branch length analysis. Solubilized starch was de-branched in the presence of isoamylase and the resulting glucan ... Song RT, Llaca V, Linton E, Messing J: Sequence, regulation, and evolution of the maize 22-kD alpha zein in gene family. Genome ...
AutoFact: starch branching enzyme II [Solanum tuberosum] 3.0e-36 • FL-Next: sp=1,4-alpha-glucan-branching enzyme 2-2, ... AutoFact: PREDICTED: glucan (1,4-alpha-), branching enzyme 1-like n=1 Tax=Saccoglossus kowalevskii RepID=UPI0001CBA1CF 1.00053e ... AutoFact: Glucose-1-phosphate adenylyltransferase n=1 Tax=Physcomitrella patens subsp. patens RepID=A9T6T4_PHYPA 4.0e-31 ... AutoFact: Glucose-1-phosphate adenylyltransferase n=1 Tax=Physcomitrella patens subsp. patens RepID=A9T6T4_PHYPA 2.0e-21 ...
3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... Exo use Glucan 1,4-alpha-Glucosidase 1,4-Benzopyrones use Chromones ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ...
3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... Exo use Glucan 1,4-alpha-Glucosidase 1,4-Benzopyrones use Chromones ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ...
3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... Exo use Glucan 1,4-alpha-Glucosidase 1,4-Benzopyrones use Chromones ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid ... 4 Hydroxyphenylpyruvate Dioxygenase Deficiency Disease use Tyrosinemias 4-Nitrophenol-2-Hydroxylase use Cytochrome P-450 CYP2E1 ...
Q-Enzyme use 1,4-alpha-Glucan Branching Enzyme Q-SNARE Proteins ...
Decreases in these enzymes have been shown to lead to increased TAG production as fatty acid biosynthesis is favoured. Data are ... this enzyme is involved in acetyl CoA production and has been linked to TAG accumulation in microalgae. In salt-stressed C. ... In addition, starch branching enzyme was lower in abundance at 168 h of salt exposure (decreasing carbohydrate levels) compared ... Alpha-1,4 glucan phosphorylase, a protein causing the degradation of starch and important in starch remobilisation [57], was ...
  • The protein encoded by this gene is a glycogen branching enzyme that catalyzes the transfer of alpha-1,4-linked glucosyl units from the outer end of a glycogen chain to an alpha-1,6 position on the same or a neighboring glycogen chain. (wikipedia.org)
  • A-kinase interacting protein 1 [Source. (gsea-msigdb.org)
  • meiosis 1 associated protein [Source:H. (gsea-msigdb.org)
  • Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity. (liberumbio.com)
  • Preliminary research suggests that the alpha lipoic acid found in supplements may be more biologically active than when bound to this protein in food. (nordicvms.com)
  • Branching enzyme belongs to the alpha-amylase family, which includes enzymes that catalyze hydrolysis or transglycosylation at alpha-(1,4)- or alpha-(1,6)-glucosidic linkages. (unboundmedicine.com)
  • AU - Mikkelsen,R, AU - Binderup,K, AU - Preiss,J, PY - 2001/5/23/pubmed PY - 2001/6/8/medline PY - 2001/5/23/entrez SP - 372 EP - 7 JF - Archives of biochemistry and biophysics JO - Arch Biochem Biophys VL - 385 IS - 2 N2 - Branching enzyme belongs to the alpha-amylase family, which includes enzymes that catalyze hydrolysis or transglycosylation at alpha-(1,4)- or alpha-(1,6)-glucosidic linkages. (unboundmedicine.com)
  • Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. (unl.edu)
  • Highly specific hydrolysis of α-1,3-linked L-arabinofuranose residues from doubly substituted D-xylosyl or L-arabinosyl residues of arabinoxylans and branched arabinans, respectively. (megazyme.com)
  • A range of α-L-arabinofuranosyl-(1-4)-β-D-xylo-oligosaccharides (AXOS) were produced by hydrolysis of wheat flour arabinoxylan (WAX) and acid debranched arabinoxylan (ADWAX), in the presence and absence of an AXH-d3 α-L-arabinofuranosidase, by several GH10 and GH11 β-xylanases. (megazyme.com)
  • Alteration of amylopectin branching patterns in opaque2 starch could contribute to generation of the soft, starchy endosperm. (biomedcentral.com)
  • While this is not necessary for conversion, as plants do exactly this when they germinate, it greatly speeds up the process though the exposure of a lot of substrate (amylose and amylopectin) from the starch granule to the starch converting enzymes (mainly α- and β-amylase). (braukaiser.com)
  • The reason for that is the presence of enzymes (in particular α-amylase) that will start breaking down the amylose and amylopectin molecules as soon as they become accessible. (braukaiser.com)
  • Since glycogen is a readily mobilized storage form of glucose, the extended glycogen polymer is branched by glycogen branching enzyme to provide glycogen breakdown enzymes, such as glycogen phosphorylase, with many terminal residues for rapid degradation. (wikipedia.org)
  • The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. (unl.edu)
  • Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). (unl.edu)
  • As a glucosidase, it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. (unl.edu)
  • Agricultural residues can thus be used for the production of various value-added products, such as industrially important enzymes. (mdpi.com)
  • Glycogen branching enzyme belongs to the α-amylase family of enzymes, which include α-amylases, pullulanas/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzyme. (wikipedia.org)
  • N-terminal Early set domain associated with the catalytic domain of Glycogen debranching enzyme and bacterial isoamylase (also called glycogen 6-glucanohydrolase). (unl.edu)
  • Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. (unl.edu)
  • Importantly, glycogen synthase can only catalyze the synthesis of α-1,4-glycosidic linkages. (wikipedia.org)
  • These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. (unl.edu)
  • Amylose is defined as a linear molecule of (1→4) linked alpha-D-glucopyranosyl units, but it is today well established that some molecules are slightly branched by (1→6)-alpha-linkages. (foodb.ca)
  • The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). (unl.edu)
  • Glycogen branching enzyme is an enzyme that adds branches to the growing glycogen molecule during the synthesis of glycogen, a storage form of glucose. (wikipedia.org)
  • More specifically, during glycogen synthesis, a glucose 1-phosphate molecule reacts with uridine triphosphate (UTP) to become UDP-glucose, an activated form of glucose. (wikipedia.org)
  • The activated glucosyl unit of UDP-glucose is then transferred to the hydroxyl group at the C-4 of a terminal residue of glycogen to form an α-1,4-glycosidic linkage, a reaction catalyzed by glycogen synthase. (wikipedia.org)
  • In glycogen, every 10 to 14 glucose units, a side branch with an additional chain of glucose units occurs. (wikipedia.org)
  • The side chain attaches at carbon atom 6 of a glucose unit, an α-1,6-glycosidic bond. (wikipedia.org)
  • As a transferase, it transfers a segment of the 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. (unl.edu)
  • Glucose-1-phosphate adenylyltransferase n=1 Tax=Physcomitrella patens subsp. (uma.es)
  • It can also hydrolyze the α-D-1, 6 glucoside branch bonds of starch and cleaves the α-1, 3 bonds to release glucose. (glucoamylaseenzyme.com)
  • Glycogen debranching enzymes have both 4-alpha-glucanotransferase and amylo-1,6-glucosidase activities. (unl.edu)
  • 1,4-alpha-glucan-branching enzyme, also known as brancher enzyme or glycogen-branching enzyme is an enzyme that in humans is encoded by the GBE1 gene. (wikipedia.org)
  • Shown by x-ray crystallography, glycogen branching enzyme has four marginally asymmetric units each that are organized into three domains: an amino-terminal domain, involved in determining the length of the chain transfer, a carboxyl-terminal domain, involved in substrate preference and catalytic capacity, and a central (α/β) barrel catalytic domain. (wikipedia.org)
  • Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. (unl.edu)
  • Exhibits an alpha-retaining catalytic mechanism. (liberumbio.com)
  • E or "early" set domains are associated with the catalytic domain of the glycogen debranching enzyme at the N-terminal end. (unl.edu)
  • branched chain amino acid transaminase 1. (gsea-msigdb.org)
  • From amino acid sequence analysis a tyrosine residue is completely conserved in the alpha-amylase family. (unboundmedicine.com)
  • In the 1960s the research groups of Mertz and Nelson at Purdue University identified several mutants with increased lysine content, opaque2 ( o2 ) and floury2 in particular, had substantially higher essential amino acid content [ 3 , 4 ]. (biomedcentral.com)
  • This endogenous metabolite of the branched-chain amino acid (BCAA) leucine (LEU) is produced when leucine is oxidised in the cell cytoplasm, mainly in the liver and muscles. (researchsquare.com)
  • Kirkman's Alpha-Ketoglutaric Acid is an organic acid that is important for the metabolism of all essential amino acids and the transfer of cellular energy in the citric acid cycle. (nordicvms.com)
  • When degraded by pure beta-amylase, linear macromolecules are completely converted into maltose, whereas branched chains give also one beta-limit dextrin consisting of the remaining inner core polysaccharide structure with its outer chains recessed. (foodb.ca)
  • Glycogen binding enzymes in other organisms have also been crystallized and structurally determined, demonstrating both similarity and variation to GBE found in Escherichia coli. (wikipedia.org)
  • In Escherichia coli branching enzyme, this residue (Y300) is located prior to the conserved region 1. (unboundmedicine.com)
  • TY - JOUR T1 - Tyrosine residue 300 is important for activity and stability of branching enzyme from Escherichia coli. (unboundmedicine.com)
  • HMB also had a positive effect on the oxidative metabolism of monocytes and granulocytes stimulated with PMA (4-phorbol-12-β-myristate-13-acetate) and Escherichia coli bacteria, expressed as MFI values and the percentage of oxidative metabolism. (researchsquare.com)
  • This enzyme belongs to the family of transferases, to be specific, those glycosyltransferases that transfer hexoses (hexosyltransferases). (wikipedia.org)
  • [ 4 ] Candida organisms and some ubiquitous filamentous fungi ( Aspergillus and Scedosporium ) can be isolated from oropharyngeal and respiratory tracts as colonizers without evidence of invasion or symptoms until a breakdown of tissue barriers or of the host's immune system occurs. (medscape.com)
  • Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic OS=Oryza sativa subsp. (uma.es)
  • The systematic name of this enzyme class is 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-D-(1,4-alpha-D-glucano)-transferase. (wikipedia.org)
  • Branching of the chains is essential to increase the solubility of the glycogen molecule and, consequently, in reducing the osmotic pressure within cells. (wikipedia.org)
  • Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. (unl.edu)
  • Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. (liberumbio.com)
  • The first process occurs in the mitochondria where α-KIC is oxidised to isovaleryl-CoA by branched-chain ketoacid dehydrogenase (BCKAD). (researchsquare.com)
  • I am interested in 200000u/G Powder Baking Glucoamylase Enzyme could you send me more details such as type, size, quantity, material, etc. (glucoamylaseenzyme.com)
  • This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. (unl.edu)
  • An alternative process takes place in the cytosol where HMB is produced from α-KIC by the KIC dioxygenase enzyme. (researchsquare.com)
  • The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. (unl.edu)
  • This enzyme participates in starch and sucrose metabolism. (wikipedia.org)
  • Branching also importantly increases the solubility and decreases the osmotic strength of glycogen. (wikipedia.org)
  • Decreases in these enzymes have been shown to lead to increased TAG production as fatty acid biosynthesis is favoured. (biomedcentral.com)
  • Site-directed mutagenesis of the Y300 residue in E. coli branching enzyme was used in order to study its possible function in branching enzymes. (unboundmedicine.com)
  • Thus, these results show that Tyr residue 300 in E. coli branching enzyme is important for activity and thermostability of the enzyme. (unboundmedicine.com)
  • In the alpha-amylase family, four highly conserved regions are proposed to make up the active site. (unboundmedicine.com)
  • C-X-C motif chemokine receptor 4 [Source. (gsea-msigdb.org)
  • With regard to predisposition through stem cell transplants, certain toll-like receptor (TLR) polymorphisms (eg, TLR 4 haplotype S4) in an unrelated stem cell donor can increase the risk of invasive aspergillosis in the transplant recipient. (medscape.com)
  • The heat stability of Y300F was analyzed, and this was lowered significantly compared to that of the wild-type enzyme. (unboundmedicine.com)
  • MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. (unl.edu)
  • PUREMEI NDS can hydrolyze α-D-1, 4 glucosidic bonds from the non-reducing end of starch one after. (glucoamylaseenzyme.com)
  • In comparison to the other family members, glycogen binding enzyme has shorter loops, which result in a more open cavity, favorable to the binding of a bulkier substrate such as branched sugar. (wikipedia.org)
  • Highly viscous hydrating molecule that can resist the attacks of hyaluronidase, a family of enzymes that degrade hyaluronic acid. (skinregimen.co.th)
  • CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). (unl.edu)
  • Proteins make up only 3% and the rest are β-glucans, vitamins and minerals. (braukaiser.com)
  • Anderson disease, also known as glycogen storage disease type IV (MIM 232500), is a rare autosomal recessive disorder caused by a deficiency of glycogen branching enzyme. (nih.gov)
  • These agents inhibit the cytochrome P450-dependent 14-alpha-lanosterol demethylase of the fungal cell membrane. (medscape.com)
  • A 2010 study [3] found that maitake eased the inflammation associated with inflammatory bowel disease by suppressing the production and activity of a cytokine (immune signaling molecule) known as TNF-alpha. (organixx.com)
  • Because of its dual solubility, alpha lipoic acid can function in both fatty and aqueous parts of a cell and is capable of defending against a wide variety of invading free radicals. (nordicvms.com)
  • The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. (liberumbio.com)
  • High purity α-L-Arabinofuranosidase ( Bifidobacterium adolescentis ) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. (megazyme.com)
  • Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. (liberumbio.com)
  • Replacement of Y300 with Ala, Asp, Leu, Ser, and Trp resulted in mutant enzymes with less than 1% of wild-type activity. (unboundmedicine.com)
  • An enzymic activity of this nature forms part of the mammalian and Saccharomyces cerevisiae glycogen branching system (see EC 3.2.1.33 ). (expasy.org)
  • Echinocandins have minimal activity against the Mucorales, which contain little or no beta-1,3-D-glucan. (medscape.com)
  • One Unit of α-L-arabinofuranosidase activity is defined as the amount of enzyme required to release one µmole of arabinose per minute from wheat arabinoxylan (10 mg/mL) in sodium phosphate buffer (100 mM), pH 6.0 at 40 o C. (megazyme.com)
  • The enzyme showed the highest activity toward wheat arabinoxylan oligosaccharides. (megazyme.com)