Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
Carbohydrates present in food comprising digestible sugars and starches and indigestible cellulose and other dietary fibers. The former are the major source of energy. The sugars are in beet and cane sugar, fruits, honey, sweet corn, corn syrup, milk and milk products, etc.; the starches are in cereal grains, legumes (FABACEAE), tubers, etc. (From Claudio & Lagua, Nutrition and Diet Therapy Dictionary, 3d ed, p32, p277)
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that occurs in fish and other aquatic animals and in a variety of mammals, including man. Its organisms probably do not belong to the normal intestinal flora of man and can cause diarrhea.
A species of gram-negative, aerobic bacteria first isolated from soil in Vineland, New Jersey. Ammonium and nitrate are used as nitrogen sources by this bacterium. It is distinguished from other members of its genus by the ability to use rhamnose as a carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Component of dermatan sulfate. Differs in configuration from glucuronic acid only at the C-5 position.
Term used to designate tetrahydroxy aldehydic acids obtained by oxidation of hexose sugars, i.e. glucuronic acid, galacturonic acid, etc. Historically, the name hexuronic acid was originally given to ascorbic acid.
Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)
A sugar acid formed by the oxidation of the C-6 carbon of GLUCOSE. In addition to being a key intermediate metabolite of the uronic acid pathway, glucuronic acid also plays a role in the detoxification of certain drugs and toxins by conjugating with them to form GLUCURONIDES.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
Salts of alginic acid that are extracted from marine kelp and used to make dental impressions and as absorbent material for surgical dressings.
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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The characteristic 3-dimensional shape of a carbohydrate.
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.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The relationships of groups of organisms as reflected by their genetic makeup.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The rate dynamics in chemical or physical systems.
Proteins found in any species of bacterium.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
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.
Carbohydrate antigens expressed by malignant tissue. They are useful as tumor markers and are measured in the serum by means of a radioimmunoassay employing monoclonal antibodies.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
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.

Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase. (1/698)

Neuraminic acids are widely expressed as terminal carbohydrates on glycoconjugates and are involved in a variety of biological functions. The key enzyme of N-acetylneuraminic acid synthesis is UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase, which catalyses the first two steps of neuraminic acid biosynthesis in the cytosol. In this study we report the complete amino acid sequence of the mouse UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase. The ORF of 2166 bp encodes 722 amino acids and a protein with a predicted molecular mass of 79.2 kDa. Northern blot analysis and in situ hybridization revealed that UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase is expressed at early stages during development and in all tissues investigated with a maximal expression in the liver.  (+info)

The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism. (2/698)

The Ca2+-dependent mannuronan C-5-epimerase AlgE4 is a representative of a family of Azotobacter vinelandii enzymes catalyzing the polymer level epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in the commercially important polysaccharide alginate. The reaction product of recombinantly produced AlgE4 is predominantly characterized by an alternating sequence distribution of the M and G residues (MG blocks). AlgE4 was purified after intracellular overexpression in Escherichia coli, and the activity was shown to be optimal at pH values between 6.5 and 7.0, in the presence of 1-3 mM Ca2+, and at temperatures near 37 degrees C. Sr2+ was found to substitute reasonably well for Ca2+ in activation, whereas Zn2+ strongly inhibited the activity. During epimerization of alginate, the fraction of GMG blocks increased linearly as a function of the total fraction of G residues and comparably much faster than that of MMG blocks. These experimental data could not be accounted for by a random attack mechanism, suggesting that the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks.  (+info)

Conversion of dTDP-4-keto-6-deoxyglucose to free dTDP-4-keto-rhamnose by the rmIC gene products of Escherichia coli and Mycobacterium tuberculosis. (3/698)

dTDP-rhamnose is made from glucose-1-phosphate and dTTP by four enzymes encoded by rmIA-D. An Escherichia coli rmIC mutant was constructed and a crude enzyme extract prepared from it did not produce dTDP-4-keto-rhamnose, in contrast to a crude enzyme extract prepared from a wild-type E. coli strain where small amounts of this intermediate were found after incubation with dTDP-glucose in the absence of NADPH. These results showed that dTDP-4-keto-rhamnose, the product of RmIC, exists as a free intermediate. Further, the Mycobacterium tuberculosis rmIC gene was expressed and incubation of the resulting purified M. tuberculosis RmIC enzyme with dTDP-4-keto-6-deoxyglucose resulted in the conversion of approximately 7% of dTDP-4-keto-6-deoxyglucose to dTDP-4-keto-rhamnose. The enzyme also allowed for the incorporation of two deuterium atoms from deuterium oxide solvent into dTDP-4-keto-glucose. Thus the rmIC gene encodes dTDP-4-keto-6-deoxyglucose epimerase capable of epimerizing at both C-3' and C-5'; this enzyme produces free dTDP-4-keto-rhamnose but the equilibrium of the 4-keto sugar nucleotides lies strongly on the side of the gluco configuration.  (+info)

The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1 are sufficient for both epimerization and binding of Ca2+. (4/698)

The industrially important polysaccharide alginate is composed of the two sugar monomers beta-D-mannuronic acid (M) and its epimer alpha-L-guluronic acid (G). In the bacterium Azotobacter vinelandii, the G residues originate from a polymer-level reaction catalyzed by one periplasmic and at least five secreted mannuronan C-5-epimerases. The secreted enzymes are composed of repeats of two protein modules designated A (385 amino acids) and R (153 amino acids). The modular structure of one of the epimerases, AlgE1, is A1R1R2R3A2R4. This enzyme has two catalytic sites for epimerization, each site introducing a different G distribution pattern, and in this article we report the DNA-level construction of a variety of truncated forms of the enzyme. Analyses of the properties of the corresponding proteins showed that an A module alone is sufficient for epimerization and that A1 catalyzed the formation of contiguous stretches of G residues in the polymer, while A2 introduces single G residues. These differences are predicted to strongly affect the physical and immunological properties of the reaction product. The epimerization reaction is Ca2+ dependent, and direct binding studies showed that both the A and R modules bind this cation. The R modules appeared to reduce the Ca2+ concentration needed for full activity and also stimulated the reaction rate when positioned both N and C terminally.  (+info)

Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. (5/698)

Sialuria is a rare inborn error of metabolism characterized by cytoplasmic accumulation and increased urinary excretion of free N-acetylneuraminic acid (NeuAc, sialic acid). Overproduction of NeuAc is believed to result from loss of feedback inhibition of uridinediphosphate-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac). We report the cloning and characterization of human UDP-GlcNAc 2-epimerase cDNA, with mutation analysis of three patients with sialuria. Their heterozygote mutations, R266W, R266Q, and R263L, indicate that the allosteric site of the epimerase resides in the region of codons 263-266. The heterozygous nature of the mutant allele in all three patients reveals a dominant mechanism of inheritance for sialuria.  (+info)

UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation. (6/698)

Modification of cell surface molecules with sialic acid is crucial for their function in many biological processes, including cell adhesion and signal transduction. Uridine diphosphate-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) is an enzyme that catalyzes an early, rate-limiting step in the sialic acid biosynthetic pathway. UDP-GlcNAc 2-epimerase was found to be a major determinant of cell surface sialylation in human hematopoietic cell lines and a critical regulator of the function of specific cell surface adhesion molecules.  (+info)

A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. (7/698)

The serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b) consists of D-fucose and L-rhamnose. Thymidine diphosphate (dTDP)-D-fucose is the activated nucleotide sugar form of D-fucose, which has been identified as a constituent of structural polysaccharides in only a few bacteria. In this paper, we show that three dTDP-D-fucose synthetic enzymes are encoded by genes in the gene cluster responsible for the synthesis of serotype b-specific polysaccharide in A. actinomycetemcomitans. The first and second steps of the dTDP-D-fucose synthetic pathway are catalyzed by D-glucose-1-phosphate thymidylyltransferase and dTDP-D-glucose 4,6-dehydratase, which are encoded by rmlA and rmlB in the gene cluster, respectively. These two reactions are common to the well studied dTDP-L-rhamnose synthetic pathway. However, the enzyme catalyzing the last step of the dTDP-D-fucose synthetic pathway has never been reported. We identified the fcd gene encoding a dTDP-4-keto-6-deoxy-D-glucose reductase. After purifying the three enzymes, their enzymatic activities were analyzed by reversed-phase high performance liquid chromatography. In addition, nuclear magnetic resonance analysis and gas-liquid chromatography analysis proved that the fcd gene product converts dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose. Moreover, kinetic analysis of the enzyme indicated that the Km values for dTDP-4-keto-6-deoxy-D-glucose and NADPH are 97.3 and 28.7 microM, respectively, and that the enzyme follows the sequential mechanism. This paper is the first report on the dTDP-D-fucose synthetic pathway and dTDP-4-keto-6-deoxy-D-glucose reductase.  (+info)

Decreased availability of GDP-L-fucose in a patient with LAD II with normal GDP-D-mannose dehydratase and FX protein activities. (8/698)

Leukocyte adhesion deficiency type II (LAD II) is caused by a disorder in the metabolism of GDP-L-fucose, which causes hypofucosylation of glycoconjugates. This study analyzes a newly identified LAD II patient who shows the same severe hypofucosylation of glycoconjugates as the other described patients. However, in vitro assays of cytosolic extracts from leukocytes and fibroblasts of the patient demonstrated a normal GDP-L-fucose biosynthesis from GDP-D-mannose. Analysis of the two enzymes involved in the pathway, GDP-D-mannose 4,6-dehydratase and FX protein, revealed normal numbers of transcripts without any detectable mutations within the coding regions of either gene. In contrast to previously published observations [Sturla et al. (1998) FEBS Lett. 429, 274-278], the major pathway of GDP-L-fucose synthesis can be normal in LAD II.  (+info)

Carbohydrate epimerases are a group of enzymes that catalyze the interconversion of specific stereoisomers (epimers) of carbohydrates by the reversible oxidation and reduction of carbon atoms, usually at the fourth or fifth position. These enzymes play important roles in the biosynthesis and modification of various carbohydrate-containing molecules, such as glycoproteins, proteoglycans, and glycolipids, which are involved in numerous biological processes including cell recognition, signaling, and adhesion.

The reaction catalyzed by carbohydrate epimerases involves the transfer of a hydrogen atom and a proton between two adjacent carbon atoms, leading to the formation of new stereochemical configurations at these positions. This process can result in the conversion of one epimer into another, thereby expanding the structural diversity of carbohydrates and their derivatives.

Carbohydrate epimerases are classified based on the type of substrate they act upon and the specific stereochemical changes they induce. Some examples include UDP-glucose 4-epimerase, which interconverts UDP-glucose and UDP-galactose; UDP-N-acetylglucosamine 2-epimerase, which converts UDP-N-acetylglucosamine to UDP-N-acetylmannosamine; and GDP-fucose synthase, which catalyzes the conversion of GDP-mannose to GDP-fucose.

Understanding the function and regulation of carbohydrate epimerases is crucial for elucidating their roles in various biological processes and developing strategies for targeting them in therapeutic interventions.

Racemases and epimerases are two types of enzymes that are involved in the modification of the stereochemistry of molecules, particularly amino acids and sugars. Here is a brief definition for each:

1. Racemases: These are enzymes that catalyze the interconversion of D- and L-stereoisomers of amino acids or other chiral compounds. They do this by promoting the conversion of one stereoisomer to its mirror image, resulting in a racemic mixture (a 1:1 mixture of two enantiomers). Racemases are important in various biological processes, such as the biosynthesis of some amino acids and the degradation of certain carbohydrates.

Example: Alanine racemase is an enzyme that catalyzes the conversion of L-alanine to D-alanine, which is essential for bacterial cell wall biosynthesis.

2. Epimerases: These are enzymes that convert one stereoisomer (epimer) of a chiral compound into another stereoisomer by changing the configuration at a single asymmetric carbon atom while keeping the rest of the molecule unchanged. Unlike racemases, epimerases do not produce racemic mixtures but rather create specific stereoisomers.

Example: Glucose-1-phosphate epimerase is an enzyme that converts glucose-1-phosphate to galactose-1-phosphate during the Leloir pathway, which is the primary metabolic route for lactose digestion in mammals.

Both racemases and epimerases play crucial roles in various biochemical processes, including the synthesis and degradation of essential molecules like amino acids and carbohydrates.

UDP-glucose 4-epimerase (UGE) is an enzyme that catalyzes the reversible interconversion of UDP-galactose and UDP-glucose, two important nucleotide sugars involved in carbohydrate metabolism. This enzyme plays a crucial role in maintaining the balance between these two molecules, which are essential for the synthesis of various glycoconjugates, such as glycoproteins and proteoglycans. UGE is widely distributed in nature and has been identified in various organisms, including humans. In humans, deficiency or mutations in this enzyme can lead to a rare genetic disorder known as galactosemia, which is characterized by an impaired ability to metabolize the sugar galactose, resulting in several health issues.

Carbohydrates are a major nutrient class consisting of organic compounds that primarily contain carbon, hydrogen, and oxygen atoms. They are classified as saccharides, which include monosaccharides (simple sugars), disaccharides (double sugars), oligosaccharides (short-chain sugars), and polysaccharides (complex carbohydrates).

Monosaccharides, such as glucose, fructose, and galactose, are the simplest form of carbohydrates. They consist of a single sugar molecule that cannot be broken down further by hydrolysis. Disaccharides, like sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar), are formed from two monosaccharide units joined together.

Oligosaccharides contain a small number of monosaccharide units, typically less than 20, while polysaccharides consist of long chains of hundreds to thousands of monosaccharide units. Polysaccharides can be further classified into starch (found in plants), glycogen (found in animals), and non-starchy polysaccharides like cellulose, chitin, and pectin.

Carbohydrates play a crucial role in providing energy to the body, with glucose being the primary source of energy for most cells. They also serve as structural components in plants (cellulose) and animals (chitin), participate in various metabolic processes, and contribute to the taste, texture, and preservation of foods.

Carbohydrate metabolism is the process by which the body breaks down carbohydrates into glucose, which is then used for energy or stored in the liver and muscles as glycogen. This process involves several enzymes and chemical reactions that convert carbohydrates from food into glucose, fructose, or galactose, which are then absorbed into the bloodstream and transported to cells throughout the body.

The hormones insulin and glucagon regulate carbohydrate metabolism by controlling the uptake and storage of glucose in cells. Insulin is released from the pancreas when blood sugar levels are high, such as after a meal, and promotes the uptake and storage of glucose in cells. Glucagon, on the other hand, is released when blood sugar levels are low and signals the liver to convert stored glycogen back into glucose and release it into the bloodstream.

Disorders of carbohydrate metabolism can result from genetic defects or acquired conditions that affect the enzymes or hormones involved in this process. Examples include diabetes, hypoglycemia, and galactosemia. Proper management of these disorders typically involves dietary modifications, medication, and regular monitoring of blood sugar levels.

Dietary carbohydrates refer to the organic compounds in food that are primarily composed of carbon, hydrogen, and oxygen atoms, with a general formula of Cm(H2O)n. They are one of the three main macronutrients, along with proteins and fats, that provide energy to the body.

Carbohydrates can be classified into two main categories: simple carbohydrates (also known as simple sugars) and complex carbohydrates (also known as polysaccharides).

Simple carbohydrates are made up of one or two sugar molecules, such as glucose, fructose, and lactose. They are quickly absorbed by the body and provide a rapid source of energy. Simple carbohydrates are found in foods such as fruits, vegetables, dairy products, and sweeteners like table sugar, honey, and maple syrup.

Complex carbohydrates, on the other hand, are made up of long chains of sugar molecules that take longer to break down and absorb. They provide a more sustained source of energy and are found in foods such as whole grains, legumes, starchy vegetables, and nuts.

It is recommended that adults consume between 45-65% of their daily caloric intake from carbohydrates, with a focus on complex carbohydrates and limiting added sugars.

"Plesiomonas" is a genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that are commonly found in aquatic environments. The most well-known species is Plesiomonas shigelloides, which is a potential human pathogen. It can cause gastroenteritis, with symptoms such as diarrhea, abdominal cramps, nausea, and vomiting. The bacteria are often transmitted through the consumption of contaminated food or water. However, it's worth noting that Plesiomonas infections are relatively rare and are more commonly seen in tropical and subtropical regions.

'Azotobacter vinelandii' is a species of free-living, nitrogen-fixing bacteria that is commonly found in soil and freshwater environments. The name 'Azotobacter' comes from the Greek words "azoto," meaning "nitrogen," and "bakterion," meaning "rod" or "staff," while "vinelandii" refers to Vineland, New Jersey, where the bacterium was first isolated.

'Azotobacter vinelandii' is known for its ability to convert atmospheric nitrogen gas (N2) into ammonia (NH3), a process called nitrogen fixation. This makes it an important contributor to the global nitrogen cycle and a valuable tool in agricultural and industrial applications.

In addition to its nitrogen-fixing abilities, 'Azotobacter vinelandii' is also known for its resistance to desiccation, high tolerance to oxygen levels, and ability to produce various extracellular polysaccharides and enzymes. These characteristics make it a popular model organism for studying bacterial metabolism, stress responses, and genetic regulation.

Overall, 'Azotobacter vinelandii' is a fascinating and important microorganism with significant implications for our understanding of the nitrogen cycle, environmental biology, and potential industrial applications.

Iduronic acid is a type of uronic acid, which is a derivative of glucose. It is a component of certain complex carbohydrates known as glycosaminoglycans (GAGs) or mucopolysaccharides, which are found in the extracellular matrix and on the surface of cells in the body. Specifically, iduronic acid is a component of dermatan sulfate and heparan sulfate, two types of GAGs that play important roles in various biological processes such as cell signaling, growth factor regulation, and blood clotting.

Iduronic acid has an unusual structure compared to other sugars because it contains a five-membered ring instead of the more common six-membered ring found in most other sugars. This unique structure allows iduronic acid to form complex structures with other sugar molecules, which is important for the biological activity of GAGs.

Abnormalities in the metabolism of iduronic acid and other GAG components can lead to various genetic disorders known as mucopolysaccharidoses (MPS), which are characterized by a range of symptoms including developmental delays, coarse facial features, skeletal abnormalities, and cardiac problems.

Hexuronic acids are a type of uronic acid that contains six carbon atoms and is commonly found in various biological tissues and polysaccharides, such as pectins, heparin, and certain glycoproteins. The most common hexuronic acids are glucuronic acid and iduronic acid, which are formed from the oxidation of the corresponding hexoses, glucose and galactose, respectively. Hexuronic acids play important roles in various biological processes, including the detoxification and excretion of xenobiotics, the formation of proteoglycans, and the regulation of cell growth and differentiation.

Uronic acids are a type of organic compound that are carboxylic acids derived from sugars (carbohydrates). They are formed by the oxidation of the primary alcohol group (-CH2OH) on a pentose sugar, resulting in a carboxyl group (-COOH) at that position.

The most common uronic acid is glucuronic acid, which is derived from glucose. Other examples include galacturonic acid (derived from galactose), iduronic acid (derived from glucose or galactose), and mannuronic acid (derived from mannose).

Uronic acids play important roles in various biological processes, such as the formation of complex carbohydrates like glycosaminoglycans, which are major components of connective tissues. They also serve as important intermediates in the metabolism of sugars and other carbohydrates.

Glucuronic acid is a physiological important organic acid, which is a derivative of glucose. It is formed by the oxidation of the primary alcohol group of glucose to form a carboxyl group at the sixth position. Glucuronic acid plays a crucial role in the detoxification process in the body as it conjugates with toxic substances, making them water-soluble and facilitating their excretion through urine or bile. This process is known as glucuronidation. It is also a component of various polysaccharides, such as heparan sulfate and chondroitin sulfate, which are found in the extracellular matrix of connective tissues.

A "carbohydrate sequence" refers to the specific arrangement or order of monosaccharides (simple sugars) that make up a carbohydrate molecule, such as a polysaccharide or an oligosaccharide. Carbohydrates are often composed of repeating units of monosaccharides, and the sequence in which these units are arranged can have important implications for the function and properties of the carbohydrate.

For example, in glycoproteins (proteins that contain carbohydrate chains), the specific carbohydrate sequence can affect how the protein is processed and targeted within the cell, as well as its stability and activity. Similarly, in complex carbohydrates like starch or cellulose, the sequence of glucose units can determine whether the molecule is branched or unbranched, which can have implications for its digestibility and other properties.

Therefore, understanding the carbohydrate sequence is an important aspect of studying carbohydrate structure and function in biology and medicine.

Alginates are a type of polysaccharide derived from brown algae or produced synthetically, which have gelling and thickening properties. In medical context, they are commonly used as a component in wound dressings, dental impressions, and bowel cleansing products. The gels formed by alginates can provide a protective barrier to wounds, help maintain a moist environment, and promote healing. They can also be used to create a mold of the mouth or other body parts in dental and medical applications. In bowel cleansing, sodium alginates are often combined with sodium bicarbonate and water to form a solution that expands and stimulates bowel movements, helping to prepare the colon for procedures such as colonoscopy.

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.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Carbohydrate conformation refers to the three-dimensional shape and structure of a carbohydrate molecule. Carbohydrates, also known as sugars, can exist in various conformational states, which are determined by the rotation of their component bonds and the spatial arrangement of their functional groups.

The conformation of a carbohydrate molecule can have significant implications for its biological activity and recognition by other molecules, such as enzymes or antibodies. Factors that can influence carbohydrate conformation include the presence of intramolecular hydrogen bonds, steric effects, and intermolecular interactions with solvent molecules or other solutes.

In some cases, the conformation of a carbohydrate may be stabilized by the formation of cyclic structures, in which the hydroxyl group at one end of the molecule forms a covalent bond with the carbonyl carbon at the other end, creating a ring structure. The most common cyclic carbohydrates are monosaccharides, such as glucose and fructose, which can exist in various conformational isomers known as anomers.

Understanding the conformation of carbohydrate molecules is important for elucidating their biological functions and developing strategies for targeting them with drugs or other therapeutic agents.

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.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

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.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

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.

Tumor-associated carbohydrate antigens (TACAs) are a type of tumor antigen that are expressed on the surface of cancer cells. These antigens are abnormal forms of carbohydrates, also known as glycans, which are attached to proteins and lipids on the cell surface.

TACAs are often overexpressed or expressed in a different form on cancer cells compared to normal cells. This makes them attractive targets for cancer immunotherapy because they can be recognized by the immune system as foreign and elicit an immune response. Some examples of TACAs include gangliosides, fucosylated glycans, and sialylated glycans.

Tumor-associated carbohydrate antigens have been studied as potential targets for cancer vaccines, antibody therapies, and other immunotherapeutic approaches. However, their use as targets for cancer therapy is still in the early stages of research and development.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

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.

It belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. ... Other names in common use include phosphoribulose isomerase, ribulose phosphate 4-epimerase, L-ribulose-phosphate 4-epimerase, ... In enzymology, a L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) is an enzyme that catalyzes the interconversion of ribulose 5- ... Ribulose 5-phosphate 4-epimerase is found on the well studied L-arabinose operon. This operon consists of eight genes araA-araH ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Other names in common use include UDP acetylglucosamine epimerase, uridine diphosphoacetylglucosamine epimerase, uridine ... In enzymology, an UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7) is an enzyme that catalyzes the chemical reaction UDP-N- ... The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine 4-epimerase. ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... epimerase, uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This ... The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity. As of late 2007, 4 ... UDP-N-acetylglucosamine 2-epimerase (hydrolysing) Not to be confused with N-acetylglucosamine 2-epimerase Swartley JS, Liu LJ, ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Other names in common use include uridine diphosphoglucuronate 5'-epimerase, UDP-glucuronic acid 5'-epimerase, and C-5-uronosyl ... In enzymology, an UDP-glucuronate 5'-epimerase (EC 5.1.3.12) is an enzyme that catalyzes the chemical reaction UDP-glucuronate ... I. Uridine diphosphate-D-glucuronic acid-5-epimerase". The Journal of Biological Chemistry. 237 (3): 638-42. doi:10.1016/S0021- ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... In enzymology, an ADP-L-glycero-D-manno-heptose 6-epimerase (EC 5.1.3.20) is an enzyme that catalyzes the chemical reaction ADP ... The systematic name of this enzyme class is ADP-L-glycero-D-manno-heptose 6-epimerase. This enzyme participates in ... "The Mechanism of the Reaction Catalyzed by ADP-β-L-glycero-D-manno-heptose 6-Epimerase". J. Am. Chem. Soc. 126 (29): 8878-9. ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... The systematic name of this enzyme class is UDP-glucosamine 4-epimerase. MALEY F, MALEY GF (1959). "The enzymic conversion of ... In enzymology, an UDP-glucosamine 4-epimerase (EC 5.1.3.16) is an enzyme that catalyzes the chemical reaction UDP-glucosamine ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... UDP-galacturonate 4-epimerase, uridine diphosphoglucuronate epimerase, and UDP-D-galacturonic acid 4-epimerase. This enzyme ... The systematic name of this enzyme class is UDP-glucuronate 4-epimerase. Other names in common use include uridine diphospho-D- ... galacturonic acid, UDP glucuronic epimerase, uridine diphosphoglucuronic epimerase, ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... In enzymology, an aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction alpha-D-glucose ⇌ {\ ... The systematic name of this enzyme class is aldose 1-epimerase. Other names in common use include mutarotase, and aldose ...
This enzyme belongs to the isomerase family, specifically those racemases and epimerases which act on carbohydrates and their ... phosphoketopentose 3-epimerase, xylulose phosphate 3-epimerase, phosphoketopentose epimerase, ribulose 5-phosphate 3-epimerase ... Phosphopentose epimerase (also known as ribulose-phosphate 3-epimerase and ribulose 5-phosphate 3-epimerase, EC 5.1.3.1) ... D-ribulose 5-phosphate epimerase, D-ribulose-5-P 3-epimerase, D-xylulose-5-phosphate 3-epimerase, and pentose-5-phosphate 3- ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... The systematic name of this enzyme class is maltose 1-epimerase. Shirokane Y, Suzuki M (1995). "A novel enzyme, maltose 1- ... In enzymology, a maltose epimerase (EC 5.1.3.21) is an enzyme that catalyzes the chemical reaction alpha-maltose ⇌ {\ ... epimerase from Lactobacillus brevis IFO 3345". FEBS Lett. 367 (2): 177-9. doi:10.1016/0014-5793(95)00524-D. PMID 7796915. ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... In enzymology, a glucose-6-phosphate 1-epimerase (EC 5.1.3.15) is an enzyme that catalyzes the chemical reaction alpha-D- ... Wurster B, Hess B (1972). "Glucose-6-phosphate-1-epimerase from baker's yeast. A new enzyme". FEBS Lett. 23 (3): 341-344. doi: ... The systematic name of this enzyme class is D-glucose-6-phosphate 1-epimerase. This enzyme participates in glycolysis / ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... 5-epimerase, TDP-4-ketorhamnose 3,5-epimerase, dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase, and TDP-4-keto-L-rhamnose-3,5- ... The systematic name of this enzyme class is dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase. Other names in common use include ... In enzymology, a dTDP-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) is an enzyme that catalyzes the chemical reaction dTDP-4- ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Other names in common use include polyglucuronate 5-epimerase, dermatan-sulfate 5-epimerase, urunosyl C-5 epimerase, and ... Assay and properties of the uronosyl C-5 epimerase". Biochem. J. 201 (3): 489-93. doi:10.1042/bj2010489. PMC 1163673. PMID ... In enzymology, a chondroitin-glucuronate 5-epimerase (EC 5.1.3.19) is an enzyme that catalyzes the chemical reaction ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... The systematic name of this enzyme class is L-ribulose-5-phosphate 3-epimerase. Other names in common use include L-xylulose 5- ... In enzymology, a L-ribulose-5-phosphate 3-epimerase (EC 5.1.3.22) is an enzyme that catalyzes the chemical reaction L-ribulose ... phosphate 3-epimerase, UlaE, and SgaU. This enzyme participates in ascorbate and aldarate metabolism. Yew WS, Gerlt JA (2002 ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Other names in common use include acylglucosamine 2-epimerase, and N-acetylglucosamine 2-epimerase. This enzyme participates in ... They show that the N-acylglucosamine 2-epimerase monomer folds as a barrel composed of α-helices, in a manner known as (α/α)6- ... In enzymology, a N-acylglucosamine 2-epimerase (EC 5.1.3.8) is an enzyme that catalyzes the chemical reaction N-acyl-D- ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... Other names in common use include acylglucosamine-6-phosphate 2-epimerase, and acylglucosamine phosphate 2-epimerase. This ... In enzymology, a N-acylglucosamine-6-phosphate 2-epimerase (EC 5.1.3.9) is an enzyme that catalyzes the chemical reaction N- ... N-Acyl--D-Glucosamine 6-Phosphate 2-Epimerase". The Journal of Biological Chemistry. 240: 1525-30. doi:10.1016/S0021-9258(18) ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... cytidine diphosphodideoxyglucose epimerase, cytidine diphosphoparatose epimerase, and cytidine diphosphate paratose-2-epimerase ... It is also incorrectly known as CDP-abequose epimerase, and CDP-D-abequose 2-epimerase. This enzyme participates in starch and ... Other names in common use include CDP-paratose epimerase, cytidine diphosphoabequose epimerase, ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and ... UDP arabinose epimerase, uridine 5'-diphosphate-D-xylose 4-epimerase, and UDP-D-xylose 4-epimerase. This enzyme participates in ... In enzymology, an UDP-arabinose 4-epimerase (EC 5.1.3.5) is an enzyme that catalyzes the chemical reaction UDP-L-arabinose ⇌ {\ ... The systematic name of this enzyme class is UDP-L-arabinose 4-epimerase. Other names in common use include uridine ...
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and their ... The systematic name of this enzyme class is cellobiose 2-epimerase. Enzymes like these can produce a more rapid syndrome that ... In enzymology a cellobiose epimerase (EC 5.1.3.11) is an enzyme that catalyzes the chemical reaction cellobiose ⇌ {\ ...
... the 1970 Nobel Prize in Chemistry for his discovery of sugar nucleotides and their role in the biosynthesis of carbohydrates. ... The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase ... GeneReviews/NCBI/NIH/UW entry on Epimerase Deficiency Galactosemia OMIM entries on Epimerase Deficiency Galactosemia ... Liu Y, Vanhooke JL, Frey PA (June 1996). "UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band associated with ...
... is caused a lack of the enzyme uridine diphosphate galactose-4-epimerase which breaks down a byproduct of galactose. This type ... Carbohydrates account for a major portion of the human diet. These carbohydrates are composed of three principal ... Inborn errors of carbohydrate metabolism are inborn error of metabolism that affect the catabolism and anabolism of ... The metabolic pathway glycolysis is used by cells to break down carbohydrates like glucose (and various other simple sugars) in ...
... specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class ... This also means that the GDP-mannose 3,5-epimerase has three reaction products, namely the main product GDP-L-galactose (C3,5- ... In enzymology, a GDP-mannose 3,5-epimerase (EC 5.1.3.18) is an enzyme that catalyzes the chemical reaction GDP-mannose ⇌ {\ ... Other names in common use include GDP-D-mannose:GDP-L-galactose epimerase, guanosine 5'-diphosphate D-mannose:guanosine 5'- ...
... carbohydrate epimerases MeSH D08.811.399.894.500.700 - UDP-glucose 4-epimerase MeSH D08.811.464.257.050 - acetyl-coa ... carbohydrate dehydrogenases MeSH D08.811.682.047.150.225 - fructuronate reductase MeSH D08.811.682.047.150.250 - galactose ...
... permethylated carbohydrate moiety as "nogalose", more recent data suggest that the nogalose moiety on nogalamycin is methylated ... 5-epimerase) snogH (2,3-dehydratase) snogN (unknown) snogI (aminotransferase) snogG (ketoreductase) snogC (ketoreductase) snogA ...
The enzyme plays an essential role in the carbohydrate metabolism. Mutations in this gene cause ribose 5-phosphate isomerase ... Dickens F, Williamson DH (November 1956). "Pentose phosphate isomerase and epimerase from animal tissues". The Biochemical ... the conversion of carbon dioxide and water into carbohydrates. RPIA is essential in the cycle, as Ru5P generated from R5P is ... RPIA converts Ru5P to R5P which then is converted by ribulose-phosphate 3-epimerase to xylulose-5-phosphate (figure 3). The end ...
When the GNE epimerase kinase does not function correctly in the human body thereby reducing the available ManNAc, it is ... terminal monosaccharides of carbohydrate chains that are attached to glycoproteins and glycolipids (glycans). ManNAc is the ... In the rate-limiting step of the pathway, UDP-GlcNAc is converted into ManNAc by UDP-GlcNAc 2-epimerase, encoded by the ... The UDP-GlcNAc 2-epimerase kinase is the rate limiting step in sialic acid biosynthesis. If the enzyme does not work ...
"The Development of Carbohydrate Chemistry and Biology". Carbohydrate Chemistry, Biology and Medical Applications: 1-28. doi: ... is a congenital disease resulted from altered function of UDP-GlcNAc epimerase . Macular corneal dystrophy: is a congenital ... Carbohydrate chemistry EamA Glycorandomization Glycosyltransferase Nucleotide sugars metabolism Derek Horton (2008). " ...
The sub-categories of isomerases containing racemases, epimerases and cis-trans isomers are examples of enzymes catalyzing the ... Isomerases catalyze reactions across many biological processes, such as in glycolysis and carbohydrate metabolism. Examples of ... Racemases act upon molecules with one chiral carbon for inversion of stereochemistry, whereas epimerases target molecules with ... and epimerases). These isomerases invert stereochemistry at the target chiral carbon. ...
Many ruminant animals form a large amount of 3-carbon propionate during the fermentation of carbohydrates in the rumen. Long- ... However, the D conformation is enzymatically converted into the L conformation by methylmalonyl-CoA epimerase, then it ... but instead use carbohydrates (red blood cells and neurons) or ketone bodies (neurons only). Because many fatty acids are not ...
... and epimerase deficiency with glucose.[citation needed] Accumulated galactose can also undergo an alternative reaction: ... the accumulation of galactose becomes the substrate for enzymes that catalyze the polyol pathway of carbohydrate metabolism. ... Dysmetria Diminished bone density Premature ovarian failure Cataract Galactosemic cataract Other Inborn errors of carbohydrate ...
Aldose-Ketose Isomerases, Base Sequence, Carbohydrate Epimerases, Ethanol, Fermentation, Genes, Bacterial, Molecular Sequence ... Carbohydrate Epimerases; Ethanol; Fermentation; Genes, Bacterial; Molecular Sequence Data; Phosphoglycerate Kinase; Recombinant ...
It belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. ... Other names in common use include phosphoribulose isomerase, ribulose phosphate 4-epimerase, L-ribulose-phosphate 4-epimerase, ... In enzymology, a L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) is an enzyme that catalyzes the interconversion of ribulose 5- ... Ribulose 5-phosphate 4-epimerase is found on the well studied L-arabinose operon. This operon consists of eight genes araA-araH ...
2020) Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases. ... Carbohydrate bioengineering meeting , Toulouse 2019-05-19 - 2019-05-22 ... 2020) Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases. ... 2018) Using alginate epimerases as a basis to understand polymer and protein design. Norwegian Biochemical Society Norwegian ...
5.1 Racemases and epimerases. 5.1.3 Acting on carbohydrates and derivatives. 5.1.3.1 ribulose-phosphate 3-epimerase. 4331761. ... 5.1 Racemases and epimerases. 5.1.3 Acting on carbohydrates and derivatives. 5.1.3.1 ribulose-phosphate 3-epimerase. 4347508. ... 09101 Carbohydrate metabolism. 00030 Pentose phosphate pathway. 4331761. 00040 Pentose and glucuronate interconversions. ... 09101 Carbohydrate metabolism. 00030 Pentose phosphate pathway. 4347508. 00040 Pentose and glucuronate interconversions. ...
... group A carbohydrate biosynthetic genes (putative functions described in van Sorge et al. [1]); gccA-N, group C carbohydrate ... gccM and gccN putatively encode an additional glycosyl transferase and UDP-monosaccharide 4-epimerase, respectively; ebsA, pore ... Structure of the streptococcal groups A, A-variant and C carbohydrates. Immunochemistry. 1978;15:755-60. DOIPubMedGoogle ... The 3 genes required for inclusion of the immunodominant N-acetylglucosamine side chain within the group A carbohydrate (gacI, ...
2] "Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) ...
The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer Acta ... Carbohydrate Research 2015 DOI. * Man Kumari Gurung, Inger Lin Uttakleiv Ræder, Bjørn Altermark, Arne O. Smalås : ...
Carbohydrate Epimerases * Carboxy-Lyases * Clostridium Botulinum * Cluster Analysis * Crystallography, X-Ray * Databases, ...
F:aldose 1-epimerase activity;P:galactose metabolic process, hexose metabolic process, carbohydrate metabolic process;C: ... pfkB-type carbohydrate kinase family protein. F:kinase activity, ribokinase activity;P:D-ribose metabolic process;C:cellular_ ...
... carbohydrate-related differential expressed genes; 6PGDH: 6-phosphogluconate dehydrogenase; RPE: ribulose-phosphate 3-epimerase ... Differential expression of carbohydrate-related genes in rapeseed, castor bean, and maize during seed development ... Lipid- and carbohydrate-related Arabidopsis genes were cited from the published data [38, 3]. Venn diagram analyses were ... Other carbohydrate metabolic pathways were up-regulated in castor bean and maize, while sucrose metabolism and sugar transport ...
racemase and epimerase activity, acting on carbohydrates and derivatives. IEP. Enrichment. BP. GO:0019219. regulation of ...
racemase and epimerase activity. IEP. Neighborhood. MF. GO:0016857. racemase and epimerase activity, acting on carbohydrates ... Carbohydrate metabolism.nucleotide sugar.... 0.02. Archaeplastida. Solyc04g051200.2.1. No alias. UDP-L-arabinose mutase. 0.04. ...
racemase and epimerase activity, acting on carbohydrates and derivatives. IEP. Enrichment. MF. GO:0016881. acid-amino acid ... racemase and epimerase activity. IEP. Enrichment. MF. GO:0016856. racemase and epimerase activity, acting on hydroxy acids and ...
racemase and epimerase activity. IEP. Neighborhood. MF. GO:0016857. racemase and epimerase activity, acting on carbohydrates ...
IBS is characterized by a multi-omics microbial signature indicating increased capacity to utilize fermentable carbohydrates- ... upregulation of enzymes involved in fructose and glucan metabolism as well as the succinate pathway of carbohydrate ... production of propionic acid in Escherichia coli through the sbm operon requires the activity of a methylmalonyl-CoA epimerase ... IBS-D also had increased levels of intermediates of the succinate pathway of carbohydrate fermentation including fumarate and ...
","L-fuculokinase [Ensembl]. N-terminal domain, C-terminal domain, FGGY family of carbohydrate kinases [InterProScan]."," ... ","Poly(beta-D-mannuronate) C5 epimerase precursor [Ensembl]. Periplasmic copper-binding protein (NosD) [Interproscan]."," ... ","hypothetical protein [Ensembl]. SGNH hydrolase-like domain, C-terminal carbohydrate-binding module [Interproscan].","protein ...
N2 - Sialic acid is a major determinant of carbohydrate-receptor interactions in many systems pertinent to human health and ... UDP-GlcNAc 2-epimerase and GlcNAc 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc, ... UDP-GlcNAc 2-epimerase and GlcNAc 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc, ... UDP-GlcNAc 2-epimerase and GlcNAc 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc, ...
UDP-glucuronate 4-epimerase activity, catalytic activity; INVOLVED IN: cellular metabolic process, carbohydrate metabolic ... UDP-D-glucuronate 4-epimerase 3. Curator Summary. Encodes a putative membrane-anchored UDP-D-glucuronate 4-epimerase.. ... Nucleotide sugar epimerase (InterPro:IPR008089); BEST Arabidopsis thaliana protein match is: UDP-D-glucuronate 4-epimerase 2 ( ... AT4G00110.1 - [+] show detail - UDP-D-glucuronate 4-epimerase 3 Distance: 0; Region: exon1 (5UTR) ...
It is caused by pathogenic variants in the carbohydrate sulfotransferase 14 gene (mcEDS-CHST14) or in the dermatan sulfate ... epimerase gene (mcEDS-DSE). As gastrointestinal complications of mcEDS-CHST14, diverticula in the colon, small intestine, or ...
In 2020, his team solved the first structure of the human carbohydrate-modifing enzyme dermatan sulfate epimerase 1, known to ... He has studied a range of human carbohydrate (glycosaminoglycan)-modifing enzymes and his work has covered many aspects of ...
Hereditary galactosemia is among the most common carbohydrate metabolism disorders and can be a life-threatening illness during ... Uridine diphosphate (UDP) galactose-4-epimerase epimerizes UDP galactose to UDP glucose and is also uncommon. [13] ... Hereditary galactosemia is among the most common carbohydrate metabolism disorders and can be a life-threatening illness during ... GALM (glactose mutorotase, aldose1-epimerase) catalyzes the interconversion of the alpha and the beta anomers of hexose sugars ...
racemase and epimerase activity, acting on carbohydrates and derivatives fucose binding It has to be done as per old AB ...
The 5‐carbon, doubly phosphorylated carbohydrate, ribulose bisphosphate is the acceptor for CO 2; the enzyme is called ribulose ... The 5‐carbon sugar phosphates are interconverted by the action of epimerase and isomerase to yield ribulose‐5‐phosphate, which ... The rest of the Calvin cycle is involved in interconversion of carbohydrates to make glucose (or starch) and the regeneration ... The 5‐carbon, doubly phosphorylated carbohydrate, ribulose bi ...
Carbohydrate kinase, FGGY family cluster with sorbitoldehydrogenase. Mjls_2814. Mjls_2814. ribulose-phosphate 3-epimerase ...
Regarding carbohydrate metabolism, in T1, of the genes involved in carbohydrate metabolism, most are those involved in the ... and glucose-6-phosphate 1-epimerase also are present (5.1.3.15-9.3%). The oxalate decarboxylase is involved in glyoxylate ... The cocoa pulp is rich in simple carbohydrates (glucose and fructose), and sucrose (Verse Herrera-Rocha et al., 2021). The fact ... The abundance of genes related to lipids metabolism is evident in T2 followed by genes related to carbohydrate metabolism in T3 ...
Amino Acid Sequence, Base Sequence, Blotting, Southern, Carbohydrate Epimerases, DNA, Bacterial, Electrophoresis, Gel, Pulsed- ...
Acetylglucosaminidase, Beta-Globulins, Carbohydrate Epimerases, Chromosome Mapping, Chromosomes, Human, 13-15, Genes, Genetic ...
Kishnani PS, Chen Y-T. Defects in metabolism of carbohydrates. In: Kliegman RM, St. Geme JW, Blum NJ, Shah SS, Tasker RC, ... Deficiency of galactose-6-phosphate epimerase (GALE). People with galactosemia are unable to fully break down the simple sugar ... Galactose-1-phosphate uridyl transferase deficiency; Galactokinase deficiency; Galactose-6-phosphate epimerase deficiency; GALT ... GALK; GALE; Epimerase deficiency galactosemia; GALE deficiency; Galactosemia type III; UDP-galactose-4; Duarte variant ...
  • Uridine diphosphate (UDP) galactose-4-epimerase epimerizes UDP galactose to UDP glucose and is also uncommon. (medscape.com)
  • GALM (glactose mutorotase, aldose1-epimerase) catalyzes the interconversion of the alpha and the beta anomers of hexose sugars like glucose and galactose and is not common. (medscape.com)
  • Carbohydrate intolerances with early onset and genetic cause include congenital sucrase-isomaltase deficiency (CSID), glucose-galactose malabsorption (GGM) and congenital lactase deficiency (CLD). (blueprintgenetics.com)
  • As an example, glucose-based carbohydrates appear effective in restoring muscle glycogen but are less effective in restoring liver glycogen compared to other sugars such as fructose and galactose (Gonzalez et al. (theiopn.com)
  • Next, the enzyme galactose 1-phosphate uridyltransferase (GALT) converts galactose 1-phosphate to UDP-galactose which is finally converted to UDP-glucose via the enzyme UDP galactose-4′-epimerase (GALE). (theiopn.com)
  • This operon consists of eight genes araA-araH with the gene for Ribulose 5-phosphate 4-epimerase called araD. (wikipedia.org)
  • The 3 genes required for inclusion of the immunodominant N- acetylglucosamine side chain within the group A carbohydrate ( gacI, gacJ , and gacK ) are shown in red. (cdc.gov)
  • gacA-L , group A carbohydrate biosynthetic genes (putative functions described in van Sorge et al. (cdc.gov)
  • gccA-N , group C carbohydrate biosynthetic genes. (cdc.gov)
  • 2] "Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-epimerase. (tcdb.org)
  • Transcriptome analyses showed that more than 61% of the lipid- and carbohydrate-related genes were regulated in rapeseed and castor bean, but only 20.1% of the lipid-related genes and 22.5% of the carbohydrate-related genes were regulated in maize. (researchsquare.com)
  • It belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. (wikipedia.org)
  • Encodes a putative membrane-anchored UDP-D-glucuronate 4-epimerase. (riken.jp)
  • In enzymology, a L-ribulose-5-phosphate 4-epimerase (EC 5.1.3.4) is an enzyme that catalyzes the interconversion of ribulose 5-phosphate and xylulose 5-phosphate in the oxidative phase of the Pentose phosphate pathway. (wikipedia.org)
  • Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis. (mpg.de)
  • IBS is characterized by a multi-omics microbial signature indicating increased capacity to utilize fermentable carbohydrates-consistent with the clinical benefit of diets restricting this energy source-that also includes multiple previously unrecognized metabolites and metabolic pathways. (biomedcentral.com)
  • Our results indicate that, unlike UDP-GlcNAc 2-epimerase, which promotes biosynthesis of sialic acid, GlcNAc 2-epimerase can serve a catabolic role, diverting metabolic flux away from the sialic acid pathway. (johnshopkins.edu)
  • Xylans are defined as carbohydrate polymers consisting of a β-1,4-xylosyl (Xyl p ) backbone, although xylans containing a β-1,3 and mixed linkage β-1,4-1,3 backbone structure have been found in algal species [ 9 ]. (biomedcentral.com)
  • This is consistent with the notion that both enzymes belong to a superfamily of epimerases/aldolases that catalyze carbon-carbon bond cleavage reactions via a metal-stabilized enolate intermediate. (wikipedia.org)
  • L-Ribulose-5-phosphate 4-epimerase and L-fuculose-1-phosphate (L-Fuc1P) aldolase are evolutionarily related enzymes that display 26% sequence identity and a very high degree of structural similarity. (wikipedia.org)
  • IBS further showed transcriptional upregulation of enzymes involved in fructose and glucan metabolism as well as the succinate pathway of carbohydrate fermentation. (biomedcentral.com)
  • UDP-GlcNAc 2-epimerase and GlcNAc 2-epimerase are two enzymes capable of generating ManNAc from UDP-GlcNAc and GlcNAc, respectively. (johnshopkins.edu)
  • Carbohydrate metabolism.nucleotide sugar. (ntu.edu.sg)
  • The 5‐carbon sugar phosphates are interconverted by the action of epimerase and isomerase to yield ribulose‐5‐phosphate, which is phosphorylated by the enzyme ribulose phosphate kinase to make RuBP, the acceptor of CO 2 . (cliffsnotes.com)
  • 5'-monophosphate deaminase from Streptomyces murinus, D-allulose 3-epimerase from Arthrobacter globiformis expressed in Escherichia coli , carbohydrate-derived fulvic acid, jagua (genipin-glycine) blue (Jagua blue), lipase from Mucor javanicus and phosphatidylinositol-specific phospholipase C expressed in Pseudomonas fluorescens ). (who.int)
  • It is caused by pathogenic variants in the carbohydrate sulfotransferase 14 gene (mcEDS-CHST14) or in the dermatan sulfate epimerase gene (mcEDS-DSE). (bvsalud.org)
  • Consequently, we present here an optimized poly-LacNAc synthesis by the combination of two glycosyltransferases and a uridine-diphospho-glucose/N-acetylglucosamine 4'-epimerase as one-pot strategy resulting in long poly-LacNAc glycans with up to six LacNAc units in high yields while minimizing reaction time and product loss. (uni-koeln.de)
  • The systematic name of this enzyme class is L-ribulose-5-phosphate 4-epimerase. (wikipedia.org)
  • Other names in common use include phosphoribulose isomerase, ribulose phosphate 4-epimerase, L-ribulose-phosphate 4-epimerase, L-ribulose 5-phosphate 4-epimerase, AraD, and L-Ru5P. (wikipedia.org)
  • Mechanism of ribulose 5-phosphate 4-epimerase in active site Aldol and dehydration mechanisms L-Ribulose 5-phosphate 4-epimerase catalyzes the epimerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate by retro-aldol cleavage and subsequent aldol reaction. (wikipedia.org)
  • First, the retro-aldol cleavage mechanism is analogous to the reaction catalyzed by L-fuculose-phosphate aldolase which has high levels of sequence similarity with L-ribulose-5-phosphate 4-epimerase. (wikipedia.org)
  • Ribulose 5-phosphate 4-epimerase is found on the well studied L-arabinose operon. (wikipedia.org)
  • The rest of the Calvin cycle is involved in interconversion of carbohydrates to make glucose (or starch) and the regeneration of the ribulose‐bisphosphate acceptor. (cliffsnotes.com)
  • Re-expression of glucuronyl C5-epimerase in the mutant MEF cells increases heparan sulfate epimerization but has no influence on the Golgi localization and enzymatic activity of 2-O-sulfotransferase. (uu.se)
  • N-terminal domain, C-terminal domain, FGGY family of carbohydrate kinases [InterProScan]. (ntu.edu.sg)
  • Accepted August 23, 2012 ABSTRACT The catabolite control protein CcpA is a pleiotropic regulator that mediates the global transcriptional response to rapidly catabolizable carbohydrates, like glucose in Gram-positive bacteria. (studyres.com)
  • Hereditary galactosemia is among the most common carbohydrate metabolism disorders and can be a life-threatening illness during the newborn period. (medscape.com)
  • Poly-N-acetyllactosamine (Poly-LacNAc, [3Gal beta 1,4GlcNAc beta 1](n)) glycans play an essential role in carbohydrate-protein interactions. (uni-koeln.de)
  • Proteoglycans are complex macromolecules comprised of a core protein and one or more covalently attached glycosaminoglycans (GAG) chains so that structurally they are both proteins and carbohydrates. (openbiochemistryjournal.com)
  • Transformed potato plants as a model for studying the hormonal and carbohydrate regulation of tuberization. (mpg.de)
  • Belongs to the N-acylglucosamine 2-epimerase family. (expasy.org)
  • Chitin is a biological polymer consisting of carbohydrate molecules bonded together to form long chains of polysaccharides. (biomedcentral.com)
  • Sialic acid is a major determinant of carbohydrate-receptor interactions in many systems pertinent to human health and disease. (johnshopkins.edu)
  • Developmental analysis of carbohydrate metabolism in tomato (Lycopersicon esculentum cv. (mpg.de)
  • Obiadalla-Ali, H. , Fernie, A. R. , Kossmann, J. & Lloyd, J. R. Developmental analysis of carbohydrate metabolism in tomato (Lycopersicon esculentum cv. (mpg.de)
  • Here we study the effects of GlcNAc 2-epimerase expression on sialic acid production in cells. (johnshopkins.edu)
  • A key tool we developed for this study is a cell-permeable, small molecule inhibitor of GlcNAc 2-epimerase designed based on mechanistic principles. (johnshopkins.edu)
  • Inhibition of chloroplastic fructose 1,6-bisphosphatase in tomato fruits leads to decreased fruit size, but only small changes in carbohydrate metabolism. (mpg.de)