Galactosyltransferases
N-Acetyllactosamine Synthase
Lactose Synthase
Galactose
Carbohydrate Sequence
Molecular Sequence Data
Substrate Specificity
Sequence Homology, Amino Acid
Amino Acid Sequence
Cloning, Molecular
Glycosylation
Encyclopedias as Topic
Glycosyltransferases
beta-N-Acetylglucosaminylglycopeptide beta-1,4-Galactosyltransferase
Purification and characterization of an alpha-galactosyltransferase from Trypanosoma brucei. (1/1005)
A membrane-associated galactosyltransferase from Trypanosoma brucei was purified 34000-fold by affinity chromatography on UDP-hexanolamine-Sepharosetrade mark. Using SDS/PAGE under reducing conditions, the isolated enzyme ran as a relatively broad band with apparent molecular masses of 53 kDa and 52 kDa, indicative of glycosylation and the existence of two isoforms. N-Glycosylation of the enzyme was subsequently confirmed using Western blotting and either specific binding of concanavalin A or peptide-N4-(N-acetylglucosaminyl)asparagine amidase digestion. The de-N-glycosylated enzyme ran with apparent molecular masses of 51 kDa and 50 kDa, indicative of a single N-glycosylation site. The galactosyltransferase exhibited a pH optimum at 7.2 and had a pronounced requirement for Mn2+ ions (KM=2.5 mM) for its action. The transferase activity was independent of the concentration of Triton X-100. The enzyme was capable of transferring galactose from UDP-galactose to a variety of galactose-based acceptors in alpha-glycosidic linkages. The apparent KM values for UDP-galactose and for the preferred acceptor substrate N-acetyl-lactosamine are 46 microM and 4.5 mM respectively. From these results we would like to suggest that the galactosyltransferase functions in the processing of terminal N-acetyl-lactosamine structures of trypanosomal glycoproteins. (+info)Galactosyltransferase, pyrophosphatase and phosphatase activities in luminal plasma of the cauda epididymidis and in the rete testis fluid of some mammals. (2/1005)
Galactosyltransferase activity was measured in the luminal plasma of the cauda epididymidis of mice, rats, rabbits, rams and boars, and in the rete testis fluid of rams and boars. The activities of nucleotide pyrophosphatase and alkaline phosphatase, which compete with galactosyltransferase for substrate, were also determined. In these species, galactosyltransferase activity in the luminal plasma of the cauda epididymidis was similar when the inhibitory effect of pyrophosphatase and phosphatase was minimized by assay conditions. However, under assay conditions that did not minimize the effect of these enzymes, the galactosyltransferase activities of these species were very different and were inversely correlated with the activities of pyrophosphatase and phosphatase. The ratio of galactosyltransferase activity to pyrophosphatase and phosphatase activity was much higher in the rete testis fluid than in the luminal plasma of the cauda epididymidis in both rams and boars. In rams, galactosyltransferase in the luminal plasma of the cauda epididymidis was more heat resistant than that in serum. These results suggest that there is a species difference in the availability of galactosyltransferase activity in the luminal plasma of the cauda epididymidis and that in some species, galactosyltransferase in the luminal fluid is unlikely to have any function. The results are also discussed with respect to the possible function of galactosyltransferase, pyrophosphatase and phosphatase in epididymal luminal plasma and rete testis fluid. (+info)Stimulation of collagen galactosyltransferase and glucosyltransferase activities by lysophosphatidylcholine. (3/1005)
Lysophosphatidylcholine stimulated the activities of collagen galactosyl- and glucosyl-transferases in chick-embryo extract and its particulate fractions in vitro, whereas essentially no stimulation was noted in the high-speed supernatant, where the enzymes are soluble and membrane-free. The stimulatory effect of lysophosphatidylcholine was masked by 0.1% Triton X-100. In kinetic experiments lysophosphatidylcholine raised the maximum velocities with respect to the substrates and co-substrates, whereas no changes were observed in the apparant Km values. Phospholipase A preincubation of the chick-embryo extract resulted in stimulation of both transferase activities, probably gy generating lysophosphatides from endogenous phospholipids. No stimulation by lysophosphatidylcholine was found when tested with 500-fold-purified glycosyltransferase. The results suggest that collagen glycosyltransferases must be associated with the membrane structures of the cell in order to be stimulated by lysophosphatidylcholine. Lysophosphatidylcholine could have some regulatory significance in vivo, since its concentration in the cell is comparable with that which produced marked stimulation in vitro. (+info)Isolation and characterization of a Golgi-rich fraction from the Harding-Passey mouse melanoma. (4/1005)
Golgi-rich fraction was isolated from Harding-Passey mouse melanoma by centrifugation through the discontinuous sucrose density gradient and its properties were compared with those of the same fraction isolated from rat liver. The specific activity of UDP-galactose: N-acetylglucosamine galactosyltransferase was 35 times higher in the melanoma Golgi fraction than in the melanoma homogenate and was a half that in the rat liver Golgi fraction. The specific activities of marker enzymes for other subcellular components such as 5'-nucleotidase, acid phosphatase and glucose-6-phosphatase in the melanoma Golgi fraction were all one-third those in the melanoma homogenate. Electron micrographs of the negatively-stained Golgi fractions of melanoma and liver revealed the presence of a system of tubules, vesicles and plate-like center regions which are known as components of Golgi apparatus. Tyrosinase activity was found to be present in this fraction of mouse melanoma, but its specific activity was lower than that in the rough or smooth surface membrane fraction or in the melanosome fraction. (+info)Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and beta1,4-galactosyltransferase I. (5/1005)
I-branched poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine branches attached to linear poly-N-acetyllactosamine, which is synthesized by I-branching beta1, 6-N-acetylglucosaminyltransferase. I-branched poly-N-acetyllactosamine can carry bivalent functional oligosaccharides such as sialyl Lewisx, which provide much better carbohydrate ligands than monovalent functional oligosaccharides. In the present study, we first demonstrate that I-branching beta1, 6-N-acetylglucosaminyltransferase cloned from human PA-1 embryonic carcinoma cells transfers beta1,6-linked GlcNAc preferentially to galactosyl residues of N-acetyllactosamine close to nonreducing terminals. We then demonstrate that among various beta1, 4-galactosyltransferases (beta4Gal-Ts), beta4Gal-TI is most efficient in adding a galactose to linear and branched poly-N-acetyllactosamines. When a beta1,6-GlcNAc branched poly-N-acetyllactosamine was incubated with a mixture of beta4Gal-TI and i-extension beta1,3-N-acetylglucosaminyltransferase, the major product was the oligosaccharide with one N-acetyllactosamine extension on the linear Galbeta1-->4GlcNAcbeta1-->3 side chain. Only a minor product contained galactosylated I-branch without N-acetyllactosamine extension. This finding was explained by the fact that beta4Gal-TI adds a galactose poorly to beta1,6-GlcNAc attached to linear poly-N-acetyllactosamines, while beta1, 3-N-acetylglucosaminyltransferase and beta4Gal-TI efficiently add N-acetyllactosamine to linear poly-N-acetyllactosamines. Together, these results strongly suggest that galactosylation of I-branch is a rate-limiting step in I-branched poly-N-acetyllactosamine synthesis, allowing poly-N-acetyllactosamine extension mostly along the linear poly-N-acetyllactosamine side chain. These findings are entirely consistent with previous findings that poly-N-acetyllactosamines in human erythrocytes, PA-1 embryonic carcinoma cells, and rabbit erythrocytes contain multiple, short I-branches. (+info)Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. (6/1005)
The human blood group A and B glycosyltransferases catalyze the transfer of GalNAc and Gal, to the (O)H-precursor structure Fuc alpha (1-2)Gal beta-OR to form the blood group A and B antigens, respectively. Changing four amino acids (176, 235, 266 and 268) alters the specificity from an A to a B glycosyltransferase. A series of hybrid blood group A/B glycosyltransferases were produced by interchanging these four amino acids in synthetic genes coding for soluble forms of the enzymes and expressed in Escherichia coli. The purified hybrid glycosyltransferases were characterized by two-substrate enzyme kinetic analysis using both UDP-GalNAc and UDP-Gal donor substrates. The A and B glycosyltransferases were screened with other donor substrates and found to also utilize the unnatural donors UDP-GlcNAc and UDP-Glc, respectively. The kinetic data demonstrate the importance of a single amino acid (266) in determining the A vs. B donor specificity. (+info)Quantitative determination of N-acetylglucosamine residues at the non-reducing ends of peptidoglycan chains by enzymic attachment of [14C]-D-galactose. (7/1005)
The ability of human milk galactosyltransferase to attach D-galactose residues quantitatively to the C-4 of N-acetylglucosamine moieties at the ends of oligosaccharides has been utilized for the specific labeling and quantitative determination of the chain length of the glycan moiety of the bacterial cell wall. The average polysaccharide chain length of the soluble, uncrosslinked peptidoglycan secreted by Micrococcus luteus cells on incubation with penicillin G was studied with this technique and found to be approximately 70 hexosamines long. Furthermore, the peptidoglycan chain length of Escherichia coli sacculi of different cell shapes and dimensions was determined both in rod-shaped cells and in filaments induced by temperature shift of a division mutant or by addition of cephalexin or nalidixic acid. The average chain length found in most of these sacculi was between 70 and 100 hexosamines long. Small spherical 'mini' cells had chain lengths similar to those of the isogenic rod-like cells. (+info)Target cell susceptibility to lysis by human natural killer cells is augmented by alpha(1,3)-galactosyltransferase and reduced by alpha(1, 2)-fucosyltransferase. (8/1005)
Susceptibility of porcine endothelial cells to human natural killer (NK) cell lysis was found to reflect surface expression of ligands containing Gal alpha(1,3)Gal beta(1,4)GlcNAc [corrected], the principal antigen on porcine endothelium recognized by xenoreactive human antibodies. Genetically modifying expression of this epitope on porcine endothelium by transfection with the alpha(1,2)-fucosyltransferase gene reduced susceptibility to human NK lysis. These results indicate that surface carbohydrate remodeling profoundly affects target cell susceptibility to NK lysis, and suggest that successful transgenic strategies to limit xenograft rejection by NK cells and xenoreactive antibodies will need to incorporate carbohydrate remodeling. (+info)Galactosyltransferases are a group of enzymes that play a crucial role in the biosynthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of many cell types. These enzymes catalyze the transfer of galactose, a type of sugar, to another molecule, such as another sugar or a lipid, to form a glycosidic bond.
Galactosyltransferases are classified based on the type of donor substrate they use and the type of acceptor substrate they act upon. For example, some galactosyltransferases use UDP-galactose as a donor substrate and transfer galactose to an N-acetylglucosamine (GlcNAc) residue on a protein or lipid, forming a lactosamine unit. Others may use different donor and acceptor substrates to form different types of glycosidic linkages.
These enzymes are involved in various biological processes, including cell recognition, signaling, and adhesion. Abnormalities in the activity of galactosyltransferases have been implicated in several diseases, such as congenital disorders of glycosylation, cancer, and inflammatory conditions. Therefore, understanding the function and regulation of these enzymes is important for developing potential therapeutic strategies for these diseases.
N-Acetyllactosamine Synthase (Galβ1,3GlcNAc-T) is an enzyme that catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-N-acetylglucosamine to a terminal β-D-galactose residue of glycoproteins or glycolipids, forming β1,3 linkages and creating the disaccharide N-acetyllactosamine (Galβ1-3GlcNAc). This enzyme plays a crucial role in the biosynthesis of complex carbohydrates called mucin-type O-glycans and some types of A, B, H, Le^a^, and Le^b^ blood group antigens. There are two major isoforms of this enzyme, β3GnT1 and β3GnT2, which differ in their substrate specificities and tissue distributions.
Lactose synthase is an enzyme composed of two subunits: a regulatory subunit, β-1,4-galactosyltransferase (β-1,4-GT), and a catalytic subunit, α-lactalbumin. This enzyme plays a crucial role in lactose biosynthesis during milk production in mammals. By catalyzing the transfer of a galactose molecule from UDP-galactose to glucose, lactose synthase generates lactose (or milk sugar), which is essential for providing energy and growth to newborns. The activity of lactose synthase is primarily regulated by α-lactalbumin, which modifies the substrate specificity of β-1,4-GT, allowing it to use glucose as an acceptor instead of other glycoconjugates.
Lactalbumin is a protein found in milk, specifically in the whey fraction. It is a globular protein with a molecular weight of around 14,000 daltons and consists of 123 amino acids. Lactalbumin is denatured and coagulates under heat, which makes it useful in cooking and baking as a stabilizer and emulsifier.
In addition to its use as a food ingredient, lactalbumin has also been studied for its potential health benefits. It contains all essential amino acids and is easily digestible, making it a high-quality source of protein. Some research suggests that lactalbumin may have immune-enhancing properties and could potentially be used in the treatment of certain medical conditions. However, more research is needed to confirm these potential benefits.
Galactose is a simple sugar or monosaccharide that is a constituent of lactose, the disaccharide found in milk and dairy products. It's structurally similar to glucose but with a different chemical structure, and it plays a crucial role in various biological processes.
Galactose can be metabolized in the body through the action of enzymes such as galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-galactose 4'-epimerase. Inherited deficiencies in these enzymes can lead to metabolic disorders like galactosemia, which can cause serious health issues if not diagnosed and treated promptly.
In summary, Galactose is a simple sugar that plays an essential role in lactose metabolism and other biological processes.
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.
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.
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.
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.
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.
Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.
An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.
Glycosyltransferases are a group of enzymes that play a crucial role in the synthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of cells and in various biological fluids. These enzymes catalyze the transfer of a sugar moiety from an activated donor molecule to an acceptor molecule, resulting in the formation of a glycosidic bond.
The donor molecule is typically a nucleotide sugar, such as UDP-glucose or CMP-sialic acid, which provides the energy required for the transfer reaction. The acceptor molecule can be a wide range of substrates, including proteins, lipids, and other carbohydrates.
Glycosyltransferases are highly specific in their activity, with each enzyme recognizing a particular donor and acceptor pair. This specificity allows for the precise regulation of glycan structures, which have been shown to play important roles in various biological processes, including cell recognition, signaling, and adhesion.
Defects in glycosyltransferase function can lead to a variety of genetic disorders, such as congenital disorders of glycosylation (CDG), which are characterized by abnormal glycan structures and a wide range of clinical manifestations, including developmental delay, neurological impairment, and multi-organ dysfunction.
Beta-N-Acetylglucosaminylglycopeptide beta-1,4-Galactosyltransferase is a type of enzyme that plays a role in the biosynthesis of complex carbohydrates known as glycoproteins. These enzymes catalyze the transfer of galactose molecules to N-acetylglucosamine residues found on glycoproteins, forming a beta-1,4 linkage between the two sugars. This enzyme is involved in various biological processes and is widely expressed in different tissues throughout the body. Defects or mutations in this gene can lead to congenital disorders of glycosylation, which are a group of genetic diseases that affect the body's ability to produce and modify complex carbohydrates.
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.
Galactosyltransferase
Ganglioside galactosyltransferase
Glycosaminoglycan galactosyltransferase
Procollagen galactosyltransferase
Galactolipid galactosyltransferase
N-acylsphingosine galactosyltransferase
Galactogen 6beta-galactosyltransferase
Sphingosine beta-galactosyltransferase
Galactinol-sucrose galactosyltransferase
Galactinol-raffinose galactosyltransferase
Glucosaminylgalactosylglucosylceramide beta-galactosyltransferase
Inositol 3-alpha-galactosyltransferase
Raffinose-raffinose alpha-galactosyltransferase
Lipopolysaccharide 3-alpha-galactosyltransferase
Soyasapogenol B glucuronide galactosyltransferase
Galactosylxylosylprotein 3-beta-galactosyltransferase
Lactosylceramide 4-alpha-galactosyltransferase
Kaempferol 3-O-galactosyltransferase
Sucrose 6F-alpha-galactosyltransferase
Fucosylgalactoside 3-alpha-galactosyltransferase
Indolylacetyl-myo-inositol galactosyltransferase
Xylosylprotein 4-beta-galactosyltransferase
Alpha 1,3-galactosyltransferase 2
Lactotriaosylceramide beta-1,4-galactosyltransferase
Lactosylceramide beta-1,3-galactosyltransferase
2-Hydroxyacylsphingosine 1-beta-galactosyltransferase
N-acetyllactosaminide 3-alpha-galactosyltransferase
Glucosylceramide beta-1,4-galactosyltransferase
Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
Collagen beta(1-o)galactosyltransferase 1
Galactosyltransferase - Wikipedia
ENZYME - 2.4.1.375 rhamnogalacturonan I galactosyltransferase
"Function and formation of beta1,4-galactosyltransferase-specific adhes" by Carol Murrell Maillet
Naphthyl Thio- and Carba-xylopyranosides for Exploration of the Active Site of β-1,4-Galactosyltransferase 7 (β4GalT7) |...
Polymorphisms of the β-1,4 galactosyltransferase-I gene in
Sperm from β1,4-galactosyltransferase I-null mice exhibit precocious capacitation | Development | The Company of Biologists
Coagulopathy in α-galactosyl transferase knockout pulmonary xenotransplants<...
Probing Elongating and Branching beta-D-Galactosyltransferase Activities in Leishmania Parasites by Making Use of Synthetic...
Mouse b3GALT2(Beta-1,3-Galactosyltransferase 2) ELISA Kit - Operatie Biotech Research Purchasing (BRP)
1nwg.1 | SWISS-MODEL Template Library
2fyc.1 | SWISS-MODEL Template Library
Glycobiology of cell death: when glycans and lectins govern cell fate | Cell Death & Differentiation
PLOD3 procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 [Homo sapiens (human)] - Gene - NCBI
Recombinant Human B4GalT1 Protein, CF 3609-GT-010: R&D Systems
Characterization of the promoter and the transcription factors for the mouse UDP-Gal:βGlcNAc β1,3-galactosyltransferase gene<...
Activation of a G protein complex by aggregation of β-1,4- galactosyltransferase on the surface of sperm<...
beta 1,3-Galactosyltransferase beta 3Gal-T5 acts on the GlcNAcbeta 1--|3Galbeta 1--|4GlcNAcbeta 1--|R sugar chains of...
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Studies Shed Light on Bt Resistance in Worms and Moths - Scientific American
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Glossary | Animal Biotechnology: Science-Based Concerns | The National Academies Press
Xenogeneic cross-circulation for extracorporeal recovery of injured human lungs | Nature Medicine
SCOP 1.73: Domain d2fycd1: 2fyc D:131-402
Isolated Noncompaction of the Ventricular Myocardium - Ontology Report - Rat Genome Database
Civ - 7377 Produits | Page 5
Publication : USDA ARS
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Ehlers-Danlos Syndrome: Practice Essentials, Background, Pathophysiology
Beta1,3-galactosyltransferase1
- We attempted to determine whether beta1,3-galactosyltransferase beta3Gal-T5 is involved in the biosynthesis of a specific subset of type 1 chain carbohydrates and expressed in a cancer-associated manner. (unipv.it)
ENZYME4
- Xyloside analogues with substitution of the endocyclic oxygen atom by sulfur or carbon were investigated as substrates for β-1,4-galactosyltransferase 7 (β4GalT7), a key enzyme in the biosynthesis of glycosaminoglycan chains. (lu.se)
- The scope of this study was to identify sequence polymorphisms in the β-1,4- galactosyltransferase-I gene (B4GALT1), the gene which encodes the catalytic part of lactose synthase enzyme. (ac.ir)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Beta-1,3-Galactosyltransferase 2 (b3GALT2) in serum, plasma, tissue homogenates and other biological fluids. (operatiebrp.nl)
- The animals lack the gene responsible for "alpha-1,3-galactosyltransferase" (GT)-an enzyme normally present in the pig vascular system. (science20.com)
Biosynthesis1
- We showed that the activity detected with L. donovani membranes is the elongating beta-D-galactosyltransferase associated with LPG phosphosaccharide backbone biosynthesis (eGalT). (dundee.ac.uk)
Gene3
- We concluded therefore that the β-1,4-galactosyltransferase-I gene was polymorphic in Holsteins. (ac.ir)
- Methods: In this study, we describe the results of two porcine-to-baboon transplants utilizing porcine lungs depleted of macrophages, deficient in the α-1,3- galactosyltransferase gene, and with the expression of human decay-accelerating factor, a complement regulatory protein. (umn.edu)
- Marked prolongation of porcine renal xenograft survival in baboons through the use of α-1,3-galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue. (nature.com)
GalTase2
- Galactosyltransferase (GalTase) is localized in the Golgi, where it functions in oligosaccharide synthesis, as well as on the cell surface where it serves as a cell adhesion molecule. (tmc.edu)
- One sperm receptor for the mouse egg is β-1,4-galactosyltransferase (GalTase), which binds O-linked oligosaccharides on the egg coat glycoprotein ZP3. (illinois.edu)
Protein1
- In this paper, we describe the capacitation phenotype of sperm lacking the long isoform of β1,4-galactosyltransferase I (GalT I), a sperm surface protein that functions as a receptor for the zona pellucida glycoprotein, ZP3, and as an inducer of the acrosome reaction following ZP3-dependent aggregation. (biologists.com)
B3galt61
- Beta-1,3-galactosyltransferase 6 (B3GALT6) transfers a second galactose to the tetrasaccharide linker. (reactome.org)
Substrates1
- Using the same substrates we detected two types of galactosyltransferase activity in L. major membranes: the elongating beta-D-galactosyltransferase and a branching beta-D-galactosyltransferase (bGalT). (dundee.ac.uk)
Pathway2
- Structural Snapshots of beta-1,4-Galactosyltransferase-I Along the Kinetic Pathway. (expasy.org)
- UDP-Gal:βGlcNAc β1,3-galactosyltransferase (Gal-T-II) is responsible for synthesis of ganglioside GM1 in the ganglioside biosynthetic pathway. (elsevierpure.com)
Galactose1
- Galactosyltransferase is a type of glycosyltransferase which catalyzes the transfer of galactose. (wikipedia.org)
BETA2
- Description: A sandwich ELISA kit for detection of Beta-1,3-Galactosyltransferase 2 from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (operatiebrp.nl)
- beta 1,3-Galactosyltransferase beta 3Gal-T5 acts on the GlcNAcbeta 1-->3Galbeta 1-->4GlcNAcbeta 1-->R sugar chains of carcinoembryonic antigen and other N-linked glycoproteins and is down-regulated in colon adenocarcinomas. (unipv.it)
Mouse1
- Description: A competitive ELISA for quantitative measurement of Mouse β 1,3 galactosyltransferase 2(B3GALT2) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (operatiebrp.nl)
Alpha 1-3-galactosyltransferase3
- Conformational Changes Induced by Binding Udp-2F-Galactose to Alpha-1,3 Galactosyltransferase-Implications for Catalysis. (nih.gov)
- Other transgenic pig strains express different glycosyltransferases which compete with alpha-1,3- galactosyltransferase, the enzyme that generates the gal epitope, to decrease the gal antigen expression. (nih.gov)
- To further reduce the risk of hyperacute rejection, two different strains of alpha-1,3-galactosyltransferase gene knockout pigs, which lack the expression of the gal epitope, were recently developed. (nih.gov)
Ceramide galactosyltransferase1
- The metabolism of sulfatide, which synthesized by two transferases (ceramide galactosyltransferase and cerebroside sulfotransferase) from ceramide and specifically degraded by a sulfatase (arylsulfatase A), is very simple compared to that of many gangliosides. (go.jp)
Galactose5
- Galactosyltransferase is a type of glycosyltransferase which catalyzes the transfer of galactose. (wikipedia.org)
- Introduction Galactosyl transferase (uridine diphosphate-D-galactose : D-glucose-l-galactosyltransferase, EC 2.4.1.22) of bovine milk catalyzes the two basic reactions below: UDPGal + GIcNAc Me(I! (docksci.com)
- This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. (unl.edu)
- Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2. (unl.edu)
- Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of collagen. (nih.gov)
Beta4GalT2
- This gene is a member of the beta-1,4-galactosyltransferase (beta4GalT) family. (nih.gov)
- This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. (novusbio.com)
Procollagen1
- Galactosylation of collagen propeptide hydroxylysines by procollagen galactosyltransferases 1, 2. (reactome.org)
Proteins2
- Background: UBE2Q1-dependent ubiquitination of key proteins including β 1,4- galactosyltransferase (GalT1), and P53 might play a pivotal role in cancer development. (benthamscience.com)
- This domain is found in plant proteins that often carry a galactosyltransferase domain, pfam01762, at their C-terminus. (unl.edu)
Genes1
- Based on the results of our previous studies and the present association analysis, the zinc-finger protein 608 (ZNF608), GRAM domain containing 3 (GRAMD3), aldehyde dehydrogenase 7 family member A1 (ALDH7A1), fem-1 homologue C (FEM1C), beta-1,4-galactosyltransferase 1 (B4GALT1) and versican (VCAN) genes were selected for the differential expression analysis. (ias.ac.in)
Tumor1
- 14. [Preclinical and clinical studies on a tumor marker, galactosyltransferase associated with tumor (GAT), in ovarian cancer (second report)--clinical significance of GAT and comparison with other tumor markers]. (nih.gov)
Human1
- NMR-based exploration of the acceptor binding site of human blood group B galactosyltransferase with molecular fragments. (mpg.de)