Enzymes that catalyze the transfer of glucose from a nucleoside diphosphate glucose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
A polysaccharide-producing species of STREPTOCOCCUS isolated from human dental plaque.
Polysaccharides composed of repeating glucose units. They can consist of branched or unbranched chains in any linkages.
A species of gram-positive, coccoid bacteria isolated from the human tooth surface. Strains have been shown to be cariogenic in experimental animals and may be associated with human dental caries.
A disaccharide consisting of two glucose units in an alpha (1-6) glycosidic linkage.
A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.
A large heterogeneous group of mostly alpha-hemolytic streptococci. They colonize the respiratory tract at birth and generally have a low degree of pathogenicity. This group of species includes STREPTOCOCCUS MITIS; STREPTOCOCCUS MUTANS; STREPTOCOCCUS ORALIS; STREPTOCOCCUS SANGUIS; STREPTOCOCCUS SOBRINUS; and the STREPTOCOCCUS MILLERI GROUP. The latter are often beta-hemolytic and commonly produce invasive pyogenic infections including brain and abdominal abscesses.
A genus of gram-positive, coccoid bacteria whose organisms occur in pairs or chains. No endospores are produced. Many species exist as commensals or parasites on man or animals with some being highly pathogenic. A few species are saprophytes and occur in the natural environment.
Dextranase is an enzyme that catalyzes the hydrolysis of dextran, a glucose polymer, into smaller oligosaccharides or simple sugars, primarily used in clinical settings to prevent or treat dextran-induced complications such as anaphylaxis and renal dysfunction.
Localized destruction of the tooth surface initiated by decalcification of the enamel followed by enzymatic lysis of organic structures and leading to cavity formation. If left unchecked, the cavity may penetrate the enamel and dentin and reach the pulp.
Enzymes that catalyze the transfer of glycosyl groups to an acceptor. Most often another carbohydrate molecule acts as an acceptor, but inorganic phosphate can also act as an acceptor, such as in the case of PHOSPHORYLASES. Some of the enzymes in this group also catalyze hydrolysis, which can be regarded as transfer of a glycosyl group from the donor to water. Subclasses include the HEXOSYLTRANSFERASES; PENTOSYLTRANSFERASES; SIALYLTRANSFERASES; and those transferring other glycosyl groups. EC 2.4.
A genus of gram-positive, facultatively anaerobic bacteria whose growth is dependent on the presence of a fermentable carbohydrate. It is nonpathogenic to plants and animals, including humans.
Physicochemical property of fimbriated (FIMBRIAE, BACTERIAL) and non-fimbriated bacteria of attaching to cells, tissue, and nonbiological surfaces. It is a factor in bacterial colonization and pathogenicity.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A group of glucose polymers made by certain bacteria. Dextrans are used therapeutically as plasma volume expanders and anticoagulants. They are also commonly used in biological experimentation and in industry for a wide variety of purposes.
Encrustations, formed from microbes (bacteria, algae, fungi, plankton, or protozoa) embedding in extracellular polymers, that adhere to surfaces such as teeth (DENTAL DEPOSITS); PROSTHESES AND IMPLANTS; and catheters. Biofilms are prevented from forming by treating surfaces with DENTIFRICES; DISINFECTANTS; ANTI-INFECTIVE AGENTS; and antifouling agents.
A nonreducing disaccharide composed of GLUCOSE and FRUCTOSE linked via their anomeric carbons. It is obtained commercially from SUGARCANE, sugar beet (BETA VULGARIS), and other plants and used extensively as a food and a sweetener.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.
Proteins found in any species of bacterium.
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.
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.
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.
Immunoglobulins produced in a response to BACTERIAL ANTIGENS.
The functional hereditary units of BACTERIA.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A protein-glucan intermediate during paramylon synthesis. (1/2513)

A sodium deoxycholate extract containing glucosyltransferase activity was obtained from a particulate preparation from Euglena gracilis. It transferred glucose from UDP-[14C]glucose into material that was precipitated by trichloroacetic acid. This material released beta-(1 leads to 3)-glucan oligosaccharides into solution on incubation with weak acid, weak alkali and beta-(1 leads to 3)-glucosidase. The products of the incubation of the deoxycholate extract with UDP-[14C]glucose were analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Radioactive bands were obtained that had the properties of beta-(1 leads to 3)-glucan covalently linked to protein by a bond labile to weak acid. High-molecular-weight material containing a beta-(1 leads to 3)-glucan was also shown to be present by gel filtration. The bond linking glucan to aglycone is possibly a pyrophosphate linkage. It is proposed that in Euglena gracilis beta-(1 leads to 3)-glucan (paramylon) is synthesized on a protein primer.  (+info)

Patterns of evolutionary rate variation among genes of the anthocyanin biosynthetic pathway. (2/2513)

The anthocyanin biosynthetic pathway is responsible for the production of anthocyanin pigments in plant tissues and shares a number of enzymes with other biochemical pathways. The six core structural genes of this pathway have been cloned and characterized in two taxonomically diverse plant species (maize and snapdragon). We have recently cloned these genes for a third species, the common morning glory, Ipomoea purpurea. This additional information provides an opportunity to examine patterns of evolution among genes within a single biochemical pathway. We report here that upstream genes in the anthocyanin pathway have evolved substantially more slowly than downstream genes and suggest that this difference in evolutionary rates may be explained by upstream genes being more constrained because they participate in several different biochemical pathways. In addition, regulatory genes associated with the anthocyanin pathway tend to evolve more rapidly than the structural genes they regulate, suggesting that adaptive evolution of flower color may be mediated more by regulatory than by structural genes. Finally, for individual anthocyanin genes, we found an absence of rate heterogeneity among three major angiosperm lineages. This rate constancy contrasts with an accelerated rate of evolution of three CHS-like genes in the Ipomoea lineage, indicating that these three genes have diverged without coordinated adjustment by other pathway genes.  (+info)

Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin. (3/2513)

UDP-glucose: anthocyanin 5-O-glucosyltransferase (5-GT) is responsible for the modification of anthocyanins to more stable molecules in complexes for co-pigmentation, supposedly resulting in a purple hue. The cDNA encoding 5-GT was isolated by a differential display applied to two different forms of anthocyanin production in Perilla frutescens var. crispa. Differential display was carried out for mRNA from the leaves of reddish-purple and green forms of P. frutescens, resulting in the isolation of five cDNA clones predominantly expressed in the red form. The cDNA encoded a polypeptide of 460 amino acids, exhibiting a low homology with the sequences of several glucosyltransferases including UDP-glucose: anthocyanidin 3-O-glucosyltransferase. By using this cDNA as the probe, we also isolated a homologous cDNA clone from a petal cDNA library of Verbena hybrida. To identify the biochemical function of the encoded proteins, these cDNAs were expressed in Saccharomyces cerevisiae cells. The recombinant proteins in the yeast extracts catalyzed the conversion of anthocyanidin 3-O-glucosides into the corresponding anthocyanidin 3,5-di-O-glucosides using UDP-glucose as a cofactor, indicating the identity of the cDNAs encoding 5-GT. Several biochemical properties (optimum pH, Km values, and sensitivity to inhibitors) were similar to those reported previously for 5-GTs. Southern blot analysis indicated the presence of two copies of 5-GT genes in the genome of both red and green forms of P. frutescens. The mRNA accumulation of the 5-GT gene was detected in the leaves of the red form but not in those of the green form and was induced by illumination of light, as observed for other structural genes for anthocyanin biosynthesis in P. frutescens.  (+info)

GTPase activity and biochemical characterization of a recombinant cotton fiber annexin. (4/2513)

A cDNA encoding annexin was isolated from a cotton (Gossypium hirsutum) fiber cDNA library. The cDNA was expressed in Escherichia coli, and the resultant recombinant protein was purified. We then investigated some biochemical properties of the recombinant annexin based on the current understanding of plant annexins. An "add-back experiment" was performed to study the effect of the recombinant annexin on beta-glucan synthase activity, but no effect was found. However, it was found that the recombinant annexin could display ATPase/GTPase activities. The recombinant annexin showed much higher GTPase than ATPase activity. Mg2+ was essential for these activities, whereas a high concentration of Ca2+ was inhibitory. A photolabeling assay showed that this annexin could bind GTP more specifically than ATP. The GTP-binding site on the annexin was mapped into the carboxyl-terminal fourth repeat of annexin from the photolabeling experiment using domain-deletion mutants of this annexin. Northern-blot analysis showed that the annexin gene was highly expressed in the elongation stages of cotton fiber differentiation, suggesting a role of this annexin in cell elongation.  (+info)

Expression and structural characterization of a baculovirus ecdysteroid UDP-glucosyltransferase. (5/2513)

The baculovirus enzyme ecdysteroid UDP-glucosyltransferase (EGT) disrupts the hormonal balance of the insect host by catalysing the conjugation of ecdysteroids, the moulting hormones, with the sugar moiety from UDP-glucose or UDP-galactose. In this study, EGT has been overproduced using a recombinant Autographa californica nucleopolyhedrovirus and an antiserum has been raised against the purified protein. This antiserum was used to visualize the kinetics of expression of EGT by wild-type AcMNPVL-1 and by the overproducing recombinant virus. The inclusion of tunicamycin during these time-course experiments suggested that EGT is glycosylated. This was confirmed by Endo F treatment, which showed that glycosylation increased the apparent subunit molecular mass by approximately 11 kDa. These sugars do not appear to be required for enzyme activity. EGT activity invariantly elutes from gel-filtration columns as a single peak corresponding to a 260 kDa (+/-50 kDa) protein. This suggests that the enzyme is an oligomer of three to five subunits, since the subunit molecular mass is 56 kDa.  (+info)

Manganese sulfate-dependent glycosylation of endogenous glycoproteins in human skeletal muscle is catalyzed by a nonglucose 6-P-dependent glycogen synthase and not glycogenin. (6/2513)

Glycogenin, a Mn2+-dependent, self-glucosylating protein, is considered to catalyze the initial glucosyl transfer steps in glycogen biogenesis. To study the physiologic significance of this enzyme, measurements of glycogenin mediated glucose transfer to endogenous trichloroacetic acid precipitable material (protein-bound glycogen, i.e., glycoproteins) in human skeletal muscle were attempted. Although glycogenin protein was detected in muscle extracts, activity was not, even after exercise that resulted in marked glycogen depletion. Instead, a MnSO4-dependent glucose transfer to glycoproteins, inhibited by glycogen and UDP-pyridoxal (which do not affect glycogenin), and unaffected by CDP (a potent inhibitor of glycogenin), was consistently detected. MnSO4-dependent activity increased in concert with glycogen synthase fractional activity after prolonged exercise, and the MnSO4-dependent enzyme stimulated glucosylation of glycoproteins with molecular masses lower than those glucosylated by glucose 6-P-dependent glycogen synthase. Addition of purified glucose 6-P-dependent glycogen synthase to the muscle extract did not affect MnSO4-dependent glucose transfer, whereas glycogen synthase antibody completely abolished MnSO4-dependent activity. It is concluded that: (1) MnSO4-dependent glucose transfer to glycoproteins is catalyzed by a nonglucose 6-P-dependent form of glycogen synthase; (2) MnSO4-dependent glycogen synthase has a greater affinity for low molecular mass glycoproteins and may thus play a more important role than glucose 6-P-dependent glycogen synthase in the initial stages of glycogen biogenesis; and (3) glycogenin is generally inactive in human muscle in vivo.  (+info)

Induction of selected lipid metabolic enzymes and differentiation-linked structural proteins by air exposure in fetal rat skin explants. (7/2513)

The epidermal permeability barrier of premature infants matures rapidly following birth. Previous studies suggest that air exposure could contribute to this acceleration, because: (i) development of a structurally and functionally mature barrier accelerates when fetal rat skin explants are incubated at an air-medium interface, and (ii) occlusion with a water-impermeable membrane prevents this acceleration. To investigate further the effects of air exposure on epidermal barrier ontogenesis, we compared the activities of several key enzymes of lipid metabolism and gene expression of protein markers of epidermal differentiation in fetal rat skin explants grown immersed versus air exposed. The rate-limiting enzymes of cholesterol (HMG CoA reductase) and ceramide (serine palmitoyl transferase) synthesis were not affected. In contrast, the normal developmental increases in activities of glucosylceramide synthase and cholesterol sulfotransferase, responsible for the synthesis of glucosylceramides and cholesterol sulfate, respectively, were accelerated further by air exposure. Additionally, two enzymes required for the final stages of barrier maturation and essential for normal stratum corneum function, beta-glucocerebrosidase, which converts glucosylceramide to ceramide, and steroid sulfatase, which desulfates cholesterol sulfate, also increased with air exposure. Furthermore, filaggrin and loricrin mRNA levels, and filaggrin, loricrin, and involucrin protein levels all increased with air exposure. Finally, occlusion with a water-impermeable membrane prevented both the air-exposure-induced increase in lipid enzyme activity, and the expression of loricrin, filaggrin, and involucrin. Thus, air exposure stimulates selected lipid metabolic enzymes and the gene expression of key structural proteins in fetal epidermis, providing a biochemical basis for air-induced acceleration of permeability barrier maturation in premature infants.  (+info)

Regulation of intracellular ceramide content in B16 melanoma cells. Biological implications of ceramide glycosylation. (8/2513)

We previously reported that ceramide released from glycosphingolipids (GSLs) by endoglycoceramidase was directly metabolized to GSLs, and thus the content of GSLs was constantly maintained in B16 melanoma cells (Ito, M., and Komori, H. (1996) J. Biol. Chem. 271, 12655-12660). In this study, the metabolism of ceramide released from sphingomyelin (SM) by bacterial sphingomyelinase (SMase) was examined using B16 cells and their GSL-deficient mutant counterpart GM95 cells. Treatment of B16 melanoma cells with bacterial SMase effectively hydrolyzed SM on the plasma membrane. Under these conditions, NeuAcalpha2,3Galbeta1, 4Glcbeta1,1ceramide was significantly increased. Interestingly, UDP-glucose:ceramide glucosyltransferase-1 (GlcT-1) activity and GSL synthesis, but not SM synthesis or sphingosine generation, were found to be up-regulated by SMase treatment. The up-regulation of GSL synthesis seemed to occur at both the transcriptional and post-translational steps of GlcT-1 synthesis. Accumulation of ceramide by bacterial SMase was much higher in GM95 cells than in the parental cells. When the enzyme was removed from the culture medium, the intracellular ceramide level in B16 cells, but not that in the mutant cells, normalized. No rapid restoration of SM in either of the cell lines was observed after removal of the enzyme. SMase treatment strongly inhibited DNA synthesis in GM95 cells but not that in B16 cells. In the presence of D-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol, an inhibitor of GlcT-1, SMase treatment markedly increased the ceramide content and thus inhibited DNA synthesis in B16 cells. Our study provides the first evidence that GlcT-1 functions to regulate the level of intracellular ceramide by glycosylation of the ceramide when it is present in excess.  (+info)

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

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

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

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

Streptococcus mutans is a gram-positive, facultatively anaerobic, beta-hemolytic species of bacteria that's part of the normal microbiota of the oral cavity in humans. It's one of the primary etiological agents associated with dental caries, or tooth decay, due to its ability to produce large amounts of acid as a byproduct of sugar metabolism, which can lead to demineralization of tooth enamel and dentin. The bacterium can also adhere to tooth surfaces and form biofilms, further contributing to the development of dental caries.

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

Streptococcus sobrinus is a gram-positive, facultatively anaerobic coccus that belongs to the viridans group of streptococci. It's a type of bacteria commonly found in the oral cavity and is one of the primary causative agents of dental caries (tooth decay) along with Streptococcus mutans.

S. sobrinus has the ability to metabolize sugars and produce acid as a byproduct, which can lower the pH of the oral environment and contribute to tooth demineralization and cavity formation. This organism is often found in higher numbers in individuals with a high risk of caries and is associated with a more severe form of the disease.

It's important to note that while S. sobrinus is a significant contributor to dental caries, good oral hygiene practices, such as regular brushing and flossing, limiting sugar intake, and receiving professional dental care can help prevent the negative effects of this bacteria on oral health.

Isomaltose is a type of disaccharide, which is a complex sugar consisting of two monosaccharides. It is specifically composed of two glucose molecules linked together in a way that forms a straight chain. Isomaltose can be found naturally in some foods such as honey and fermented products, and it can also be produced industrially as a sweetener.

In the medical field, isomaltose may be relevant in the context of carbohydrate metabolism disorders or in relation to certain types of diagnostic tests that measure the ability to digest and absorb specific sugars. However, it is not a commonly used term in most areas of medical practice.

Uridine Diphosphate Glucose (UDP-glucose) is a nucleotide sugar that plays a crucial role in the synthesis and metabolism of carbohydrates in the body. It is formed from uridine triphosphate (UTP) and glucose-1-phosphate through the action of the enzyme UDP-glucose pyrophosphorylase.

UDP-glucose serves as a key intermediate in various biochemical pathways, including glycogen synthesis, where it donates glucose molecules to form glycogen, a large polymeric storage form of glucose found primarily in the liver and muscles. It is also involved in the biosynthesis of other carbohydrate-containing compounds such as proteoglycans and glycolipids.

Moreover, UDP-glucose is an essential substrate for the enzyme glucosyltransferase, which is responsible for adding glucose molecules to various acceptor molecules during the process of glycosylation. This post-translational modification is critical for the proper folding and functioning of many proteins.

Overall, UDP-glucose is a vital metabolic intermediate that plays a central role in carbohydrate metabolism and protein function.

Viridans Streptococci are a group of gram-positive, facultatively anaerobic bacteria that are part of the normal flora in the oral cavity, upper respiratory tract, and gastrointestinal tract. They are called "viridans" because they tend to decolorize slowly and appear greenish in Gram stains. This group includes several species, such as Streptococcus mitis, Streptococcus sanguinis, Streptococcus salivarius, and Streptococcus mutans.

Viridans Streptococci are often associated with dental caries and periodontal disease. However, they can also cause invasive infections, particularly in immunocompromised individuals or those with underlying medical conditions. These infections may include bacteremia, endocarditis, abscesses, and meningitis.

It is important to note that the identification of Viridans Streptococci can be challenging due to their similarities in biochemical characteristics. Therefore, molecular methods such as 16S rRNA gene sequencing are often used for accurate species-level identification.

Streptococcus is a genus of Gram-positive, spherical bacteria that typically form pairs or chains when clustered together. These bacteria are facultative anaerobes, meaning they can grow in the presence or absence of oxygen. They are non-motile and do not produce spores.

Streptococcus species are commonly found on the skin and mucous membranes of humans and animals. Some strains are part of the normal flora of the body, while others can cause a variety of infections, ranging from mild skin infections to severe and life-threatening diseases such as sepsis, meningitis, and toxic shock syndrome.

The pathogenicity of Streptococcus species depends on various virulence factors, including the production of enzymes and toxins that damage tissues and evade the host's immune response. One of the most well-known Streptococcus species is Streptococcus pyogenes, also known as group A streptococcus (GAS), which is responsible for a wide range of clinical manifestations, including pharyngitis (strep throat), impetigo, cellulitis, necrotizing fasciitis, and rheumatic fever.

It's important to note that the classification of Streptococcus species has evolved over time, with many former members now classified as different genera within the family Streptococcaceae. The current classification system is based on a combination of phenotypic characteristics (such as hemolysis patterns and sugar fermentation) and genotypic methods (such as 16S rRNA sequencing and multilocus sequence typing).

Dextranase is an enzyme that breaks down dextran, a type of complex sugar (polysaccharide) consisting of many glucose molecules linked together in a chain. Dextran is produced by certain bacteria and can be found in some foods, as well as in the body during infections or after surgery. Dextranase is used medically to help prevent or treat complications associated with dextran, such as blockages in blood vessels caused by the accumulation of dextran molecules. It may also be used in research and industry for various purposes, including the production of clarified fruit juices and wine.

Dental caries, also known as tooth decay or cavities, refers to the damage or breakdown of the hard tissues of the teeth (enamel, dentin, and cementum) due to the activity of acid-producing bacteria. These bacteria ferment sugars from food and drinks, producing acids that dissolve and weaken the tooth structure, leading to cavities.

The process of dental caries development involves several stages:

1. Demineralization: The acidic environment created by bacterial activity causes minerals (calcium and phosphate) to be lost from the tooth surface, making it weaker and more susceptible to decay.
2. Formation of a white spot lesion: As demineralization progresses, a chalky white area appears on the tooth surface, indicating early caries development.
3. Cavity formation: If left untreated, the demineralization process continues, leading to the breakdown and loss of tooth structure, resulting in a cavity or hole in the tooth.
4. Infection and pulp involvement: As the decay progresses deeper into the tooth, it can reach the dental pulp (the soft tissue containing nerves and blood vessels), causing infection, inflammation, and potentially leading to toothache, abscess, or even tooth loss.

Preventing dental caries involves maintaining good oral hygiene, reducing sugar intake, using fluoride toothpaste and mouthwash, and having regular dental check-ups and cleanings. Early detection and treatment of dental caries can help prevent further progression and more severe complications.

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.

Leuconostoc is a genus of gram-positive, facultatively anaerobic bacteria that belong to the family Leuconostocaceae. These bacteria are non-motile, non-spore forming, and occur as pairs or chains. They are catalase-negative and reduce nitrate to nitrite.

Leuconostoc species are commonly found in nature, particularly in plants, dairy products, and fermented foods. They play a significant role in the food industry, where they are used in the production of various fermented foods such as sauerkraut, pickles, and certain cheeses.

In clinical settings, Leuconostoc species can sometimes be associated with healthcare-associated infections, particularly in patients who have underlying medical conditions or who are immunocompromised. They can cause bacteremia, endocarditis, and device-related infections. However, these infections are relatively rare, and the majority of Leuconostoc species are considered to be non-pathogenic.

Bacterial adhesion is the initial and crucial step in the process of bacterial colonization, where bacteria attach themselves to a surface or tissue. This process involves specific interactions between bacterial adhesins (proteins, fimbriae, or pili) and host receptors (glycoproteins, glycolipids, or extracellular matrix components). The attachment can be either reversible or irreversible, depending on the strength of interaction. Bacterial adhesion is a significant factor in initiating biofilm formation, which can lead to various infectious diseases and medical device-associated infections.

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.

Dextrans are a type of complex glucose polymers that are formed by the action of certain bacteria on sucrose. They are branched polysaccharides consisting of linear chains of α-1,6 linked D-glucopyranosyl units with occasional α-1,3 branches.

Dextrans have a wide range of applications in medicine and industry. In medicine, dextrans are used as plasma substitutes, volume expanders, and anticoagulants. They are also used as carriers for drugs and diagnostic agents, and in the manufacture of immunoadsorbents for the removal of toxins and pathogens from blood.

Dextrans can be derived from various bacterial sources, but the most common commercial source is Leuconostoc mesenteroides B-512(F) or L. dextranicum. The molecular weight of dextrans can vary widely, ranging from a few thousand to several million Daltons, depending on the method of preparation and purification.

Dextrans are generally biocompatible and non-toxic, but they can cause allergic reactions in some individuals. Therefore, their use as medical products requires careful monitoring and testing for safety and efficacy.

Biofilms are defined as complex communities of microorganisms, such as bacteria and fungi, that adhere to surfaces and are enclosed in a matrix made up of extracellular polymeric substances (EPS). The EPS matrix is composed of polysaccharides, proteins, DNA, and other molecules that provide structural support and protection to the microorganisms within.

Biofilms can form on both living and non-living surfaces, including medical devices, implants, and biological tissues. They are resistant to antibiotics, disinfectants, and host immune responses, making them difficult to eradicate and a significant cause of persistent infections. Biofilms have been implicated in a wide range of medical conditions, including chronic wounds, urinary tract infections, middle ear infections, and device-related infections.

The formation of biofilms typically involves several stages, including initial attachment, microcolony formation, maturation, and dispersion. Understanding the mechanisms underlying biofilm formation and development is crucial for developing effective strategies to prevent and treat biofilm-associated infections.

Sucrose is a type of simple sugar, also known as a carbohydrate. It is a disaccharide, which means that it is made up of two monosaccharides: glucose and fructose. Sucrose occurs naturally in many fruits and vegetables and is often extracted and refined for use as a sweetener in food and beverages.

The chemical formula for sucrose is C12H22O11, and it has a molecular weight of 342.3 g/mol. In its pure form, sucrose is a white, odorless, crystalline solid that is highly soluble in water. It is commonly used as a reference compound for determining the sweetness of other substances, with a standard sucrose solution having a sweetness value of 1.0.

Sucrose is absorbed by the body through the small intestine and metabolized into glucose and fructose, which are then used for energy or stored as glycogen in the liver and muscles. While moderate consumption of sucrose is generally considered safe, excessive intake can contribute to weight gain, tooth decay, and other health problems.

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.

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.

Saliva is a complex mixture of primarily water, but also electrolytes, enzymes, antibacterial compounds, and various other substances. It is produced by the salivary glands located in the mouth. Saliva plays an essential role in maintaining oral health by moistening the mouth, helping to digest food, and protecting the teeth from decay by neutralizing acids produced by bacteria.

The medical definition of saliva can be stated as:

"A clear, watery, slightly alkaline fluid secreted by the salivary glands, consisting mainly of water, with small amounts of electrolytes, enzymes (such as amylase), mucus, and antibacterial compounds. Saliva aids in digestion, lubrication of oral tissues, and provides an oral barrier against microorganisms."

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.

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 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.

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.

Bacterial antibodies are a type of antibodies produced by the immune system in response to an infection caused by bacteria. These antibodies are proteins that recognize and bind to specific antigens on the surface of the bacterial cells, marking them for destruction by other immune cells. Bacterial antibodies can be classified into several types based on their structure and function, including IgG, IgM, IgA, and IgE. They play a crucial role in the body's defense against bacterial infections and provide immunity to future infections with the same bacteria.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

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

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

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

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

Glucosyltransferases are a type of glycosyltransferase that enable the transfer of glucose. Examples include: glycogen synthase ... ISBN 978-0-87969-770-9. {{cite book}}: ,author= has generic name (help) Glucosyltransferases at the U.S. National Library of ...
... collagen glucosyltransferase, collagen hydroxylysyl glucosyltransferase, galactosylhydroxylysyl glucosyltransferase, UDP- ... The systematic name of this enzyme class is UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase. Other ... In enzymology, a procollagen glucosyltransferase (EC 2.4.1.66) is an enzyme that catalyzes the chemical reaction UDP-glucose + ... Isolation, purification and properties of the glucosyl transferase". Biochem. Biophys. Res. Commun. 30 (1): 89-94. doi:10.1016/ ...
The systematic name of this enzyme class is UDP-glucose:hydroquinone-O-beta-D-glucosyltransferase. Other names in common use ... In enzymology, a hydroquinone glucosyltransferase (EC 2.4.1.218) is an enzyme that catalyzes the chemical reaction UDP-glucose ... Arend J, Warzecha H, Stockigt J (2000). "Hydroquinone: O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and ... include arbutin synthase, and hydroquinone:O-glucosyltransferase. ...
... (or glucosylceramide synthase) is a glucosyltransferase enzyme involved in the production of ... Ceramide+glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Transferases, All ... "Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of ...
Other names in common use include cyanohydrin glucosyltransferase, and uridine diphosphoglucose-cyanohydrin glucosyltransferase ... In enzymology, a hydroxymandelonitrile glucosyltransferase (EC 2.4.1.178) is an enzyme that catalyzes the chemical reaction UDP ... The systematic name of this enzyme class is UDP-glucose:4-hydroxymandelonitrile glucosyltransferase. ...
The systematic name of this enzyme class is UDP-glucose:hydroxyanthraquinone O-glucosyltransferase. Other names in common use ... In enzymology, a hydroxyanthraquinone glucosyltransferase (EC 2.4.1.181) is an enzyme that catalyzes the chemical reaction UDP- ... Khouri HE, Ibrahim RK (1987). "Purification and some properties of five anthraquinone-specific glucosyltransferases from ... include uridine diphosphoglucose-anthraquinone glucosyltransferase, and anthraquinone-specific glucosyltransferase. ...
The systematic name of this enzyme class is UDP-glucose:phosphopolyprenol D-glucosyltransferase. Other names in common use ... In enzymology, a phosphopolyprenol glucosyltransferase (EC 2.4.1.78) is an enzyme that catalyzes the chemical reaction UDP- ... polyprenol monophosphate glucosyltransferase. Jankowski W, Mankowski T, Chojnacki T (1974). "Formation of polyprenol ... include uridine diphosphoglucose-polyprenol monophosphate, glucosyltransferase, and UDP-glucose: ...
The systematic name of this enzyme class is UDP-glucose:nicotinate N-glucosyltransferase. Other names in common use include ... In enzymology, a nicotinate glucosyltransferase (EC 2.4.1.196) is an enzyme that catalyzes the chemical reaction UDP-glucose + ... uridine diphosphoglucose-nicotinate N-glucosyltransferase, and UDP-glucose:nicotinic acid-N-glucosyltransferase. Upmeier B, ...
... (EC 2.4.1.271, crocetin GTase, UGTCs2) is an enzyme with systematic name UDP-glucose:crocetin 8-O- ... Crocetin+glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.4.1 ... Côté F, Cormier F, Dufresne C, Willemot C (2000). "Properties of a glucosyltransferase involved in crocin synthesis". Plant Sci ... D-glucosyltransferase. This enzyme catalyses the following chemical reaction (1) UDP-glucose + crocetin ⇌ {\displaystyle \ ...
The systematic name of this enzyme class is UDP-glucose:vomilenine 21-O-beta-D-glucosyltransferase. This enzyme is also called ... In enzymology, a vomilenine glucosyltransferase (EC 2.4.1.219) is an enzyme that catalyzes the chemical reaction UDP-glucose + ... UDPG:vomilenine 21-beta-D-glucosyltransferase. This enzyme participates in indole and ipecac alkaloid biosynthesis. Warzecha H ...
... (EC 2.4.1.276, crtX (gene)) is an enzyme with systematic name UDP-glucose:zeaxanthin beta-D- ... Zeaxanthin+glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.4 ... Hundle BS, O'Brien DA, Alberti M, Beyer P, Hearst JE (October 1992). "Functional expression of zeaxanthin glucosyltransferase ... glucosyltransferase. This enzyme catalyses the following chemical reaction 2 UDP-glucose + zeaxanthin ⇌ {\displaystyle \ ...
In enzymology, a limonoid glucosyltransferase (EC 2.4.1.210) is an enzyme that catalyzes the chemical reaction. UDP-glucose + ... The systematic name of this enzyme class is uridine diphosphoglucose-limonoid glucosyltransferase. Shin H, Suhayda CG, Hsu, WJ ... Robertson GH (1997). "Purification of limonoid glucosyltransferase from navel orange albedo tissue". Phytochemistry. 46: 33-37 ...
The systematic name of this enzyme class is UDP-glucose:arylamine N-D-glucosyltransferase. Other names in common use include ... In enzymology, an arylamine glucosyltransferase (EC 2.4.1.71) is an enzyme that catalyzes the chemical reaction UDP-glucose + ... I. Purification and properties of UDP-glucose:arylamine N-glucosyl-transferase from soybean". Phytochemistry. 7 (3): 381-390. ... UDP glucose-arylamine glucosyltransferase, and uridine diphosphoglucose-arylamine glucosyltransferase. Frear DS (1968). " ...
The systematic name of this enzyme class is UDP-glucose:scopoletin O-beta-D-glucosyltransferase. Other names in common use ... In enzymology, a scopoletin glucosyltransferase (EC 2.4.1.128) is an enzyme that catalyzes the chemical reaction UDP-glucose + ... Betry, P.; Fliniaux, M.A.; Mackova, M.; Gillet, F.; Macek, T.; Jacquin-Dubreuil, A. (1995). "Scopoletin-glucosyltransferase ... include uridine diphosphoglucose-scopoletin glucosyltransferase, UDP-glucose:scopoletin glucosyltransferase, and SGTase. This ...
In enzymology, a lipopolysaccharide glucosyltransferase II (EC 2.4.1.73) is an enzyme that catalyzes the chemical reaction UDP- ... The systematic name of this enzyme class is UDP-glucose:galactosyl-lipopolysaccharide alpha-D-glucosyltransferase. Other names ... in common use include uridine diphosphoglucose-galactosylpolysaccharide, and glucosyltransferase. Edstrom RD, Heath EC (1967 ...
... beta-glucosyltransferase, UDP-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase, UGT85B1, and UDP-glucose:p- ... UDP-glucose-p-hydroxymandelonitrile glucosyltransferase, uridine diphosphoglucose-cyanohydrin glucosyltransferase, uridine ... In enzymology, a cyanohydrin beta-glucosyltransferase (EC 2.4.1.85) is an enzyme that catalyzes the chemical reaction UDP-D- ... The systematic name of this enzyme class is UDP-D-glucose:(S)-4-hydroxymandelonitrile beta-D-glucosyltransferase. Other names ...
... alpha-glucosyltransferase, T2-HMC-alpha-glucosyl transferase, T4-HMC-alpha-glucosyl transferase, and T6-HMC-alpha-glucosyl ... In enzymology, a DNA alpha-glucosyltransferase (EC 2.4.1.26) is an enzyme that catalyzes the chemical reaction in which an ... The systematic name of this enzyme class is UDP-glucose:DNA alpha-D-glucosyltransferase. Other names in common use include ... uridine diphosphoglucose-deoxyribonucleate, alpha-glucosyltransferase, UDP-glucose-DNA alpha-glucosyltransferase, uridine ...
The systematic name of this enzyme class is UDP-glucose:isovitexin 2"-O-beta-D-glucosyltransferase. This enzyme is also called ... In enzymology, an isovitexin beta-glucosyltransferase (EC 2.4.1.106) is an enzyme that catalyzes the chemical reaction UDP- ... uridine diphosphoglucose-isovitexin 2"-glucosyltransferase. Kamsteeg J, Besson E, Chopin J (1980). "The 2''-O-glucosylation of ...
In enzymology, a vitexin beta-glucosyltransferase (EC 2.4.1.105) is an enzyme that catalyzes the chemical reaction UDP-glucose ... glucosyltransferase. Kamsteeg J, Besson E, Chopin J (1980). "The 2''-O-glucosylation of vitexin and isovitexin in petals of ...
The systematic name of this enzyme class is UDP-glucose:sinapate D-glucosyltransferase. Other names in common use include ... In enzymology, a sinapate 1-glucosyltransferase (EC 2.4.1.120) is an enzyme that catalyzes the chemical reaction: UDP-glucose ... uridine diphosphoglucose-sinapate glucosyltransferase, UDP-glucose:sinapic acid glucosyltransferase, uridine 5'- ...
26-diol 3-O-beta-D-glucosyltransferase. This enzyme is also called uridine diphosphoglucose-nuatigenin glucosyltransferase. ... In enzymology, a nuatigenin 3beta-glucosyltransferase (EC 2.4.1.192) is an enzyme that catalyzes the chemical reaction UDP- ... "Subcellular-localization of UDPG-nuatigenin glucosyltransferase in oat leaves". Phytochemistry. 26 (2): 353-357. doi:10.1016/ ...
The systematic name of this enzyme class is UDP-glucose:indoxyl 3-O-beta-D-glucosyltransferase. This enzyme is also called ... In enzymology, an indoxyl-UDPG glucosyltransferase (EC 2.4.1.220) is an enzyme that catalyzes the chemical reaction UDP-glucose ... Marcinek H, Weyler W, Deus-Neumann B, Zenk MH (2000). "Indoxyl-UDPG-glucosyltransferase from Baphicacanthus cusia". ...
T4-beta-glucosyl transferase, T4 phage beta-glucosyltransferase, UDP glucose-DNA beta-glucosyltransferase, and uridine ... In enzymology, a DNA beta-glucosyltransferase (EC 2.4.1.27) is an enzyme that catalyzes the chemical reaction in which a beta-D ... Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase (GT). In other words, it transfers ... The systematic name of this enzyme class is UDP-glucose:DNA beta-D-glucosyltransferase. Other names in common use include T4- ...
... (EC 2.4.1.284, kanF (gene)) is an enzyme with systematic name UDP-alpha-D-glucose:2- ... 2-deoxystreptamine+glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... deoxystreptamine 6-alpha-D-glucosyltransferase. This enzyme catalyses the following chemical reaction UDP-alpha-D-glucose + 2- ...
Other names in common use include UDP-glucose:lipopolysaccharide glucosyltransferase I, lipopolysaccharide glucosyltransferase ... In enzymology, a lipopolysaccharide glucosyltransferase I (EC 2.4.1.58) is an enzyme that catalyzes the chemical reaction UDP- ... 3. Purification and properties of uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I". J. Biol. Chem. 247 (8 ... The systematic name of this enzyme class is UDP-glucose:lipopolysaccharide glucosyltransferase. ...
The systematic name of this enzyme class is UDP-glucose:(-)-menthol O-beta-D-glucosyltransferase. Other names in common use ... In enzymology, a monoterpenol beta-glucosyltransferase (EC 2.4.1.127) is an enzyme that catalyzes the chemical reaction UDP- ... include uridine diphosphoglucose-monoterpenol glucosyltransferase, and UDPglucose:monoterpenol glucosyltransferase. Fleuriet A ... Macheix JJ, Suen R, Ibrahim RK (1980). "Partial purifiction and some properties of a hydroxycinnamoyl glucosyltransferase from ...
... sterol glucosyltransferase, sterol-beta-D-glucosyltransferase, and UDP-glucose-sterol glucosyltransferase. Duperon R; Duperon P ... Other names in common use include UDPG:sterol glucosyltransferase, UDP-glucose-sterol beta-glucosyltransferase, sterol:UDPG ... uridine diphosphoglucose-poriferasterol glucosyltransferase, uridine diphosphoglucose-sterol glucosyltransferase, ... In enzymology, a sterol 3beta-glucosyltransferase (EC 2.4.1.173) is an enzyme that catalyzes the chemical reaction UDP-glucose ...
... xyloglucan 4beta-D-glucosyltransferase, and xyloglucan glucosyltransferase. Hayashi T, Matsuda K (1981). "Biosynthesis of ... The systematic name of this enzyme class is UDP-glucose:xyloglucan 1,4-beta-D-glucosyltransferase. Other names in common use ... In enzymology, a xyloglucan 4-glucosyltransferase (EC 2.4.1.168) is an enzyme that catalyzes the chemical reaction in which a ... xyloglucan in suspension-cultured soybean cells Occurrence and some properties of xyloglucan 4-beta-D-glucosyltransferase and 6 ...
... (EC 2.4.1.263, ABA-glucosyltransferase, ABA-GTase, AOG) is an enzyme with systematic name ... Abscisate+beta-glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... "Cloning and characterization of the abscisic acid-specific glucosyltransferase gene from adzuki bean seedlings". Plant ... UDP-D-glucose:abscisate beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction UDP-D-glucose + ...
In enzymology, a N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase (EC 2.4.1.188) is an enzyme that catalyzes the ... Other names in common use include UDP-D-glucose:N-acetylglucosaminyl pyrophosphorylundecaprenol, glucosyltransferase, uridine, ... diphosphoglucose-acetylglucosaminylpyrophosphorylundecaprenol, and glucosyltransferase. Kumita K, Murazumi N, Araki Y, Ito E ( ... N-acetylglucosaminyl pyrophosphorylundecaprenol glucosyltransferase from Bacillus coagulans AHU 1366 membranes". J. Biochem. ...

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