The Nobel Prize is not a medical term, but a prestigious international award given annually in several categories, including Physiology or Medicine, for significant contributions to humanity that have conferred the greatest benefit to mankind.
A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
An enzyme that catalyzes the synthesis of UDPgalactose from UTP and galactose-1-phosphate. It is present in low levels in fetal and infant liver, but increases with age, thereby enabling galactosemic infants who survive to develop the capacity to metabolize galactose. EC 2.7.7.10.
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.

A genetic model of substrate deprivation therapy for a glycosphingolipid storage disorder. (1/467)

Inherited defects in the degradation of glycosphingolipids (GSLs) cause a group of severe diseases known as GSL storage disorders. There are currently no effective treatments for the majority of these disorders. We have explored a new treatment paradigm, substrate deprivation therapy, by constructing a genetic model in mice. Sandhoff's disease mice, which abnormally accumulate GSLs, were bred with mice that were blocked in their synthesis of GSLs. The mice with simultaneous defects in GSL synthesis and degradation no longer accumulated GSLs, had improved neurologic function, and had a much longer life span. However, these mice eventually developed a late-onset neurologic disease because of accumulation of another class of substrate, oligosaccharides. The results support the validity of the substrate deprivation therapy and also highlight some limitations.  (+info)

Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold. (2/467)

Mucin-type O-glycosylation is initiated by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases). Based on sequence relationships with divergent proteins, the ppGaNTases can be subdivided into three putative domains: each putative domain contains a characteristic sequence motif. The 112-amino acid glycosyltransferase 1 (GT1) motif represents the first half of the catalytic unit and contains a short aspartate-any residue-histidine (DXH) or aspartate-any residue-aspartate (DXD)-like sequence. Secondary structure predictions and structural threading suggest that the GT1 motif forms a 5-stranded parallel beta-sheet flanked by 4 alpha-helices, which resembles the first domain of the lactose repressor. Four invariant carboxylates and a histidine residue are predicted to lie at the C-terminal end of three beta-strands and line the active site cleft. Site-directed mutagenesis of murine ppGaNTase-T1 reveals that conservative mutations at these 5 positions result in products with no detectable enzyme activity (D156Q, D209N, and H211D) or <1% activity (E127Q and E213Q). The second half of the catalytic unit contains a DXXXXXWGGENXE motif (positions 310-322) which is also found in beta1,4-galactosyltransferases (termed the Gal/GalNAc-T motif). Mutants of carboxylates within this motif express either no detectable activity, 1% or 2% activity (E319Q, E322Q, and D310N, respectively). Mutagenesis of highly conserved (but not invariant) carboxylates produces only modest alterations in enzyme activity. Mutations in the C-terminal 128-amino acid ricin-like lectin motif do not alter the enzyme's catalytic properties.  (+info)

Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli. (3/467)

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)

Dynamic epigenetic regulation of initial O-glycosylation by UDP-N-Acetylgalactosamine:Peptide N-acetylgalactosaminyltransferases. site-specific glycosylation of MUC1 repeat peptide influences the substrate qualities at adjacent or distant Ser/Thr positions. (4/467)

In search of possible epigenetic regulatory mechanisms ruling the initiation of O-glycosylation by polypeptide:N-acetylgalactosaminyltransferases, we studied the influences of mono- and disaccharide substituents of glycopeptide substrates on the site-specific in vitro addition of N-acetylgalactosamine (GalNAc) residues by recombinant GalNAc-Ts (rGalNAc-T1, -T2, and -T3). The substrates were 20-mers (HGV20) or 21-mers (AHG21) of the MUC1 tandem repeat peptide carrying GalNAcalpha or Galbeta1-3GalNAcalpha at different positions. The enzymatic products were analyzed by MALDI mass spectrometry and Edman degradation for the number and sites of incorporated GalNAc. Disaccharide placed on the first position of the diad Ser-16-Thr-17 prevents glycosylation of the second, whereas disaccharide on the second position of Ser-16-Thr-17 and Thr-5-Ser-6 does not prevent GalNAc addition to the first. Multiple disaccharide substituents suppress any further glycosylation at the remaining sites. Glycosylation of Ser-16 is negatively affected by glycosylation at position -6 (Thr-10) or -10 (Ser-6) and is inhibited by disaccharide at position -11 (Thr-5), suggesting the occurrence of glycosylation-induced effects on distant acceptor sites. Kinetic studies revealed the accelerated addition of GalNAc to Ser-16 adjacent to GalNAc-substituted Thr-17, demonstrating positive regulatory effects induced by glycosylation on the monosaccharide level. These antagonistic effects of mono- and disaccharides could underlie a postulated regulatory mechanism.  (+info)

Attenuation of interleukin 2 signal in the spleen cells of complex ganglioside-lacking mice. (5/467)

T cell development and function in complex ganglioside-lacking (GM2/GD2 synthase gene-disrupted) mice were analyzed. GM1, asialo-GM1, and GD1b were representative gangliosides expressed on T cells of the wild type mice and completely deleted on those of the mutant mice. The sizes and cell numbers of the mutant mice spleen and thymus were significantly reduced. Spleen cells from the mutant mice showed clearly reduced proliferation compared with the wild type when stimulated by interleukin 2 (IL-2) but not when treated with concanavalin A or anti-CD3 cross-linking. Expression levels of IL-2 receptor alpha, beta, and gamma were almost equivalent, and up-regulation of alpha chain after T cell activation was also similar between the mutant and wild type mice. Activation of JAK1, JAK3, and SAT5 after IL-2 treatment was reduced, and c-fos expression was delayed and reduced in the mutant spleen cells, suggesting that the IL-2 signal was attenuated in the mutant mice probably due to the modulation of IL-2 receptors by the lack of complex gangliosides.  (+info)

Involvement of the core protein in the first beta-N-acetylgalactosamine transfer to the glycosaminoglycan-protein linkage-region tetrasaccharide and in the subsequent polymerization: the critical determining step for chondroitin sulphate biosynthesis. (6/467)

alpha-Thrombomodulin (alpha-TM) with a truncated glycosaminoglycan-protein linkage tetrasaccharide, GlcAbeta1-3Galbeta1-3Galbeta1-4Xyl, was tested as an acceptor together with a sugar donor, UDP-N-[3H]acetylgalactosamine, using a cell-free enzyme system prepared from the serum-free culture medium of a human melanoma cell line. The truncated tetrasaccharide on alpha-TM served as an acceptor, whereas the linkage tetrasaccharide-serine did not. Our characterization of the radioactively labelled product by enzymic digestion revealed that the N-[3H]acetylgalactosamine residue was transferred to alpha-TM through a beta1,4-linkage. The substrate competition experiments with the chondro-hexasaccharide and alpha-TM reinforced our speculation that a common N-acetylgalactosaminyltransferase catalysed the transfer of N-acetylgalactosamine to both the linkage tetrasaccharide and the longer chondroitin oligosaccharides. Moreover, chondroitin polymerization was demonstrated on the tetrasaccharide of alpha-TM using both UDP-glucuronic acid and UDP-N-acetylgalactosamine as sugar donors. Much longer chains were synthesized on alpha-TM than on the linkage penta- and hexa-saccharide-serines. Together, these results indicated that the core protein is required for the transfer of the first N-acetylgalactosamine residue through a beta1,4-linkage and also for subsequent efficient chain polymerization reactions, and that the critical determining step for chondroitin sulphate biosynthesis is the transfer of the first N-acetylgalactosamine residue.  (+info)

Incorporation of N-acetylgalactosamine into consecutive threonine residues in MUC2 tandem repeat by recombinant human N-acetyl-D-galactosamine transferase-T1, T2 and T3. (7/467)

An oligopeptide containing three consecutive Thr residues mimicking the tandem repeat portion of MUC2 (PTTTPLK) was investigated for the acceptor specificity to UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase isozymes, UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase-T1, T2 and T3. The enzymatic reaction products were fractionated by the reversed-phase high performance liquid chromatography, then characterized by matrix-assisted laser desorption ionization time of flight mass spectrometry and by a peptide sequencing analysis. A maximum of two, one or three N-acetyl-D-galactosamine residues was transferred by UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase-T1, T2 or T3, respectively. The preferential orders of N-acetyl-D-galactosamine incorporation were Thr-2, then Thr-4 for UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase-T1, Thr-2 for UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase-T2 and Thr4, Thr-3, then Thr-2 for UDP-N-acetyl-D-galactosamine:peptide N-acetylgalactosaminyltransferase-T3.  (+info)

Reevaluating the effect of Brefeldin A (BFA) on ganglioside synthesis: the location of GM2 synthase cannot be deduced from the inhibition of GM2 synthesis by BFA. (8/467)

Brefeldin A reversibly disassembles the Golgi complex, causing mixing of the Golgi cisternae with the ER while the trans Golgi network persists as part of a separate endosomal membrane system. Because of this compartmental separation, Brefeldin A treatment has been used to map the sub-Golgi locations of several Golgi enzymes including GM2 synthase. We previously proposed that GM2 synthase might be located in a distal portion of the Golgi complex which in the presence of Brefeldin A would be separated from the substrate ganglioside GM3 present in the mixed ER-Golgi membrane system. In the present study we show using GM2 synthase chimeras that GM2 synthesis was blocked by Brefeldin A when GM2 synthase was distributed throughout all Golgi subcompartments or even when it was restricted to the medial Golgi. Because these findings opposed our speculation regarding a distal location of this enzyme, we sought an alternative explanation for the inhibition of ganglioside synthesis by Brefeldin A. However, Brefeldin A did not degrade GM2 synthase, prevent its homodimerization, or inhibit its in vitro activity. Brefeldin A did result in the conversion of a portion of membrane bound GM2 synthase into a soluble form which has minimal capability to produce GM2 in whole cells. However, this conversion was not sufficient to explain the nearly total loss of GM2 production in intact cells in the presence of Brefeldin A. Nevertheless, the results of this study indicate that Brefeldin A-induced inhibition of ganglioside synthesis cannot be used to deduce the location of GM2 synthase.  (+info)

I'm sorry for any confusion, but the term "Nobel Prize" is not a medical definition. The Nobel Prize is an international award given annually in several categories, and one of those categories is physiology or medicine. The Nobel Prize in Physiology or Medicine is awarded to individuals who have made significant discoveries of outstanding importance in the fields of life sciences and medicine. It is one of the most prestigious awards in these fields.

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

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.

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.

Uridine Diphosphate (UDP) Glucose Dehydrogenase is an enzyme that plays a role in carbohydrate metabolism. Its systematic name is UDP-glucose:NAD+ oxidoreductase, and it catalyzes the following chemical reaction:

UDP-glucose + NAD+ -> UDP-glucuronate + NADH + H+

This enzyme helps convert UDP-glucose into UDP-glucuronate, which is a crucial component in the biosynthesis of various substances in the body, such as glycosaminoglycans and other glyconjugates. The reaction also results in the reduction of NAD+ to NADH, which is an essential coenzyme in numerous metabolic processes.

UDP-glucose dehydrogenase is widely distributed in various tissues, including the liver, kidney, and intestine. Deficiencies or mutations in this enzyme can lead to several metabolic disorders, such as glucosuria and hypermethioninemia.

UTP-hexose-1-phosphate uridylyltransferase is an enzyme that catalyzes the transfer of a uridine monophosphate (UMP) group from a uridine triphosphate (UTP) molecule to a hexose-1-phosphate molecule, forming a UDP-hexose molecule. This reaction is an essential step in the biosynthesis of various glycosylated compounds, including glycoproteins and polysaccharides.

The systematic name for this enzyme is UTP:alpha-D-hexose-1-phosphate uridylyltransferase. It is also known as UDP-glucose pyrophosphorylase, which is a more specific name that refers to the formation of UDP-glucose from glucose-1-phosphate and UTP.

The enzyme plays a crucial role in carbohydrate metabolism and has been implicated in several diseases, including diabetes and cancer. Inhibitors of this enzyme have been explored as potential therapeutic agents for the treatment of these conditions.

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

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

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

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

... polypeptide N-acetylgalactosaminyltransferases". Glycobiology. 13 (1): 1R-16R. doi:10.1093/glycob/cwg007. PMID 12634319. ...
"Differential roles of two N-acetylgalactosaminyltransferases, CSGalNAcT-1, and a novel enzyme, CSGalNAcT-2. Initiation and ...
4-N-acetylgalactosaminyltransferases IV synthesizing N,N'-diacetyllactosediamine". FEBS Letters. 562 (1-3): 134-40. doi:10.1016 ...
... polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l( ...
... n-acetylgalactosaminyltransferases MeSH D08.811.913.400.100.200.300 - fucosyl galactose alpha-n-acetylgalactosaminyltransferase ...
This definition of the word Acetylgalactosaminyltransferases is from the Wiktionary dictionary, where you can also find the ... Definition of acetylgalactosaminyltransferases. Do you know the meaning of acetylgalactosaminyltransferases?. Word in 32 ... The word acetylgalactosaminyltransferases does not have anagrams.. Acetylgalactosaminyltransferases backwards:. The word ... This definition of the word acetylgalactosaminyltransferases is from the Wiktionary, where you can also find the etimology, ...
... polypeptide N-acetylgalactosaminyltransferases". Glycobiology. 13 (1): 1R-16R. doi:10.1093/glycob/cwg007. PMID 12634319. ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
... acetylgalactosaminyltransferases (GALNT); 5) hexosaminidase (HEX); 6) mannosidase (MAN); 7) acetylglucosaminyltransferase (MGAT ...
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree. Glycobiology ...
H Differential roles of two N-acetylgalactosaminyl-transferases, CSGalNAcT-1 and a novel enzyme CSGalNAcT-2 Initiation and ...
The family of GalNAc-Ts (GalNAcpolypeptide:N-Acetylgalactosaminyl transferases) catalyzes the first committed step in the ...
Farrow EG, Imel EA, White KE. Miscellaneous non-inflammatory musculoskeletal conditions. Hyperphosphatemic familial tumoral calcinosis (FGF23, GALNT3 and aKlotho). Best Pract Res Clin Rheumatol. 2011 Oct; 25(5):735-47 ...
N-Acetylgalactosaminyltransferases; Phenotype; Polymorphism, Single Nucleotide/genetics ...
N-Acetylgalactosaminyltransferases / genetics* Actions. * Search in PubMed * Search in MeSH * Add to Search ...
N-Acetylgalactosaminyltransferases / genetics* Actions. * Search in PubMed * Search in MeSH * Add to Search ...
... polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and canine submaxillary gland mucin ... Peptide N-acetylgalactosaminyltransferases. site-specific glycosylation of MUC1 repeat peptide influences the substrate ...
... mucin-type O-glycosylation by transferring O-GalNAc to Thr/Ser residues are the polypeptide N-acetylgalactosaminyltransferases ...
Figure 31.5 Structure and function of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs) ...
acetylgalactosaminyltransferases (GalNAc-Ts) catalyzes this reaction predominantly in the Golgi, in contrast to the initiation ...
Cloning and Characterization of the Gene Family Encoding the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferases from ...
N Acetylgalactosaminyltransferases use N-Acetylgalactosaminyltransferases N Acetylglucosamine 6 Sulfatase Deficiency use ... N-Acetylgalactosamine Transferases use N-Acetylgalactosaminyltransferases N-Acetylgalactosamine, Uridine Diphosphate use ...
N-Acetylgalactosaminyltransferases Preferred Term Term UI T051873. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1993). ... N-Acetylgalactosaminyltransferases Preferred Concept UI. M0026343. Registry Number. EC 2.4.1.-. Scope Note. Enzymes that ... N-Acetylgalactosaminyltransferases [D08.811.913.400.100.200] * Fucosyl Galactose alpha-N-Acetylgalactosaminyltransferase [ ... N-Acetylgalactosaminyltransferases. Tree Number(s). D08.811.913.400.100.200. Unique ID. D017350. RDF Unique Identifier. http:// ...
N-Acetylgalactosaminyltransferases Preferred Term Term UI T051873. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1993). ... N-Acetylgalactosaminyltransferases Preferred Concept UI. M0026343. Registry Number. EC 2.4.1.-. Scope Note. Enzymes that ... N-Acetylgalactosaminyltransferases [D08.811.913.400.100.200] * Fucosyl Galactose alpha-N-Acetylgalactosaminyltransferase [ ... N-Acetylgalactosaminyltransferases. Tree Number(s). D08.811.913.400.100.200. Unique ID. D017350. RDF Unique Identifier. http:// ...
N-Acetylgalactosaminyltransferases *ChGn. *GALNACT-2. * N-Acetylgalactosaminyltransferases Glucuronyltransferases GalNAc/GlcA * ...
acetylgalactosaminyltransferases → Definition and anagrams of acetylgalactosaminyltransferases. → Other senses and detailed ...
N-Acetylgalactosaminyltransferases 62% * Head and Neck Neoplasms 60% * Squamous Cell Carcinoma of Head and Neck 39% ...
It really is initiated by Golgi-resident polypeptide N-acetylgalactosaminyltransferases (GALNTs) that catalyse the addition of ...
N-Dimethyltryptamine N0000167607 N-Acetylgalactosamine-4-Sulfatase N0000168367 N-Acetylgalactosaminyltransferases N0000168369 N ...
The polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts) are a family of conserved enzymes that initiate the mucin-type ...
... mucin-type O-glycosylation by transferring O-GalNAc to Thr/Ser residues are the polypeptide N-acetylgalactosaminyltransferases ...
Cloning and characterization of a family of Toxoplasma gondii UDP-GalNAcpolypeptide N-acetylgalactosaminyltransferases. FASEB ...
N-Dimethyltryptamine N-Acetylgalactosamine-4-Sulfatase N-Acetylgalactosaminyltransferases N-Acetylglucosaminyltransferases N- ...
This gene encodes a member of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, which catalyze the ... This gene encodes a member of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, which catalyze the ...
... to arise acetylgalactosaminyltransferases to factors shown in chain and target from species targeted in metropolisation ...
  • The large family of isoenzymes that initiate mucin-type O-glycosylation by transferring O-GalNAc to Thr/Ser residues are the polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). (nih.gov)
  • Initiation of mucin-type O-glycosylation is controlled by a large family of UDP GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). (nih.gov)
  • This gene encodes a member of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, which catalyze the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc to a serine or threonine residue on a polypeptide acceptor in the initial step of O-linked protein glycosylation. (nih.gov)