Cytidine Monophosphate
Deoxycytidine Monophosphate
Nucleoside-Phosphate Kinase
Cytidine Monophosphate N-Acetylneuraminic Acid
Cytidine
Cytidine Deaminase
Cytidine Triphosphate
Cytosine Nucleotides
Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-sialyltransferase from human fetal liver. (1/99)
Based on the sequences of the highly conserved segments in the previously cloned sialyltransferases, a cDNA encoding Galbeta1, 3GalNAc alpha2,3-sialyltransferase (SIATFL) has been isolated from human fetal liver. Expression analysis of the gene has been performed with various carcinoma cell lines, fetal tissues, fetal and adult liver and both hepatoma and the surrounding tissue from the same liver. The SIATFL gene was expressed poorly in fetal liver and in adult liver, slightly in hepatoma and highly in the surrounding tissue of hepatoma. The cDNA encoding the putative active domain was expressed in COS-1, Escherichia coli, and Pichia pastoris. The recombinant protein expressed in COS-1 could catalyse the transfer of NeuAc from CMP-NeuAc to asialo-fetuin. No enzyme activity was detected with a 32-kDa protein in E. coli and both 32-kDa and 41-kDa proteins in P. pastoris. These results suggested that correct glycosylation of the enzyme might play a key role in its folding that may be directly related to the enzymatic activity. (+info)Expression and activity of chimeric molecules between human UDP-galactose transporter and CMP-sialic acid transporter. (2/99)
Human UDP-galactose transporter (hUGT1) and CMP-sialic acid transporter (hCST) are related Golgi proteins with eight putative transmembrane helices predicted by computer analysis. We constructed chimeric molecules in which segments of various lengths from the C- or N-terminus of hUGT1 were replaced by corresponding portions of hCST. The chimeras were transiently expressed in UGT-deficient mutant Lec8 cells, and their UGT activity was assessed by the binding of GS-II lectin to the transfected cells. The replacement of either the N- or C-terminal cytoplasmic segment by that of hCST did not affect the expression or activity of hUGT1. A chimera in which the eighth helix and the C-terminal tail were replaced also retained the UGT activity, indicating that this helix is not involved in the determination of substrate specificity. In contrast, three types of chimeras, in which the first helix, the first and the second helices, and a segment from the seventh helix to the C-terminus were replaced, respectively, were expressed very infrequently in the transfected cells, and had no UGT activity. They are likely folded incorrectly and degraded by a quality-control system, since the amounts of their mRNAs were normal and the proteins were mainly localized in the ER. The first and the seventh helices are important for the stability of the transporter protein. (+info)Biosynthetic incorporation of unnatural sialic acids into polysialic acid on neural cells. (3/99)
In this study we demonstrate that polysialyltransferases are capable of accepting unnatural substrates in terminally differentiated human neurons. Polysialyltransferases catalyze the glycosylation of the neural cell adhesion molecule (NCAM) with polysialic acid (PSA). The unnatural sialic acid analog, N-levulinoyl sialic acid (SiaLev), was incorporated into cell surface glycoconjugates including PSA by the incubation of cultured neurons with the metabolic precursor N-levulinoylmannosamine (ManLev). The ketone group within the levulinoyl side chain of SiaLev was then used as a chemical handle for detection using a biotin probe. The incorporation of SiaLev residues into PSA was demonstrated by protection from sialidases that can cleave natural sialic acids but not those bearing unnatural N-acyl groups. The presence of SiaLev groups on the neuronal cell surface did not impede neurite outgrowth or significantly affect the distribution of PSA on neuronal compartments. Since PSA is important in neural plasticity and development, this mechanism for modulating PSA structure might be useful for functional studies. (+info)Exploring the acceptor substrate recognition of the human beta-galactoside alpha 2,6-sialyltransferase. (4/99)
Human beta1,4-galactoside alpha2,6-sialyltransferase I (ST6GalI) recognition of glycoprotein acceptors has been investigated using various soluble forms of the enzyme deleted to a variable extent in the N-terminal half of the polypeptide. Full-length and truncated forms of the enzyme have been investigated with respect to their specificity for a variety of desialylated glycoproteins of known complex glycans as well as related proteins with different carbohydrate chains. Differences in transfer efficiency have been observed between membrane and soluble enzymatic forms, indicating that deletion of the transmembrane fragment induces loss of acceptor preference. No difference in substrate recognition could be observed when soluble enzymes of similar peptide sequence were produced in yeast or mammalian cells, confirming that removal of the membrane anchor and heterologous expression do not alter enzyme folding and activity. When tested on free oligosaccharides, soluble ST6GalI displayed full ability to sialylate free N-glycans as well as various N-acetyllactosaminyl substrates. Progressive truncation of the N terminus demonstrated that the catalytic domain can proceed with sialic acid transfer with increased efficiency until 80 amino acids are deleted. Fusion of the ST6GalI catalytic domain to the N-terminal half of an unrelated transferase (core 2 beta1,6-N-acetylglucosaminyltransferase) further showed that a chimeric form of broad acceptor specificity and high activity could also be engineered in vivo. These findings therefore delineate a peptide region of approximately 50 amino acids within the ST6GalI stem region that governs both the preference for glycoprotein acceptors and catalytic activity, thereby suggesting that it may exert a steric control on the catalytic domain. (+info)Substrate recognition by UDP-galactose and CMP-sialic acid transporters. Different sets of transmembrane helices are utilized for the specific recognition of UDP-galactose and CMP-sialic acid. (5/99)
Human UDP-galactose transporter (hUGT1) and CMP-sialic acid transporter (hCST) are related Golgi membrane proteins with 10 transmembrane helices. We have constructed chimeras between these proteins in order to identify submolecular regions responsible for the determination of substrate specificity. To assess the UGT and CST activities, chimeric cDNAs were transiently expressed in either UGT-deficient mutant Lec8 cells or CST-deficient mutant Lec2 cells, and the binding of plant lectins, GS-II or PNA, respectively, to these cells was examined. During the course of analysis of various chimeric transporters, we found that chimeras whose submolecular regions contained helices 1, 8, 9, and 10, and helices 2, 3, and 7 derived from hUGT1 and hCST sequences, respectively, exhibited both UGT and CST activities. The dual substrate specificity for UDP-galactose and CMP-sialic acid of one such representative chimera was directly confirmed by in vitro measurement of the nucleotide sugar transport activity using a heterologous expression system in the yeast Saccharomyces cerevisiae. These findings indicated that the regions which are critical for determining the substrate specificity of UGT and CST resided in different submolecular sites in the two transporters, and that these different determinants could be present within one protein without interfering with each other's function. (+info)Dominant inheritance of sialuria, an inborn error of feedback inhibition. (6/99)
"French type" sialuria, a presumably dominant disorder that, until now, had been documented in only five patients, manifests with mildly coarse facies, slight motor delay, and urinary excretion of large quantities (>1 g/d) of free N-acetylneuraminic acid (NeuAc). The basic defect consists of the very rare occurrence of failed feedback inhibition of a rate-limiting enzyme, in this case uridinediphosphate-N-acetylglucosamine (UDP-GlcNAc) 2-epimerase, by a downstream product, in this case cytidine monophosphate (CMP)-NeuAc. We report a new patient with sialuria who has a heterozygous G-->A substitution in nucleotide 848 of the epimerase gene, which results in an R266Q change. The proband's other allele, as expected, had no mutation. However, the heterozygous R266Q mutation was detected in the patient's mother, who has similarly increased urinary levels of free NeuAc, thereby confirming, for the first time, the dominant mode of inheritance of this inborn error. The biochemical diagnosis of the proband was verified by the greatly increased level of free NeuAc in his cultured fibroblasts, the NeuAc distribution, mainly (59%) in the cytoplasm, and by the complete failure of 100 microM CMP-NeuAc to inhibit UDP-GlcNAc 2-epimerase activity in the mutant cells. These findings call for expansion of the phenotype to include adults and for more-extensive assaying of free NeuAc in the urine of children with mild developmental delay. The prevalence of sialuria is probably grossly underestimated. (+info)Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing. (7/99)
A significant proportion of the alpha2,6-sialyltransferase of protein Asn-linked glycosylation (ST6Gal I) forms disulfide-bonded dimers that exhibit decreased activity, but retain the ability to bind asialoglycoprotein substrates. Here, we have investigated the subcellular location and mechanism of ST6Gal I dimer formation, as well as the role of Cys residues in the enzyme's trafficking, localization, and catalytic activity. Pulse-chase analysis demonstrated that the ST6Gal I disulfide-bonded dimer forms in the endoplasmic reticulum. Mutagenesis experiments showed that Cys-24 in the transmembrane region is required for dimerization, while catalytic domain Cys residues are required for trafficking and catalytic activity. Replacement of Cys-181 and Cys-332 generated proteins that are largely retained in the endoplasmic reticulum and minimally active or inactive, respectively. Replacement of Cys-350 or Cys-361 inactivated the enzyme without compromising its localization or processing, suggesting that these amino acids are part of the enzyme's active site. Replacement of Cys-139 or Cys-403 generated proteins that are catalytically active and appear to be more stably localized in the Golgi, since they exhibited decreased cleavage and secretion. The Cys-139 mutant also exhibited increased dimer formation suggesting that ST6Gal I dimers may be critical in the oligomerization process involved in stable ST6Gal I Golgi localization. (+info)Mannose-binding lectin accelerates complement activation and increases serum killing of Neisseria meningitidis serogroup C. (8/99)
The capacity for different lipo-oligosaccharide (LOS) sialylation patterns of Neisseria meningitidis serogroup C to influence the binding and function of the innate humoral component, mannose-binding lectin (MBL), was investigated. By use of flow cytometry and immunogold electron microscopy, a clinical isolate with reduced endogenous LOS sialylation was found to bind more MBL than did strains with higher endogenous sialylation. MBL binding was reduced but not ablated if the same strain was allowed to exogenously sialylate its LOS structures after incubation with cytidine-5'-monophospho-neuraminic acid. MBL binding led to an increased rate of complement activation, with enhanced deposition of the complement components C4 and C5b-9, and this correlated with an increase in bactericidal activity. LOS sialylation appears to be an important determinant of MBL binding to N. meningitidis and can modulate complement-dependent killing of the bacterium. These findings could explain the observed susceptibility to meningococcal disease of individuals genetically deficient in MBL. (+info)Cytidine monophosphate (CMP) is a nucleotide that consists of a cytosine molecule attached to a ribose sugar molecule, which in turn is linked to a phosphate group. It is one of the four basic building blocks of RNA (ribonucleic acid) along with adenosine monophosphate (AMP), guanosine monophosphate (GMP), and uridine monophosphate (UMP). CMP plays a critical role in various biochemical reactions within the body, including protein synthesis and energy metabolism.
Deoxycytidine monophosphate (dCMP) is a nucleotide that is a building block of DNA. It consists of the sugar deoxyribose, the base cytosine, and one phosphate group. Nucleotides like dCMP are linked together through the phosphate groups to form long chains of DNA. In this way, dCMP plays an essential role in the structure and function of DNA, including the storage and transmission of genetic information.
Nucleoside-phosphate kinase (NPK) is an enzyme that plays a crucial role in the synthesis and metabolism of nucleotides, which are the building blocks of DNA and RNA. NPK catalyzes the transfer of a phosphate group from a donor molecule, typically ATP, to a nucleoside or deoxynucleoside, forming a nucleoside monophosphate (NMP) or deoxynucleoside monophosphate (dNMP).
There are several isoforms of NPK found in different cellular compartments and tissues, each with distinct substrate specificities. These enzymes play essential roles in maintaining the balance of nucleotides required for various cellular processes, including DNA replication, repair, and transcription, as well as RNA synthesis and metabolism.
Abnormalities in NPK activity or expression have been implicated in several human diseases, such as cancer, viral infections, and neurological disorders. Therefore, understanding the function and regulation of NPK is crucial for developing novel therapeutic strategies to target these conditions.
Cytidine monophosphate N-acetylneuraminic acid, often abbreviated as CMP-Neu5Ac or CMP-NANA, is a nucleotide sugar that plays a crucial role in the biosynthesis of complex carbohydrates known as glycoconjugates. These molecules are important components of cell membranes and have various functions, including cell recognition and communication.
CMP-Neu5Ac is formed from N-acetylneuraminic acid (Neu5Ac) and cytidine triphosphate (CTP) in a reaction catalyzed by the enzyme CMP-sialic acid synthetase. Once synthesized, CMP-Neu5Ac serves as the activated donor of Neu5Ac residues in the process of glycosylation, where Neu5Ac is added to the non-reducing end of oligosaccharide chains on glycoproteins and gangliosides. This reaction is catalyzed by sialyltransferases, a family of enzymes that use CMP-Neu5Ac as their substrate.
Abnormal levels or functions of CMP-Neu5Ac and its associated enzymes have been implicated in various diseases, including cancer, neurodevelopmental disorders, and microbial infections. Therefore, understanding the biology of CMP-Neu5Ac and its role in glycosylation is essential for developing new therapeutic strategies to target these conditions.
Cytidine is a nucleoside, which consists of the sugar ribose and the nitrogenous base cytosine. It is an important component of RNA (ribonucleic acid), where it pairs with guanosine via hydrogen bonding to form a base pair. Cytidine can also be found in some DNA (deoxyribonucleic acid) sequences, particularly in viral DNA and in mitochondrial DNA.
Cytidine can be phosphorylated to form cytidine monophosphate (CMP), which is a nucleotide that plays a role in various biochemical reactions in the body. CMP can be further phosphorylated to form cytidine diphosphate (CDP) and cytidine triphosphate (CTP), which are involved in the synthesis of lipids, glycogen, and other molecules.
Cytidine is also available as a dietary supplement and has been studied for its potential benefits in treating various health conditions, such as liver disease and cancer. However, more research is needed to confirm these potential benefits and establish safe and effective dosages.
Cytidine deaminase is an enzyme that catalyzes the removal of an amino group from cytidine, converting it to uridine. This reaction is part of the process of RNA degradation and also plays a role in the immune response to viral infections.
Cytidine deaminase can be found in various organisms, including bacteria, humans, and other mammals. In humans, cytidine deaminase is encoded by the APOBEC3 gene family, which consists of several different enzymes that have distinct functions and expression patterns. Some members of this gene family are involved in the restriction of retroviruses, such as HIV-1, while others play a role in the regulation of endogenous retroelements and the modification of cellular RNA.
Mutations in cytidine deaminase genes have been associated with various diseases, including cancer and autoimmune disorders. For example, mutations in the APOBEC3B gene have been linked to an increased risk of breast cancer, while mutations in other members of the APOBEC3 family have been implicated in the development of lymphoma and other malignancies. Additionally, aberrant expression of cytidine deaminase enzymes has been observed in some autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, suggesting a potential role for these enzymes in the pathogenesis of these conditions.
Cytidine triphosphate (CTP) is a nucleotide that plays a crucial role in the synthesis of RNA. It consists of a cytosine base, a ribose sugar, and three phosphate groups. Cytidine triphosphate is one of the four main building blocks of RNA, along with adenosine triphosphate (ATP), guanosine triphosphate (GTP), and uridine triphosphate (UTP). These nucleotides are essential for various cellular processes, including energy transfer, signal transduction, and biosynthesis. CTP is also involved in the regulation of several metabolic pathways and serves as a cofactor for enzymes that catalyze biochemical reactions. Like other triphosphate nucleotides, CTP provides energy for cellular functions by donating its phosphate groups in energy-consuming processes.
Cytosine nucleotides are the chemical units or building blocks that make up DNA and RNA, one of the four nitrogenous bases that form the rung of the DNA ladder. A cytosine nucleotide is composed of a cytosine base attached to a sugar molecule (deoxyribose in DNA and ribose in RNA) and at least one phosphate group. The sequence of these nucleotides determines the genetic information stored in an organism's genome. In particular, cytosine nucleotides pair with guanine nucleotides through hydrogen bonding to form base pairs that are held together by weak interactions. This pairing is specific and maintains the structure and integrity of the DNA molecule during replication and transcription.
Bimal Kumar Bachhawat
CMAS (gene)
CMAH
CMP-N-acetylneuraminate monooxygenase
List of MeSH codes (D09)
CMP-N-acylneuraminate phosphodiesterase
CMAS
List of MeSH codes (D02)
N-acylneuraminate cytidylyltransferase
Sialic acid
List of MeSH codes (D13)
Bimal Kumar Bachhawat - Wikipedia
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Synthetase2
- Cytidine monophosphate (CMP) N-acetylneuraminic acid (NeuNAc) synthetase, which is encoded by the neuA gene, can catalyze the activation of sialic acid with CMP, and plays an important role in Streptococcus agalactiae infection pathogenesis. (geneticsmr.com)
- Then, bile acyl-CoA synthetase teams up with 3a,7a-dihydroxycoprostanic acid to create 3a,7a-dihydroxy-5b-cholestanoyl-CoA. (smpdb.ca)
Amino acids6
- On his return to India, he focused his studies on amino acids and inorganic sulphate metabolism, as well as glycosaminoglycan. (wikipedia.org)
- The results showed that the neuA nucleotide sequence con-tained a complete coding region, which comprised 1242 bp, encoding 413 amino acids (aa). (geneticsmr.com)
- D-Amino acids have been show to be present in high concentrations in humans and play a role in biological functions. (smpdb.ca)
- D-Amino acid oxidase (DAAO) is one of the main enzymes that metabolize D-Amino acids via deamination. (smpdb.ca)
- DAAO is highly specific towards D-amino acids and favours free neutral D-amino acids or those with hydrophobic, polar or aromatic groups. (smpdb.ca)
- Acidic amino acids are not catalyze by DAOO. (smpdb.ca)
Nucleotide2
- Molecular characterization analyses of the neuA nucleotide amino acid sequence were performed using bioinformatic tools and an online server. (geneticsmr.com)
- CMP-β-D- N -Acetlylneuraminic acid (CMP-Neu5Ac) is a nucleotide sugar and the donor substrate for eukaryotic and prokaryotic sialyltransferases. (biolog.de)
Biosynthesis1
- Dive into the research topics of 'Sialic acid-like sugars in Archaea: Legionaminic acid biosynthesis in the halophile Halorubrum sp. (bgu.ac.il)
Sialic1
- The aa sequence was highly conserved and contained a Glyco_tranf_GTA_type superfamily and an SGNH_hydrolase superfam-ily conserved domain, which are related to sialic acid activation catalysis. (geneticsmr.com)
Important2
Alpha3
- L-Lysine and oxoglutaric acid will be combined to form saccharopine by facilitation of mitochondrial alpha-aminoadipic semialdehyde synthase, and then, mitochondrial alpha-aminoadipic semialdehyde synthase will further breaks saccharopine down to allysine and glutamic acid. (smpdb.ca)
- Allysine will be degraded to form aminoadipic acid through alpha-aminoadipic semialdehyde dehydrogenase. (smpdb.ca)
- Oxoadipic acid is formed from catalyzation of mitochondrial kynurenine/alpha-aminoadipate aminotransferase on aminoadipic acid. (smpdb.ca)
Nucleoside monophosphate2
Kinase8
- 1. Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates. (nih.gov)
- 2. Phosphorylation of Cytidine, Deoxycytidine, and Their Analog Monophosphates by Human UMP/CMP Kinase Is Differentially Regulated by ATP and Magnesium. (nih.gov)
- 5. Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme. (nih.gov)
- 13. Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase. (nih.gov)
- 17. Kinetic mechanism and energetics of binding of phosphoryl group acceptors to Mycobacterium tuberculosis cytidine monophosphate kinase. (nih.gov)
- In this study, we developed a cell-free regeneration of ATP based on polyphosphate kinase 2 (PPK2) to manufacture 5'-CMP from cytidine (CR). (bvsalud.org)
- McPPK2 and LhUCK (a uridine-cytidine kinase from Lactobacillus helveticus) were combined to convert CR to 5'-CMP. (bvsalud.org)
- The wider applicability of this cell-free system was demonstrated in the synthesis of deoxycytidine 5'-monophosphate (5'-dCMP) from deoxycytidine (dCR) by incorporating McPPK2 and BsdCK (a deoxycytidine kinase from Bacillus subtilis). (bvsalud.org)
Sialic acid4
- All GBS capsules have a terminal alpha 2-3-linked sialic acid [N-acetylneuraminic acid (Neu5Ac)], which interferes with complement-mediated killing. (nih.gov)
- 7. Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-Sialyltransferase is related to poor patient survival in human colorectal carcinomas. (nih.gov)
- 8. Genetically altered mice with different sialyltransferase deficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetylation. (nih.gov)
- 14. A novel viral alpha2,3-sialyltransferase (v-ST3Gal I): transfer of sialic acid to fucosylated acceptors. (nih.gov)
Deoxycytidine1
- Towards this question, three nucleotide complexes based on 2'-deoxycytidine-5'-monophosphate (dCMP) and cytidine-5'-monophosphate (CMP) were synthesized in different solvents and pH values, and an unusual cytosine-cytosine base paring pattern (named full C : C base pairing) has been successfully obtained. (bvsalud.org)
Amino1
- On his return to India, he focused his studies on amino acids and inorganic sulphate metabolism, as well as glycosaminoglycan. (wikipedia.org)
Synthesis2
- 9. Reversible sialylation: synthesis of cytidine 5'-monophospho-N-acetylneuraminic acid from cytidine 5'-monophosphate with alpha2,3-sialyl O-glycan-, glycolipid-, and macromolecule-based donors yields diverse sialylated products. (nih.gov)
- Palmitate is incorporated into cholesteryl esters: The parasite contains acyl-CoA:cholesterol acyltransferase (ACAT) and host fatty acids and low-density lipoproteins directly serve as Toxoplasma ACAT activators by stimulating cholesteryl ester synthesis and lipid droplet biogenesis. (polygenicpathways.co.uk)
Sialyltransferase1
- CMP-N-acetylneuraminic acid:lactosylceramide (α2-3) sialyltransferase (G(M3)-synthase) was purified to homogeneity from a Triton CF-54 extract of young rat brain. (elsevierpure.com)
Production2
- 18. Production of cytidine 5'-monophosphate N-acetylneuraminic acid using recombinant Escherichia coli as a biocatalyst. (nih.gov)
- Cytidine 5'-monophosphate (5'-CMP), a key intermediate for the production of nucleotide derivatives, has been extensively used in food, agriculture, and medicine industries. (bvsalud.org)
Cell2
- 1. Cell surface n-acetylneuraminic acid alpha2,3-galactoside-dependent intercellular adhesion of human colon cancer cells. (nih.gov)
- Humans lack the common mammalian cell surface molecule N-glycolylneuraminic acid (Neu5Gc) due to a CMAH gene inactivation, which occurred approximately three million years ago. (anthropogeny.org)
Specific1
- Final purification of G(M3)-synthase was achieved by chromatography on a 'lactosylceramide acid'-Sepharose column and specific elution with lactosylceramide. (elsevierpure.com)