Relevant bibliographies by topics / CMP-sialic acid synthetases

Academic literature on the topic 'CMP-sialic acid synthetases'

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Published: 4 June 2021
Last updated: 19 February 2023

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Journal articles on the topic "CMP-sialic acid synthetases"

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Münster, Anja-K., Matthias Eckhardt, Barry Potvin, Martina Mühlenhoff, Pamela Stanley, and Rita Gerardy-Schahn. "Mammalian cytidine 5′-monophosphateN-acetylneuraminic acid synthetase: A nuclear protein with evolutionarily conserved structural motifs." Proceedings of the National Academy of Sciences 95, no. 16 (August 4, 1998): 9140–45. http://dx.doi.org/10.1073/pnas.95.16.9140.

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Sialic acids of cell surface glycoproteins and glycolipids play a pivotal role in the structure and function of animal tissues. The pattern of cell surface sialylation is species- and tissue-specific, is highly regulated during embryonic development, and changes with stages of differentiation. A prerequisite for the synthesis of sialylated glycoconjugates is the activated sugar-nucleotide cytidine 5′-monophosphateN-acetylneuraminic acid (CMP-Neu5Ac), which provides a substrate for Golgi sialyltransferases. Although a mammalian enzymatic activity responsible for the synthesis of CMP-Neu5Ac has been described and the enzyme has been purified to near homogeneity, sequence information is restricted to bacterial CMP-Neu5Ac synthetases. In this paper, we describe the molecular characterization, functional expression, and subcellular localization of murine CMP-Neu5Ac synthetase. Cloning was achieved by complementation of the Chinese hamster ovarylec32mutation that causes a deficiency in CMP-Neu5Ac synthetase activity. A murine cDNA encoding a protein of 432 amino acids rescued thelec32mutation and also caused polysialic acid to be expressed in the capsule of the CMP-Neu5Ac synthetase negativeEscherichia colimutant EV5. Three potential nuclear localization signals were found in the murine synthetase, and immunofluorescence studies confirmed predominantly nuclear localization of an N-terminally Flag-tagged molecule. Four stretches of amino acids that occur in the N-terminal region are highly conserved in bacterial CMP-Neu5Ac synthetases, providing evidence for an ancestral relationship between the sialylation pathways of bacterial and animal cells.
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Munster-Kuhnel, A. K. "Structure and function of vertebrate CMP-sialic acid synthetases." Glycobiology 14, no. 10 (May 26, 2004): 43R—51R. http://dx.doi.org/10.1093/glycob/cwh113.

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Schaper, Wiebke, Joachim Bentrop, Jana Ustinova, Linda Blume, Elina Kats, Joe Tiralongo, Birgit Weinhold, Martin Bastmeyer, and Anja-K. Münster-Kühnel. "Identification and Biochemical Characterization of Two Functional CMP-Sialic Acid Synthetases inDanio rerio." Journal of Biological Chemistry 287, no. 16 (February 20, 2012): 13239–48. http://dx.doi.org/10.1074/jbc.m111.327544.

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Yu, Hai, Hui Yu, Rebekah Karpel, and Xi Chen. "Chemoenzymatic synthesis of CMP–sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP–sialic acid synthetases." Bioorganic & Medicinal Chemistry 12, no. 24 (December 2004): 6427–35. http://dx.doi.org/10.1016/j.bmc.2004.09.030.

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Oschlies, Melanie, Achim Dickmanns, Thomas Haselhorst, Wiebke Schaper, Katharina Stummeyer, Joe Tiralongo, Birgit Weinhold, et al. "A C-Terminal Phosphatase Module Conserved in Vertebrate CMP-Sialic Acid Synthetases Provides a Tetramerization Interface for the Physiologically Active Enzyme." Journal of Molecular Biology 393, no. 1 (October 2009): 83–97. http://dx.doi.org/10.1016/j.jmb.2009.08.003.

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Yu, Hai, Jie Zeng, Yanhong Li, Vireak Thon, Baojun Shi, and Xi Chen. "Effective one-pot multienzyme (OPME) synthesis of monotreme milk oligosaccharides and other sialosides containing 4-O-acetyl sialic acid." Organic & Biomolecular Chemistry 14, no. 36 (2016): 8586–97. http://dx.doi.org/10.1039/c6ob01706a.

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Chemoenzymatic synthesis: Monotreme milk glycans and other sialosides containing a 4-O-acetyl-sialic acid were synthesized in a gram or preparative scales using a one-pot two-enzyme sialylation system containing bacterial CMP-sialic acid synthetase and sialyltransferase PmST3.
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KEAN, E. "CMP-sialic acid synthetase of the nucleus." Biochimica et Biophysica Acta (BBA) - General Subjects 1673, no. 1-2 (July 2004): 56–65. http://dx.doi.org/10.1016/j.bbagen.2004.04.006.

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STOUGHTON, Daniel M., Gerardo ZAPATA, Robert PICONE, and Willie F. VANN. "Identification of Arg-12 in the active site of Escherichia coli K1 CMP-sialic acid synthetase." Biochemical Journal 343, no. 2 (October 8, 1999): 397–402. http://dx.doi.org/10.1042/bj3430397.

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Escherichia coli K1 CMP-sialic acid synthetase catalyses the synthesis of CMP-sialic acid from CTP and sialic acid. The active site of the 418 amino acid E. coli enzyme was localized to its N-terminal half. The bacterial CMP-sialic acid synthetase enzymes have a conserved motif, IAIIPARXXSKGLXXKN, at their N-termini. Several basic residues have been identified at or near the active site of the E. coli enzyme by chemical modification and site-directed mutagenesis. Only one of the lysines in the N-terminal motif, Lys-21, appears to be essential for activity. Mutation of Lys-21 in the N-terminal motif results in an inactive enzyme. Furthermore, Arg-12 of the N-terminal motif appears to be an active-site residue, based on the following evidence. Substituting Arg-12 with glycine or alanine resulted in inactive enzymes, indicating that this residue is required for enzymic activity. The Arg-12 → Lys mutant was partially active, demonstrating that a positive charge is required at this site. Steady-state kinetic analysis reveals changes in kcat, Km and Ks for CTP, which implicates Arg-12 in catalysis and substrate binding.
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Bose, Sucharita, Debayan Purkait, Deepthi Joseph, Vinod Nayak, and Ramaswamy Subramanian. "Structural and functional characterization of CMP-N-acetylneuraminate synthetase fromVibrio cholerae." Acta Crystallographica Section D Structural Biology 75, no. 6 (May 31, 2019): 564–77. http://dx.doi.org/10.1107/s2059798319006831.

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Several pathogenic bacteria utilize sialic acid, including host-derivedN-acetylneuraminic acid (Neu5Ac), in at least two ways: they use it as a nutrient source and as a host-evasion strategy by coating themselves with Neu5Ac. Given the significant role of sialic acid in pathogenesis and host-gut colonization by various pathogenic bacteria, includingNeisseria meningitidis,Haemophilus influenzae,Pasteurella multocidaandVibrio cholerae, several enzymes of the sialic acid catabolic, biosynthetic and incorporation pathways are considered to be potential drug targets. In this work, findings on the structural and functional characterization of CMP-N-acetylneuraminate synthetase (CMAS), a key enzyme in the incorporation pathway, fromVibrio choleraeare reported. CMAS catalyzes the synthesis of CMP-sialic acid by utilizing CTP and sialic acid. Crystal structures of the apo and the CDP-bound forms of the enzyme were determined, which allowed the identification of the metal cofactor Mg2+in the active site interacting with CDP and the invariant Asp215 residue. While open and closed structural forms of the enzyme from eukaryotic and other bacterial species have already been characterized, a partially closed structure ofV. choleraeCMAS (VcCMAS) observed upon CDP binding, representing an intermediate state, is reported here. The kinetic data suggest that VcCMAS is capable of activating the two most common sialic acid derivatives, Neu5Ac and Neu5Gc. Amino-acid sequence and structural comparison of the active site of VcCMAS with those of eukaryotic and other bacterial counterparts reveal a diverse hydrophobic pocket that interacts with the C5 substituents of sialic acid. Analyses of the thermodynamic signatures obtained from the binding of the nucleotide (CTP) and the product (CMP-sialic acid) to VcCMAS provide fundamental information on the energetics of the binding process.
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Li, Yanhong, Hai Yu, Hongzhi Cao, Saddam Muthana, and Xi Chen. "Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity." Applied Microbiology and Biotechnology 93, no. 6 (October 4, 2011): 2411–23. http://dx.doi.org/10.1007/s00253-011-3579-6.

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Dissertations / Theses on the topic "CMP-sialic acid synthetases"

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Abu-Izneid, Tareq, and n/a. "The Synthesis and Evaluation of Functionalised Carbohydrates as Probes of Tumour Metastasis." Griffith University. Institute for Glycomics, 2005. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20061019.111424.

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Sialyltransferases, CMP-sialic acid synthetases and CMP-sialic acid transport proteins play a crucial role in the construction of cell surface glycoconjugates. These proteins also have a pivotal role to play in a number of diseases, including cancer. The sialyltransferase enzymes are responsible for transfering sialic acids from the donor substrate (CMP-sialic acid) to growing cell surface glycoconjugate chains within the Golgi apparatus. The CMP-sialic acid synthetase enzymes are responsible for the synthesis of the CMP-sialic acid, the donor substrate of the sialyltransferases in the nucleus, while the CMP-sialic acid transport proteins are responsible for transporting CMP-sialic acid from the Cytosol to the Golgi apparatus. When these proteins function in an abnormal way, hypersialylation results, leading to an increased level of sialylation on the cell surface. This increased level of sialylation aids in the detachment of primary tumour cells due to an increase in the level of overall negative charge, causing repulsion between the cancer cells. Therefore, the sialyltransferase enzymes, CMP-sialic acid synthetases and CMP-sialic acid transport proteins are intimately involved in the metastatic cascade associated with cancer. Chapter 1 provides a general introduction of cancer metastasis, discussing the roles of three target proteins (CMP-sialic acid synthetases, CMP-sialic acid transport proteins and sialyltransferases), as well as discussing their substrate specificities, with an emphasis on their involvements in cancer metastasis. The Chapter concludes with an overview of the types of compounds intended to be utilised as probes or inhibitors of these proteins. Chapter 2 describes the general approach towards the synthesis of CMP-Neu5Ac mimetics with a sulfur linkage in the presence of a phosphate group in the general structure 38. The precursor phosphoramidite derivative 45 was prepared and isolated in a good yield using Py.TFA. Unfortunately, the target compound 38 could not be prepared. Chapter 3 describes an alternative strategy wherein S-linked sialylnucleoside mimetics, of the general structure 39, with a sulfur linkage, but no phosphate group, between the sialylmimetic and the ribose moiety in the base is targeted. A series of these S-linked sialylnucleoside mimetics were successfully prepared. Cytidine, uridine, adenosine and 5-fluorouridine nucleosides were used to create a library of different nucleosides and with structural variability also present in the sialylmimetic portion. This small 'library' of 15 compounds was designed to shed light on the interaction of these compounds with the binding sites of the sialyltranferase, CMP-sialic acid synthetase and/or CM-sialic acid transport protein. Approaches towards the synthesis of O-linked sialylnucleoside mimetics of the general structure 40 are described in Chapter 4. Several methodologies are reported, as well as protecting group manipulations, for successful preparation of these sialylnucleoside mimetics. Cytidine and uridine were employed as the nucleosides, thus allowing a direct comparison between the O- and S-linked sialylnucleoside mimetics in biological evaluation. It appears from these synthetic investigations that gaining access into the O-linked series is not as straightforward as for the S-linked series, with alternative protecting group strategies required for the different nucleosides. The biological evaluation of some of the compounds reported in Chapters 3 and 4 is detailed in Chapter 5. The sialylnucleoside mimetics were evaluated, by 1H NMR spectroscopy, for their ability to inhibit CMP-KDN synthetase. In addition, an initial 1H NMR spectroscopic-based assay was investigated for inhibition studies of α(2,6)sialyltranferase in the absence of potential inhibitors. The final chapter (Chapter 6) brings together full experimental details in support of the compounds described in the preceding Chapters.
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Yu, Ching-Ching, and 游景晴. "Site-Specific CMP-Sialic Acid Synthetase Immobilized Magnetic Nanoparticle and Its Application in Organic Synthesis." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/34913132745834592014.

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碩士
國立清華大學
化學系
95
CMP-sialic acid synthetase ( CSS ) was immobilized on magnetic nanoparticles ( MNPs ) by combining the intein expression system and native chemical ligation. Without tedious enzyme purification steps, the enzyme was site specifically and covalently immobilized via its C terminus to MNP and could be directly separated from aqueous solution by a magnet. The MNP-CSS was stable for long-term storage ( 30 days at 4 oC ) and could be reused without loss of activity. Compared with conventional immobilization by random amide bond formation, our method of site-specific immobilization of CSS yielded much higher activity. These features of MNP-CSS suggest that it, and similarly immobilized enzymes, may be amenable to practical applications in organic synthesis.
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Oschlies, Melanie [Verfasser]. "Murine CMP-sialic acid synthetase : structural analysis of the C-terminal domain and biochemical characterisation of nuclear localisation / von Melanie Oschlies." 2008. http://d-nb.info/999015273/34.

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Carnahan, Mindy. "Elucidating the Functions of the Sialylation Pathway in Drosophila melanogaster." Thesis, 2011. http://hdl.handle.net/1969.1/ETD-TAMU-2011-08-9768.

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Sialylation is an important carbohydrate modification of glycoconjugates, which introduces sialic acids (SA). The relatively large nine-carbon, negatively charged sugars are typically located at the termini of carbohydrate chains. SA's are often required for functionally important molecular and cellular interactions including virus-host interactions, tumor progression and malignancy, immune system development and function, and nervous system development and function. However, the study of sialylation in vertebrates, including man, encounters serious obstacles associated with the complexity of vertebrates' biology and limitations of available experimental approaches. Drosophila is a useful model system with many advantages including quick generation time, a large number of progeny, simplified glycosylation and neurophysiology, and ease of genetic manipulations. The primary focus of this thesis is on the functions of Drosophila melanogaster CMP sialic acid synthetase (DmCSAS) and sialyltransferase (DSiaT) in the central nervous system (CNS). A combination of genetic, immunostaining, and neurobiology approaches were used to characterize the functions of DmCSAS and DSiaT in Drosophila. This investigation revealed the expression of DmCSAS and suggested that it plays an important role in a specialized and developmentally regulated process in the nervous system of Drosophila. Further experiments examined sub-cellular localization of DmCSAS revealing that this protein has a complex mostly Golgi-associated distribution within the cell in vivo. I discovered a novel link between Drosophila sialylation and circadian rhythm regulation. I also characterized the electrophysiological phenotypes of DmCSAS mutants and compared them to the corresponding defects associated with DSiaT mutations. My experiments also revealed that the relationship between DmCSAS and DSiaT are more complex than originally thought; these genes may have independent functions while also participating in the same pathway. Taken together, these results elucidate the sialylation pathway in Drosophila and shed more light on the role of sialylation in the nervous system. My experiments provide a unique evolutionary perspective on the sialylation pathway in animals and suggest that the neural function of SA in Drosophila can be conserved in vertebrates, including humans.
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Book chapters on the topic "CMP-sialic acid synthetases"

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Sellmeier, Melanie, Birgit Weinhold, and Anja Münster-Kühnel. "CMP-Sialic Acid Synthetase: The Point of Constriction in the Sialylation Pathway." In Topics in Current Chemistry, 139–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/128_2013_477.

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