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

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Published: 4 June 2021
Last updated: 19 February 2023

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1

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
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2

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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3

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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4

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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5

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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6

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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7

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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8

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
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9

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 s
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10

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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11

Liu, Jennifer Lin Chun, Gwo Jenn Shen, Yoshitaka Ichikawa, James F. Rutan, Gerardo Zapata, Willie F. Vann, and Chi Huey Wong. "Overproduction of CMP-sialic acid synthetase for organic synthesis." Journal of the American Chemical Society 114, no. 10 (May 1992): 3901–10. http://dx.doi.org/10.1021/ja00036a044.

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12

Viswanathan, Karthik, Noboru Tomiya, Jung Park, Sundeep Singh, Yuan C. Lee, Karen Palter, and Michael J. Betenbaugh. "Expression of a Functional Drosophila melanogaster CMP-sialic Acid Synthetase." Journal of Biological Chemistry 281, no. 23 (March 14, 2006): 15929–40. http://dx.doi.org/10.1074/jbc.m512186200.

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13

Yu, Ching-Ching, Po-Chiao Lin, and Chun-Cheng Lin. "Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles and its use in the synthesis of CMP-sialic acid." Chemical Communications, no. 11 (2008): 1308. http://dx.doi.org/10.1039/b716330d.

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14

Misaki, Ryo, Kazuhito Fujiyama, and Tatsuji Seki. "Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell." Biochemical and Biophysical Research Communications 339, no. 4 (January 2006): 1184–89. http://dx.doi.org/10.1016/j.bbrc.2005.11.130.

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15

Mertsalov, Ilya B., Boris N. Novikov, Hilary Scott, Lawrence Dangott, and Vladislav M. Panin. "Characterization of Drosophila CMP-sialic acid synthetase activity reveals unusual enzymatic properties." Biochemical Journal 473, no. 13 (June 28, 2016): 1905–16. http://dx.doi.org/10.1042/bcj20160347.

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DmCSAS has unique localization in the cell secretory compartment. Our results demonstrated that DmCSAS has unusual enzymatic properties that revealed evolutionary adaptation to the milieu of the Golgi compartment and suggested mechanisms that control sialylation in insect organisms.
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16

Lewis, Amanda L., Hongzhi Cao, Silpa K. Patel, Sandra Diaz, Wesley Ryan, Aaron F. Carlin, Vireak Thon, et al. "NeuA Sialic Acid O-Acetylesterase Activity Modulates O-Acetylation of Capsular Polysaccharide in Group B Streptococcus." Journal of Biological Chemistry 282, no. 38 (July 23, 2007): 27562–71. http://dx.doi.org/10.1074/jbc.m700340200.

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Group B Streptococcus (GBS) is a common cause of neonatal sepsis and meningitis. A major GBS virulence determinant is its sialic acid (Sia)-capped capsular polysaccharide. Recently, we discovered the presence and genetic basis of capsular Sia O-acetylation in GBS. We now characterize a GBS Sia O-acetylesterase that modulates the degree of GBS surface O-acetylation. The GBS Sia O-acetylesterase operates cooperatively with the GBS CMP-Sia synthetase, both part of a single polypeptide encoded by the neuA gene. NeuA de-O-acetylation of free 9-O-acetyl-N-acetylneuraminic acid (Neu5,9Ac2) was enhanc
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17

Wong, Jessica H., Urvashi Sahni, Yanhong Li, Xi Chen, and Jacquelyn Gervay-Hague. "Synthesis of sulfone-based nucleotide isosteres: identification of CMP-sialic acid synthetase inhibitors." Org. Biomol. Chem. 7, no. 1 (2009): 27–29. http://dx.doi.org/10.1039/b819155g.

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18

Karwaski, Marie-France, Warren W. Wakarchuk, and Michel Gilbert. "High-level expression of recombinant Neisseria CMP-sialic acid synthetase in Escherichia coli." Protein Expression and Purification 25, no. 2 (July 2002): 237–40. http://dx.doi.org/10.1016/s1046-5928(02)00004-9.

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19

Urbanek, Kelly, Danica M. Sutherland, Robert C. Orchard, Craig B. Wilen, Jonathan J. Knowlton, Pavithra Aravamudhan, Gwen M. Taylor, Herbert W. Virgin, and Terence S. Dermody. "Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase and Solute Carrier Family 35 Member A1 Are Required for Reovirus Binding and Infection." Journal of Virology 95, no. 2 (October 21, 2020): e01571-20. http://dx.doi.org/10.1128/jvi.01571-20.

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ABSTRACTEngagement of cell surface receptors by viruses is a critical determinant of viral tropism and disease. The reovirus attachment protein σ1 binds sialylated glycans and proteinaceous receptors to mediate infection, but the specific requirements for different cell types are not entirely known. To identify host factors required for reovirus-induced cell death, we conducted a CRISPR-knockout screen targeting over 20,000 genes in murine microglial BV2 cells. Candidate genes required for reovirus to cause cell death were highly enriched for sialic acid synthesis and transport. Two of the top
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20

Mosimann, Steven C., Michel Gilbert, Dennise Dombroswki, Rebecca To, Warren Wakarchuk, and Natalie C. J. Strynadka. "Structure of a Sialic Acid-activating Synthetase, CMP-acylneuraminate Synthetase in the Presence and Absence of CDP." Journal of Biological Chemistry 276, no. 11 (December 11, 2000): 8190–96. http://dx.doi.org/10.1074/jbc.m007235200.

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21

Swords, W. Edward, Miranda L. Moore, Luciana Godzicki, Gail Bukofzer, Michael J. Mitten, and Jessica VonCannon. "Sialylation of Lipooligosaccharides Promotes Biofilm Formation by Nontypeable Haemophilus influenzae." Infection and Immunity 72, no. 1 (January 2004): 106–13. http://dx.doi.org/10.1128/iai.72.1.106-113.2004.

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ABSTRACT Nontypeable Haemophilus influenzae (NTHi) is a major cause of opportunistic respiratory tract infections, including otitis media and bronchitis. The persistence of NTHi in vivo is thought to involve bacterial persistence in a biofilm community. Therefore, there is a need for further definition of bacterial factors contributing to biofilm formation by NTHi. Like other bacteria inhabiting host mucosal surfaces, NTHi has on its surface a diverse array of lipooligosaccharides (LOS) that influence host-bacterial interactions. In this study, we show that LOS containing sialic (N-acetyl-neur
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22

Matthews, Melissa M., John B. McArthur, Yanhong Li, Hai Yu, Xi Chen, and Andrew J. Fisher. "Catalytic Cycle of Neisseria meningitidis CMP-Sialic Acid Synthetase Illustrated by High-Resolution Protein Crystallography." Biochemistry 59, no. 34 (October 4, 2019): 3157–68. http://dx.doi.org/10.1021/acs.biochem.9b00517.

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23

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 15, 1999): 397. http://dx.doi.org/10.1042/0264-6021:3430397.

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24

Kalpana. "BIOTRANSFORMATION USING RECOMBINANT CMP SIALIC ACID SYNTHETASE AND α-2, 6-SIALYLTRAN SFERASE: ENZYMATIC SYNTHESIS OF SIALOSIDES." American Journal of Biochemistry and Biotechnology 8, no. 4 (April 1, 2012): 288–303. http://dx.doi.org/10.3844/ajbbsp.2012.288.303.

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25

Fujita, Akiko, Chihiro Sato, and Ken Kitajima. "Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase." Biochemical and Biophysical Research Communications 355, no. 1 (March 2007): 174–80. http://dx.doi.org/10.1016/j.bbrc.2007.01.139.

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26

Knorst, Marion, and Wolf-Dieter Fessner. "CMP-Sialate Synthetase fromNeisseria meningitidis− Overexpression and Application to the Synthesis of Oligosaccharides Containing Modified Sialic Acids." Advanced Synthesis & Catalysis 343, no. 6-7 (August 2001): 698–710. http://dx.doi.org/10.1002/1615-4169(200108)343:6/7<698::aid-adsc698>3.0.co;2-j.

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27

Greiner, L. L., H. Watanabe, N. J. Phillips, J. Shao, A. Morgan, A. Zaleski, B. W. Gibson, and M. A. Apicella. "Nontypeable Haemophilus influenzae Strain 2019 Produces a Biofilm Containing N-Acetylneuraminic Acid That May Mimic Sialylated O-Linked Glycans." Infection and Immunity 72, no. 7 (July 2004): 4249–60. http://dx.doi.org/10.1128/iai.72.7.4249-4260.2004.

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ABSTRACT Previous studies suggested that nontypeable Haemophilus influenzae (NTHI) can form biofilms during human and chinchilla middle ear infections. Microscopic analysis of a 5-day biofilm of NTHI strain 2019 grown in a continuous-flow chamber revealed that the biofilm had a diffuse matrix interlaced with multiple water channels. Our studies showed that biofilm production was significantly decreased when a chemically defined medium lacking N-acetylneuraminic acid (sialic acid) was used. Based on these observations, we examined mutations in seven NTHI strain 2019 genes involved in carbohydra
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28

Nakata, D., A. K. Munster, R. Gerardy-Schahn, N. Aoki, T. Matsuda, and K. Kitajima. "Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates." Glycobiology 11, no. 8 (August 1, 2001): 685–92. http://dx.doi.org/10.1093/glycob/11.8.685.

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29

Tiralongo, J., A. Fujita, C. Sato, K. Kitajima, F. Lehmann, M. Oschlies, R. Gerardy-Schahn, and A. K. Munster-Kuhnel. "The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme." Glycobiology 17, no. 9 (April 18, 2007): 945–54. http://dx.doi.org/10.1093/glycob/cwm064.

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30

Spinola, Stanley M., Wei Li, Kate R. Fortney, Diane M. Janowicz, Beth Zwickl, Barry P. Katz, and Robert S. Munson. "Sialylation of Lipooligosaccharides Is Dispensable for the Virulence of Haemophilus ducreyi in Humans." Infection and Immunity 80, no. 2 (December 5, 2011): 679–87. http://dx.doi.org/10.1128/iai.05826-11.

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ABSTRACTSialylated glycoconjugates on the surfaces of mammalian cells play important roles in intercellular communication and self-recognition. The sialic acid preferentially expressed in human tissues isN-acetylneuraminic acid (Neu5Ac). In a process called molecular mimicry, many bacterial pathogens decorate their cell surface glycolipids with Neu5Ac. Incorporation of Neu5Ac into bacterial glycolipids promotes bacterial interactions with host cell receptors called Siglecs. These interactions affect bacterial adherence, resistance to serum killing and phagocytosis, and innate immune responses.
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31

Ganguli, S., G. Zapata, T. Wallis, C. Reid, G. Boulnois, W. F. Vann, and I. S. Roberts. "Molecular cloning and analysis of genes for sialic acid synthesis in Neisseria meningitidis group B and purification of the meningococcal CMP-NeuNAc synthetase enzyme." Journal of Bacteriology 176, no. 15 (1994): 4583–89. http://dx.doi.org/10.1128/jb.176.15.4583-4589.1994.

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32

Niculovic, Kristina M., Linda Blume, Henri Wedekind, Elina Kats, Iris Albers, Stephanie Groos, Markus Abeln, et al. "Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS." Journal of the American Society of Nephrology 30, no. 6 (April 30, 2019): 1021–35. http://dx.doi.org/10.1681/asn.2018090951.

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BackgroundThe etiology of steroid-resistant nephrotic syndrome, which manifests as FSGS, is not completely understood. Aberrant glycosylation is an often underestimated factor for pathologic processes, and structural changes in the glomerular endothelial glycocalyx have been correlated with models of nephrotic syndrome. Glycans are frequently capped by sialic acid (Sia), and sialylation’s crucial role for kidney function is well known. Human podocytes are highly sialylated; however, sialylation’s role in podocyte homeostasis remains unclear.MethodsWe generated a podocyte-specific sialylation-d
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33

Knorst, Marion, and Wolf-Dieter Fessner. "ChemInform Abstract: Enzymes in Organic Synthesis. Part 18. CMP-Sialate Synthetase from Neisseria meningitidis - Overexpression and Application to the Synthesis of Oligosaccharides Containing Modified Sialic Acids." ChemInform 32, no. 49 (May 23, 2010): no. http://dx.doi.org/10.1002/chin.200149247.

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34

Mizanur, Rahman M., and Nicola L. Pohl. "Bacterial CMP-sialic acid synthetases: production, properties, and applications." Applied Microbiology and Biotechnology 80, no. 5 (October 2008). http://dx.doi.org/10.1007/s00253-008-1643-7.

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35

Di, Wu, Akiko Fujita, Kayo Hamaguchi, Philippe Delannoy, Chihiro Sato, and Ken Kitajima. "Diverse subcellular localizations of the insect CMP-sialic acid synthetases." Glycobiology, December 16, 2016. http://dx.doi.org/10.1093/glycob/cww128.

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36

Ng, Preston S. K., Christopher J. Day, John M. Atack, Lauren E. Hartley-Tassell, Linda E. Winter, Tal Marshanski, Vered Padler-Karavani, et al. "NontypeableHaemophilus influenzaeHas Evolved Preferential Use ofN-Acetylneuraminic Acid as a Host Adaptation." mBio 10, no. 3 (May 7, 2019). http://dx.doi.org/10.1128/mbio.00422-19.

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ABSTRACTNontypeableHaemophilus influenzae(NTHi) is a Gram-negative bacterial pathogen that is adapted exclusively to human hosts. NTHi utilizes sialic acid from the host as a carbon source and as a terminal sugar on the outer membrane glycolipid lipooligosaccharide (LOS). Sialic acid expressed on LOS is critical in NTHi biofilm formation and immune evasion. There are two major forms of sialic acids in most mammals,N-acetylneuraminic acid (Neu5Ac) andN-glycolylneuraminic acid (Neu5Gc), the latter of which is derived from Neu5Ac. Humans lack the enzyme to convert Neu5Ac to Neu5Gc and do not expre
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37

Wu, Di, Hiromu Arakawa, Akiko Fujita, Hisashi Hashimoto, Masahiko Hibi, Kiyoshi Naruse, Yasuhiro Kamei, Chihiro Sato, and Ken Kitajima. "A point-mutation in the C-domain of CMP-sialic acid synthetase leads to lethality of medaka due to protein insolubility." Scientific Reports 11, no. 1 (December 2021). http://dx.doi.org/10.1038/s41598-021-01715-3.

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AbstractVertebrate CMP-sialic acid synthetase (CSS), which catalyzes the synthesis of CMP-sialic acid (CMP-Sia), consists of a 28 kDa-N-domain and a 20 kDa-C-domain. The N-domain is known to be a catalytic domain; however, the significance of the C-domain still remains unknown. To elucidate the function of the C-domain at the organism level, we screened the medaka TILLING library and obtained medaka with non-synonymous mutations (t911a), or single amino acid substitutions of CSS, L304Q, in the C-domain. Prominently, most L304Q medaka was lethal within 19 days post-fertilization (dpf). L304Q yo
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38

Wu, Di, Pierre-André Gilormini, Sakura Toda, Christophe Biot, Cédric Lion, Yann Guérardel, Chihiro Sato, and Ken Kitajima. "A novel C-domain-dependent inhibition of the rainbow trout CMP-sialic acid synthetase activity by CMP-deaminoneuraminic acid." Biochemical and Biophysical Research Communications, May 2022. http://dx.doi.org/10.1016/j.bbrc.2022.05.031.

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39

Schelch, Sabine, Romana Koszagova, Jürgen Kuballa та Bernd Nidetzky. "Immobilization of CMP‐Sialic Acid Synthetase and α2,3‐Sialyltransferase for Cascade Synthesis of 3′‐Sialyl β‐D‐Galactoside with Enzyme Reuse". ChemCatChem, 30 березня 2022. http://dx.doi.org/10.1002/cctc.202101860.

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