This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Shaw, L.; Schauer, R.: The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid. Biol. Chem. Hoppe-Seyler, 369, 477–486 (1988)
Shaw, L.; Schauer, R.: Detection of CMP-N-acetylneuraminic acid hydroxylase activity in fractionated mouse liver. Biochem. J., 263, 355–363 (1989)
Kozutsumi, Y.; Kawano, T.; Yamakawa, T.; Suzuki, A.: Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol. J. Biochem., 108, 704–706 (1990)
Muchmore, E.A.; Milewski, M.; Varki, A.; Diaz, S.: Biosynthesis of N-glycolyneuraminic acid. The primary site of hydroxylation of N-acetylneuraminic acid is the cytosolic sugar nucleotide pool. J. Biol. Chem., 264, 20216–20223 (1989)
Bergwerff, A.A.; Hulleman, S.H.D.; Kamerling, J.P.; Vliegenthart, J.F.G.; Shaw, L.; Reuter, G.; Schauer, R.: Nature and biosynthesis of sialic acids in the starfish Asterias rubens. Identification of sialo-oligomers and detection of S-adenosyl-l-methionine: N-acylneuraminate 8-O-methyltransferase and CMP-N-acetylneuraminate monooxygenase activities. Biochimie, 74, 25–37 (1992)
Schlenzka, W.; Shaw, L.; Kelm, S.; Schmidt, C.L.; Bill, E.; Trautwein, A.X.; Lottspeich, F.; Schauer, R.: CMP-N-acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron-sulfur protein to be described in Eukarya. FEBS Lett., 385, 197–200 (1996)
Shaw, L.; Schneckenburger, P.; Schlenzka, W.; Carlsen, J.; Christiansen, K.; Juergensen, D.; Schauer, R.: CMP-N-acetylneuraminic acid hydroxylase from mouse liver and pig submandibular glands. Interaction with membrane-bound and soluble cytochrome b5-dependent electron transport chains. Eur. J. Biochem., 219, 1001–1011 (1994)
Martensen, I.; Schauer, R.; Shaw, L.: Cloning and expression of a membrane-bound CMP-N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens. Eur. J. Biochem., 268, 5157–5166 (2001)
Kawano, T.; Kozutsumi, Y.; Kawasaki, T.; Suzuki, A.: Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system. J. Biol. Chem., 269, 9024–9029 (1994)
Kawano, T.; Koyama, S.; Takematsu, H.; Kozutsumi, Y.; Kawasaki, H.; Kawashima, S.; Kawasaki, T.; Suzuki, A.: Molecular cloning of cytidine mono-phospho-N-acetylneuraminic acid hydroxylase. Regulation of species-and tissue-specific expression of N-glycolylneuraminic acid. J. Biol. Chem., 270, 16458–16463 (1995)
Chou, H.H.; Hayakawa, T.; Diaz, S.; Krings, M.; Indriati, E.; Leakey, M.; Paabo, S.; Satta, Y.; Takahata, N.; Varki, A.: Inactivation of CMP-N-acetyl-neuraminic acid hydroxylase occurred prior to brain expansion during human evolution. Proc. Natl. Acad. Sci. USA, 99, 11736–11741 (2002)
Irie, A.; Suzuki, A.: CMP-N-acetylneuraminic acid hydroxylase is exclusively inactive in humans. Biochem. Biophys. Res. Commun., 248, 330–333 (1998)
Schlenzka, W.; Shaw, L.; Schauer, R.: Catalytic properties of the CMP-N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens: comparison with the mammalian enzyme. Biochim. Biophys. Acta, 1161, 131–138 (1993)
Takematsu, H.; Kawano, T.; Koyama, S.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T.: Reaction mechanism underlying CMP-N-acetylneuraminic acid hydroxylation in mouse liver: formation of a ternary complex of cytochrome b5, CMP-N-acetylneuraminic acid, and a hydroxylation enzyme. J. Biochem., 115, 381–386 (1994)
Schneckenburger, R; Shaw, L.; Schauer, R.: Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver. Glycoconjugate J., 11, 194–203 (1994)
Koyama, S.; Yamaji, T.; Takematsu, H.; Kawano, T.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T.: A naturally occurring 46-amino acid deletion of cytidine monophospho-N-acetylneuraminic acid hydroxylase leads to a change in the intracellular distribution of the protein. Glycoconjugate J., 13, 353–358 (1996)
Malykh, Y.N.; Shaw, L.; Schauer, R.: The role of CMP-N-acetylneuraminic acid hydroxylase in determining the level of N-glycolylneuraminic acid in porcine tissues. Glycoconjugate J., 15, 885–893 (1998)
Malykh, Y.N.; Krisch, B.; Shaw, L.; Warner, T.G.; Sinicrop, D.; Smith, R.; Chang, J.; Schauer, R.: Distribution and localization of CMP-N-acetylneur-aminic acid hydroxylase and N-glycolylneuraminic acid-containing glycoconjugates in porcine lymph node and peripheral blood lymphocytes. Eur. J. Cell Biol., 80, 48–58 (2001)
Gollub, M.; Schauer, R.; Shaw, L.: Cytidine monophosphate-N-acetylneuraminate hydroxylase in the starfish Asterias rubens and other echinoderms. Comp. Biochem. Physiol. B, 120, 605–615 (1998)
Gollub, M.; Shaw, L.: Isolation and characterization of cytidine-5′-monophosphate-N-acetylneuraminate hydroxylase from the starfish Asterias rubens. Comp. Biochem. Physiol. B, 134, 89–101 (2003)
Schlenzka, W.; Shaw, L.; Schneckenburger, P.; Schauer, R.: Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands. Glycobiology, 4, 675–683 (1994)
Shaw, L.; Schneckenburger, P.; Carlsen, J.; Christiansen, K.; Schauer, R.: Mouse liver cytidine-5-monophosphate-N-acetylneuraminic acid hydroxylase. Catalytic function and regulation. Eur. J. Biochem., 206, 269–277 (1992)
Lepers, A.; Shaw, L.; Schneckenburger, P.; Cacan, R.; Verbert, A.; Schauer, R.: A study on the regulation of N-glycoloylneuraminic acid biosynthesis and utilization in rat and mouse liver. Eur. J. Biochem., 193, 715–723 (1990)
Malykh, Y.N.; King, T.P.; Logan, E.; Kelly, D.; Schauer, R.; Shaw, L.: Regulation of N-glycolylneuraminic acid biosynthesis in developing pig small intestine. Biochem. J., 22, 2–29 (2002)
Rights and permissions
Copyright information
© 2006 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
(2006). CMP-N-Acetylneuraminate monooxygenase. In: Class 1 Oxidoreductases XI. Springer Handbook of Enzymes, vol 26. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37708-5_84
Download citation
DOI: https://doi.org/10.1007/3-540-37708-5_84
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-26586-3
Online ISBN: 978-3-540-37708-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)