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Gene Review

Cmah  -  cytidine monophospho-N-acetylneuraminic...

Mus musculus

Synonyms: CMP-N-acetylneuraminate monooxygenase, CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, CMP-NeuAc hydroxylase, Cytidine monophosphate-N-acetylneuraminic acid hydroxylase
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Disease relevance of Cmah


High impact information on Cmah


Anatomical context of Cmah

  • Compared to the parental cell line, the new strain (CHO-AsUH2), which was transfected with a 199-bp antisense fragment derived from the mouse CMP-Neu5Ac hydroxylase cDNA, showed an 80% reduction in hydroxylase activity [7].

Associations of Cmah with chemical compounds

  • In mouse germinal center B cells, the expression of the GL7 epitope was upregulated due to the in situ repression of CMP-Neu5Ac hydroxylase (Cmah), the enzyme responsible for Sia modification of Neu5Ac to Neu5Gc [3].
  • An antibody against cytochrome b5 markedly reduced the CMP-NeuAc hydroxylase activity when added to incubation mixture containing either NADH or NADPH as an electron donor [8].

Other interactions of Cmah

  • In summary, mTf glycans differed from those of other analyzed mammalian transferrins by the presence of Neu5Gc and by a Neu5Gc(alpha 2-6)GlcNAc linkage in trisialylated biantennary structures, reflecting in mouse liver, a high activity of CMP-Neu5Ac hydroxylase and (alpha 2-6)GlcNAc sialyltransferase [9].

Analytical, diagnostic and therapeutic context of Cmah

  • Immunization of a rabbit with enriched and purified hydroxylase led to an antiserum that inhibited CMP-Neu5Ac hydroxylase activity and reacted with the purified 65 kDa protein on a Western blot after SDS-PAGE [5].
  • In order to shed light on the structural basis for these differences, the primary structure of CMP-Neu5Ac hydroxylase from A. rubens has been determined by PCR and cDNA-cloning techniques, using initial sequence information from the mouse enzyme [2].
  • The activity of CMP-N-acetylneuraminic acid hydroxylase, that converts CMP-N-acetylneuraminic acid (CMP-NeuAc) to CPM-N-glycolylneuraminic acid (CMP-NeuGc), in mouse liver was determined by a newly developed HPLC method using non-radioactive CMP-NeuAc as a substrate [8].


  1. Ganglioside biosynthetic gene expression in experimental mouse brain tumors. Ecsedy, J.A., Manfredi, M.G., Yohe, H.C., Seyfried, T.N. Cancer Res. (1997) [Pubmed]
  2. Cloning and expression of a membrane-bound CMP-N-acetylneuraminic acid hydroxylase from the starfish Asterias rubens. Martensen, I., Schauer, R., Shaw, L. Eur. J. Biochem. (2001) [Pubmed]
  3. Germinal Center Marker GL7 Probes Activation-Dependent Repression of N-Glycolylneuraminic Acid, a Sialic Acid Species Involved in the Negative Modulation of B-Cell Activation. Naito, Y., Takematsu, H., Koyama, S., Miyake, S., Yamamoto, H., Fujinawa, R., Sugai, M., Okuno, Y., Tsujimoto, G., Yamaji, T., Hashimoto, Y., Itohara, S., Kawasaki, T., Suzuki, A., Kozutsumi, Y. Mol. Cell. Biol. (2007) [Pubmed]
  4. Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N-acetylneuraminic acid hydroxylation system. Kawano, T., Kozutsumi, Y., Kawasaki, T., Suzuki, A. J. Biol. Chem. (1994) [Pubmed]
  5. Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands. Schlenzka, W., Shaw, L., Schneckenburger, P., Schauer, R. Glycobiology (1994) [Pubmed]
  6. Mouse liver cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. Catalytic function and regulation. Shaw, L., Schneckenburger, P., Carlsen, J., Christiansen, K., Schauer, R. Eur. J. Biochem. (1992) [Pubmed]
  7. Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy. Chenu, S., Grégoire, A., Malykh, Y., Visvikis, A., Monaco, L., Shaw, L., Schauer, R., Marc, A., Goergen, J.L. Biochim. Biophys. Acta (2003) [Pubmed]
  8. Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol. Kozutsumi, Y., Kawano, T., Yamakawa, T., Suzuki, A. J. Biochem. (1990) [Pubmed]
  9. Structural analysis of trisialylated biantennary glycans isolated from mouse serum transferrin. Characterization of the sequence Neu5Gc(alpha 2-3)Gal(beta 1-3)[Neu5Gc(alpha 2-6)]GlcNAc(beta 1-2)Man. Coddeville, B., Regoeczi, E., Strecker, G., Plancke, Y., Spik, G. Biochim. Biophys. Acta (2000) [Pubmed]
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