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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


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Disease relevance of Deamination


High impact information on Deamination


Chemical compound and disease context of Deamination


Biological context of Deamination


Anatomical context of Deamination

  • Our results may explain why SMUG1 cannot compensate the UNG2 deficiency in human B cells, and are fully consistent with the DNA deamination model that requires active nuclear UNG2 [21].
  • The electrophoretic mobility and Michaelis constants for the deamination of histimine and putrescine were identical for histaminases from human placenta and from medullary thyroid carcinoma [22].
  • G.T mispairs, the sole mismatch type that can arise in "resting" mammalian DNA (through spontaneous hydrolytic deamination of 5-methylcytosine), are corrected in vivo with high efficiency and mostly to a G.C. We identified a protein factor, present in HeLa cell extracts, that binds selectively to DNA substrates containing this mismatch [23].
  • 2. Quantitative analysis of catabolites in incubated hemolysates confirmed that AMP degradation preferentially occurred via deamination to IMP with subsequent dephosphorylation by another erythrocyte nucleotidase isozyme, deoxyribonucleotidase [24].
  • In the liver and cirrhotic liver mitochondria, glutamate was oxidized via the routes of transamination and deamination [25].

Associations of Deamination with chemical compounds


Gene context of Deamination

  • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites [30].
  • Indexes of deamination, sulfoconjugation, and O-methylation, with the exception of a reduced deamination of dopamine and the activities of COMT, MAO-B, and TL-PST were not different in the two groups [31].
  • This unique genetic system further enabled us to show that expression of APOBEC3G or its homolog APOBEC3F was able to inhibit the mobility of the retrotransposon Ty1 by a mechanism that involves the deamination of cDNA cytosines [32].
  • RNA editing of specific residues by adenosine deamination is a nuclear process catalyzed by adenosine deaminases acting on RNA (ADAR) [33].
  • These proteins have two putative deaminase domains, and it is unclear whether one or both catalyze deamination, unlike their homologs, AID and APOBEC1, which are well characterized single domain deaminases [34].

Analytical, diagnostic and therapeutic context of Deamination


  1. C-terminal deletion of AID uncouples class switch recombination from somatic hypermutation and gene conversion. Barreto, V., Reina-San-Martin, B., Ramiro, A.R., McBride, K.M., Nussenzweig, M.C. Mol. Cell (2003) [Pubmed]
  2. 5-Methylcytosine is not a mutation hot spot in nondividing Escherichia coli. Lieb, M., Rehmat, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  3. HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. Santa-Marta, M., da Silva, F.A., Fonseca, A.M., Goncalves, J. J. Biol. Chem. (2005) [Pubmed]
  4. AMP deamination delays muscle acidification during heavy exercise and hypoxia. Korzeniewski, B. J. Biol. Chem. (2006) [Pubmed]
  5. Involvement of semicarbazide-sensitive amine oxidase-mediated deamination in lipopolysaccharide-induced pulmonary inflammation. Yu, P.H., Lu, L.X., Fan, H., Kazachkov, M., Jiang, Z.J., Jalkanen, S., Stolen, C. Am. J. Pathol. (2006) [Pubmed]
  6. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Barrett, T.E., Savva, R., Panayotou, G., Barlow, T., Brown, T., Jiricny, J., Pearl, L.H. Cell (1998) [Pubmed]
  7. Different base/base mispairs are corrected with different efficiencies and specificities in monkey kidney cells. Brown, T.C., Jiricny, J. Cell (1988) [Pubmed]
  8. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Sheehy, A.M., Gaddis, N.C., Malim, M.H. Nat. Med. (2003) [Pubmed]
  9. Uracil-DNA glycosylase acts by substrate autocatalysis. Dinner, A.R., Blackburn, G.M., Karplus, M. Nature (2001) [Pubmed]
  10. Point mutation in an AMPA receptor gene rescues lethality in mice deficient in the RNA-editing enzyme ADAR2. Higuchi, M., Maas, S., Single, F.N., Hartner, J., Rozov, A., Burnashev, N., Feldmeyer, D., Sprengel, R., Seeburg, P.H. Nature (2000) [Pubmed]
  11. In vitro deamination of cytosine to uracil in single-stranded DNA by apolipoprotein B editing complex catalytic subunit 1 (APOBEC1). Petersen-Mahrt, S.K., Neuberger, M.S. J. Biol. Chem. (2003) [Pubmed]
  12. Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3' endonuclease, from Escherichia coli. Yao, M., Hatahet, Z., Melamede, R.J., Kow, Y.W. J. Biol. Chem. (1994) [Pubmed]
  13. Oxidative deamination of epsilon-aminolysine residues and formation of Schiff base cross-linkages in cell envelopes of Escherichia coli. Mirelman, D., Siegel, R.C. J. Biol. Chem. (1979) [Pubmed]
  14. Involvement of semicarbazide-sensitive amine oxidase-mediated deamination in atherogenesis in KKAy diabetic mice fed with high cholesterol diet. Yu, P.H., Wang, M., Deng, Y.L., Fan, H., Shira-Bock, L. Diabetologia (2002) [Pubmed]
  15. Influence of pyruvate on ammonia metabolism by renal cortical mitochondria. Tannen, R.L., Kunin, A.S. Kidney Int. (1982) [Pubmed]
  16. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Slupphaug, G., Mol, C.D., Kavli, B., Arvai, A.S., Krokan, H.E., Tainer, J.A. Nature (1996) [Pubmed]
  17. A mammalian RNA editing enzyme. Melcher, T., Maas, S., Herb, A., Sprengel, R., Seeburg, P.H., Higuchi, M. Nature (1996) [Pubmed]
  18. MRE11/RAD50 cleaves DNA in the AID/UNG-dependent pathway of immunoglobulin gene diversification. Larson, E.D., Cummings, W.J., Bednarski, D.W., Maizels, N. Mol. Cell (2005) [Pubmed]
  19. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. Hardeland, U., Steinacher, R., Jiricny, J., Schär, P. EMBO J. (2002) [Pubmed]
  20. Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase. Kavli, B., Slupphaug, G., Mol, C.D., Arvai, A.S., Peterson, S.B., Tainer, J.A., Krokan, H.E. EMBO J. (1996) [Pubmed]
  21. B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil. Kavli, B., Andersen, S., Otterlei, M., Liabakk, N.B., Imai, K., Fischer, A., Durandy, A., Krokan, H.E., Slupphaug, G. J. Exp. Med. (2005) [Pubmed]
  22. Histaminase (diamine oxidase) activity in human tumors: an expression of a mature genome. Baylin, S.B. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  23. A human 200-kDa protein binds selectively to DNA fragments containing G.T mismatches. Jiricny, J., Hughes, M., Corman, N., Rudkin, B.B. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  24. Mechanisms of adenosine 5'-monophosphate catabolism in human erythrocytes. Paglia, D.E., Valentine, W.N., Nakatani, M., Brockway, R.A. Blood (1986) [Pubmed]
  25. Glutaminase and glutamine synthetase activities in human cirrhotic liver and hepatocellular carcinoma. Matsuno, T., Goto, I. Cancer Res. (1992) [Pubmed]
  26. A specific mismatch repair event protects mammalian cells from loss of 5-methylcytosine. Brown, T.C., Jiricny, J. Cell (1987) [Pubmed]
  27. Editing of glutamate receptor subunit B pre-mRNA in vitro by site-specific deamination of adenosine. Yang, J.H., Sklar, P., Axel, R., Maniatis, T. Nature (1995) [Pubmed]
  28. The vsr gene product of E. coli K-12 is a strand- and sequence-specific DNA mismatch endonuclease. Hennecke, F., Kolmar, H., Bründl, K., Fritz, H.J. Nature (1991) [Pubmed]
  29. A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Gallinari, P., Jiricny, J. Nature (1996) [Pubmed]
  30. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Hendrich, B., Hardeland, U., Ng, H.H., Jiricny, J., Bird, A. Nature (1999) [Pubmed]
  31. Catecholamine metabolic pathways and exercise training. Plasma and urine catecholamines, metabolic enzymes, and chromogranin-A. Rogers, P.J., Tyce, G.M., Weinshilboum, R.M., O'Connor, D.T., Bailey, K.R., Bove, A.A. Circulation (1991) [Pubmed]
  32. APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast. Schumacher, A.J., Nissley, D.V., Harris, R.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  33. CRM1 mediates the export of ADAR1 through a nuclear export signal within the Z-DNA binding domain. Poulsen, H., Nilsson, J., Damgaard, C.K., Egebjerg, J., Kjems, J. Mol. Cell. Biol. (2001) [Pubmed]
  34. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. Haché, G., Liddament, M.T., Harris, R.S. J. Biol. Chem. (2005) [Pubmed]
  35. The mechanism of action of phenylalanine ammonia-lyase: the role of prosthetic dehydroalanine. Schuster, B., Rétey, J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  36. The peroxisome proliferator-activated receptor alpha regulates amino acid metabolism. Kersten, S., Mandard, S., Escher, P., Gonzalez, F.J., Tafuri, S., Desvergne, B., Wahli, W. FASEB J. (2001) [Pubmed]
  37. Amyloid-specific heparan sulfate from human liver and spleen. Lindahl, B., Lindahl, U. J. Biol. Chem. (1997) [Pubmed]
  38. Structural analysis of the light subunit of the Entamoeba histolytica galactose-specific adherence lectin. McCoy, J.J., Mann, B.J., Vedvick, T.S., Pak, Y., Heimark, D.B., Petri, W.A. J. Biol. Chem. (1993) [Pubmed]
  39. Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution. Ko, T.P., Lin, J.J., Hu, C.Y., Hsu, Y.H., Wang, A.H., Liaw, S.H. J. Biol. Chem. (2003) [Pubmed]
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