The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

yahJ  -  putative metallo-dependent hydrolase...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0322, JW0316
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of yahJ


High impact information on yahJ


Chemical compound and disease context of yahJ


Biological context of yahJ

  • Studies are in progress to define the location of this nucleotide, which will be aided greatly by our recent clarification of the complete amino acid sequence of T2-deoxycytidylate deaminase [16].
  • The Arabidopsis thaliana open reading frame At4g20960 predicts a protein whose N-terminal part is similar to the eubacterial 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate deaminase domain [17].
  • The second atom of zinc is proposed to be located in a region of T4-dCMP deaminase that resembles a zinc finger [3].
  • The crystallographic structure of the T state of Phe174-Ala deaminase, determined at 2.02 A resolution, shows no density for the segment 162-181, which is part of the active-site lid (PDB 1JT9) [18].
  • On the basis of these cumulative findings, it has been possible to construct a mechanistic scheme for the deaminase reaction involving a single catalytic site which is able to catalyze the addition or removal of either NH3 or H2O [19].

Anatomical context of yahJ


Associations of yahJ with chemical compounds

  • However, on changing the arginine (Arg) at residue 115 of the T4-deaminase to either a glutamate (R115E) or a glutamine (R115Q), the resulting mutant enzymes were active in the absence of dCTP, with each mutant possessing a turnover number or k(cat) that is about 15% that of the wild-type deaminase [22].
  • The deaminase is induced over 100-fold by GlcNAc and its level is about 0.3-0.5% of the proteins in crude extract [11].
  • The deaminase has been crystallized through the use of polyethylene glycol; a scanning electron micrograph is presented [23].
  • Another feature emphasizing the difference between the WT and mutant deaminases was observed on their denaturation-renaturation in EDTA, which revealed the mutants to be restored to 50% of their original activities with the WT deaminase only marginally restored [22].
  • The NH2-terminal sequence (35 residues) determined from the purified deaminase was identical to the sequence of the deduced protein [11].

Other interactions of yahJ


Analytical, diagnostic and therapeutic context of yahJ


  1. Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria. Delfau, M.H., Picat, C., de Rooij, F.W., Hamer, K., Bogard, M., Wilson, J.H., Deybach, J.C., Nordmann, Y., Grandchamp, B. J. Clin. Invest. (1990) [Pubmed]
  2. Activation induced deaminase: the importance of being specific. Smith, H.C., Bottaro, A., Sowden, M.P., Wedekind, J.E. Trends Genet. (2004) [Pubmed]
  3. T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit. Moore, J.T., Silversmith, R.E., Maley, G.F., Maley, F. J. Biol. Chem. (1993) [Pubmed]
  4. Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different. Seffernick, J.L., de Souza, M.L., Sadowsky, M.J., Wackett, L.P. J. Bacteriol. (2001) [Pubmed]
  5. Proteus mirabilis amino acid deaminase: cloning, nucleotide sequence, and characterization of aad. Massad, G., Zhao, H., Mobley, H.L. J. Bacteriol. (1995) [Pubmed]
  6. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Bransteitter, R., Pham, P., Scharff, M.D., Goodman, M.F. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. The transcription elongation complex directs activation-induced cytidine deaminase-mediated DNA deamination. Besmer, E., Market, E., Papavasiliou, F.N. Mol. Cell. Biol. (2006) [Pubmed]
  8. Mice deficient in APOBEC2 and APOBEC3. Mikl, M.C., Watt, I.N., Lu, M., Reik, W., Davies, S.L., Neuberger, M.S., Rada, C. Mol. Cell. Biol. (2005) [Pubmed]
  9. Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA. Laliberté, J., Momparler, R.L. Cancer Res. (1994) [Pubmed]
  10. 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]
  11. Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans. Natarajan, K., Datta, A. J. Biol. Chem. (1993) [Pubmed]
  12. Tyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase. Montero-Morán, G.M., Horjales, E., Calcagno, M.L., Altamirano, M.M. Biochemistry (1998) [Pubmed]
  13. Isolation, sequence, and expression in Escherichia coli of the Pseudomonas sp. strain ACP gene encoding 1-aminocyclopropane-1-carboxylate deaminase. Sheehy, R.E., Honma, M., Yamada, M., Sasaki, T., Martineau, B., Hiatt, W.R. J. Bacteriol. (1991) [Pubmed]
  14. Recombinant f1 phage-mediated transfection of mammalian cells using lipopolyamine technique. Yokoyama-Kobayashi, M., Kato, S. Anal. Biochem. (1994) [Pubmed]
  15. Enzymatic treatment to eliminate the extracellular ATP for improving the detectability of bacterial intracellular ATP. Sakakibara, T., Murakami, S., Hattori, N., Nakajima, M., Imai, K. Anal. Biochem. (1997) [Pubmed]
  16. Studies on identifying the allosteric binding sites of deoxycytidylate deaminase. Maley, F., Maley, G.F. J. Biol. Chem. (1982) [Pubmed]
  17. Evolution of vitamin B2 biosynthesis: structural and functional similarity between pyrimidine deaminases of eubacterial and plant origin. Fischer, M., Römisch, W., Saller, S., Illarionov, B., Richter, G., Rohdich, F., Eisenreich, W., Bacher, A. J. Biol. Chem. (2004) [Pubmed]
  18. On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. Bustos-Jaimes, I., Sosa-Peinado, A., Rudiño-Piñera, E., Horjales, E., Calcagno, M.L. J. Mol. Biol. (2002) [Pubmed]
  19. Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase. Warren, M.J., Jordan, P.M. Biochemistry (1988) [Pubmed]
  20. Overcoming inclusion body formation in a high-level expression system. Moore, J.T., Uppal, A., Maley, F., Maley, G.F. Protein Expr. Purif. (1993) [Pubmed]
  21. Statistical modelling and phylogenetic analysis of a deaminase domain. Mian, I.S., Moser, M.J., Holley, W.R., Chatterjee, A. J. Comput. Biol. (1998) [Pubmed]
  22. A T4-phage deoxycytidylate deaminase mutant that no longer requires deoxycytidine 5'-triphosphate for activation. Keefe, R.G., Maley, G.F., Saxl, R.L., Maley, F. J. Biol. Chem. (2000) [Pubmed]
  23. Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase. Maley, G.F., Guarino, D.U., Maley, F. J. Biol. Chem. (1983) [Pubmed]
  24. Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. Thomas, S.D., Jordan, P.M. Nucleic Acids Res. (1986) [Pubmed]
  25. Alternative route for biosynthesis of amino sugars in Escherichia coli K-12 mutants by means of a catabolic isomerase. Vogler, A.P., Trentmann, S., Lengeler, J.W. J. Bacteriol. (1989) [Pubmed]
  26. Crystallization and preliminary X-ray diffraction studies of blasticidin S deaminase from Aspergillus terreus. Nakasako, M., Kimura, M., Yamaguchi, I. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  27. Toxicity and mutagenicity studies of DN-50000((R)) and RP-1((R)) enzymes. Burdock, G.A., Flamm, W.G., Carabin, I.G. Food Chem. Toxicol. (2000) [Pubmed]
  28. The biosynthesis of uroporphyrinogen III: mechanism of action of porphobilinogen deaminase. Jordan, P.M. Ciba Found. Symp. (1994) [Pubmed]
WikiGenes - Universities