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

xylC  -  xylC

Pseudomonas putida

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 xylC

  • The predicted protein sequence exhibits significant homology to eukaryotic aldehyde dehydrogenases (ADHs) and to the products of two other Pseudomonas catabolic genes, i.e. xylC and alkH [1].
  • This confirms the interpretation of the N-terminal sequence comparisons and also indicates that benzaldehyde dehydrogenase I from Acinetobacter may be related to the other two benzaldehyde dehydrogenases [2].

High impact information on xylC


Biological context of xylC

  • Between the promoter of the operon and xylC, there is a 1.7-kilobase-long space of DNA in which no gene function was identified [5].
  • Assays of cell-free extracts of 7/167 and 8/46 demonstrated activity of catechol 2,3-dioxygenase, benzyl alcohol dehydrogenase, and benzaldehyde dehydrogenase, indicating that the isolates use the meta-cleavage pathway enzymes of toluene degradation typical of TOL type plasmids [6].

Associations of xylC with chemical compounds


Other interactions of xylC

  • In contrast, most of the DNA between xylC and xylN consists of coding sequences [5].


  1. DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of Pseudomonas putida: implications for the evolution of aromatic catabolism. Horn, J.M., Harayama, S., Timmis, K.N. Mol. Microbiol. (1991) [Pubmed]
  2. Comparison of benzyl alcohol dehydrogenases and benzaldehyde dehydrogenases from the benzyl alcohol and mandelate pathways in Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid compositions and immunological cross-reactions. Chalmers, R.M., Keen, J.N., Fewson, C.A. Biochem. J. (1991) [Pubmed]
  3. Substrate-specificity of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase encoded by TOL plasmid pWW0. Metabolic and mechanistic implications. Shaw, J.P., Schwager, F., Harayama, S. Biochem. J. (1992) [Pubmed]
  4. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. Inoue, J., Shaw, J.P., Rekik, M., Harayama, S. J. Bacteriol. (1995) [Pubmed]
  5. Characterization of five genes in the upper-pathway operon of TOL plasmid pWW0 from Pseudomonas putida and identification of the gene products. Harayama, S., Rekik, M., Wubbolts, M., Rose, K., Leppik, R.A., Timmis, K.N. J. Bacteriol. (1989) [Pubmed]
  6. Toluene-degrading Antarctic Pseudomonas strains from fuel-contaminated soil. Farrell, R.L., Rhodes, P.L., Aislabie, J. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  7. XylUW, two genes at the start of the upper pathway operon of TOL plasmid pWW0, appear to play no essential part in determining its catabolic phenotype. Williams, P.A., Shaw, L.M., Pitt, C.W., Vrecl, M. Microbiology (Reading, Engl.) (1997) [Pubmed]
WikiGenes - Universities