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Gene Review:

xylW - xylW

Pseudomonas putida

Gillooly, D.J. et al., Shaw, J.P. et al., Farrell, R.L. et al., Williams, P.A. et al., Inoue, J. et al., et al.

Williams, Shaw, Pitt, Vrecl,

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Disease relevance of xylW

The nucleotide sequence of the structural gene for benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO of Pseudomonas putida has been determined [1].
Molecular characterization of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II of Acinetobacter calcoaceticus [2].

High impact information on xylW

Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family [1].
Benzyl alcohol dehydrogenase, while sharing 31% identical residues with horse liver alcohol dehydrogenase, contains several amino acid substitutions near the active site, some of which may be responsible for the substrate specificity of benzyl alcohol dehydrogenase, which oxidizes exclusively aromatic substrates [1].
The kcat/K(m) value of the His47Gln mutant for benzyl alcohol was 125-fold lower than that of wild-type BADH, while the kcat/K(m) value of the His47Gln/Val51His double mutant was 12-fold higher than that of the His47Gln mutant [3].
However, this residue was found to be replaced in benzyl alcohol dehydrogenase from A. calcoaceticus by an isoleucine, and the introduction of a histidine residue in this position did not alter the kinetic coefficients, pH optimum or substrate specificity of the enzyme [2].
Benzyl alcohol dehydrogenase has a subunit Mr of 38923 consisting of 370 amino acids, it stereospecifically transfers the proR hydride of NADH, and it is a member of the family of zinc-dependent long-chain alcohol dehydrogenases [2].

Chemical compound and disease context of xylW

Sequence analysis of PCR products amplified using xylB (the gene encoding benzyl alcohol dehydrogenase) primers revealed that isolates 7/167 and 8/46 were 100% and 92% homologous, respectively, to the xylB gene of the meta-cleavage toluene degradative pathway encoded by the TOL plasmid (pWWO) of Pseudomonas putida mt-2 [4].

Associations of xylW with chemical compounds

The results of continuous-culture experiments showed that the activity of the upper-pathway toluene monooxygenase decreased but that the activity of benzyl alcohol dehydrogenase was not affected under iron-limited conditions [5].
Benzyl alcohol dehydrogenase catalyses the oxidation of benzyl alcohol to benzaldehyde with the concomitant reduction of NAD+; the reaction is reversible [6].

Other interactions of xylW

These were designated xylUW: xylU encoded a protein of 131 amino acid residues (M(r) 14,244) which bore no relationship with any protein in the databases, and xylW encoded a protein of 348 residues (M(r) 36,992) which was strongly homologous to other long-chain Zn-containing alcohol dehydrogenases [7].

References

Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family. Shaw, J.P., Rekik, M., Schwager, F., Harayama, S. J. Biol. Chem. (1993) [Pubmed]
Molecular characterization of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II of Acinetobacter calcoaceticus. Gillooly, D.J., Robertson, A.G., Fewson, C.A. Biochem. J. (1998) [Pubmed]
Proton transfer in benzyl alcohol dehydrogenase during catalysis: alternate proton-relay routes. Inoue, J., Tomioka, N., Itai, A., Harayama, S. Biochemistry (1998) [Pubmed]
Toluene-degrading Antarctic Pseudomonas strains from fuel-contaminated soil. Farrell, R.L., Rhodes, P.L., Aislabie, J. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
Effects of iron limitation on the degradation of toluene by Pseudomonas strains carrying the tol (pWWO) plasmid. Dinkla, I.J., Gabor, E.M., Janssen, D.B. Appl. Environ. Microbiol. (2001) [Pubmed]
Purification and characterisation of TOL plasmid-encoded benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase of Pseudomonas putida. Shaw, J.P., Harayama, S. Eur. J. Biochem. (1990) [Pubmed]
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]

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