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Masai, E. et al.

Eiji Masai, Yuko Yamamoto, Tomohiko Inoue, Kazuhiro Takamura, Hirofumi Hara, Daisuke Kasai, Yoshihiro Katayama, Masao Fukuda,

Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6.

The vanillin dehydrogenase gene (ligV), which conferred the ability to transform vanillin into vanillate on Escherichia coli, was isolated from Sphingomonas paucimobilis SYK-6. The ligV gene consists of a 1,440-bp open reading frame encoding a polypeptide with a molecular mass of 50,301 Da. The deduced amino acid sequence of ligV showed about 50% identity with the known vanillin dehydrogenases of Pseudomonas vanillin degraders. The gene product of ligV (LigV) produced in E. coli preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde, but the activity toward syringaldehyde was less than 5% of that toward vanillin. Insertional inactivation of ligV in SYK-6 indicated that ligV is essential for normal growth on vanillin. On the other hand, growth on syringaldehyde was only slightly affected by ligV disruption, indicating the presence of a syringaldehyde dehydrogenase gene or genes in SYK-6.[1]

References

Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6. Masai, E., Yamamoto, Y., Inoue, T., Takamura, K., Hara, H., Kasai, D., Katayama, Y., Fukuda, M. Biosci. Biotechnol. Biochem. (2007) [Pubmed]

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