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

Biosci Biotechnol Biochem. 2007 Oct;71(10):2487-92. doi: 10.1271/bbb.70267. Epub 2007 Oct 7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Benzaldehydes / chemistry
  • Benzaldehydes / metabolism*
  • Catechols / chemistry
  • Catechols / metabolism
  • Escherichia coli / genetics
  • Gene Expression
  • Genes, Bacterial / physiology*
  • Models, Biological
  • Molecular Sequence Data
  • Molecular Structure
  • Molecular Weight
  • Mutation
  • NAD / metabolism
  • Open Reading Frames
  • Restriction Mapping
  • Sequence Homology, Amino Acid
  • Sphingomonas / enzymology*
  • Sphingomonas / genetics
  • Sphingomonas / metabolism
  • Substrate Specificity


  • Benzaldehydes
  • Catechols
  • NAD
  • protocatechualdehyde
  • vanillin
  • benzaldehyde