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PMID:17928721
| Citation |
Masai, E, Yamamoto, Y, Inoue, T, Takamura, K, Hara, H, Kasai, D, Katayama, Y and Fukuda, M (2007) Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6. Biosci. Biotechnol. Biochem. 71:2487-92 |
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| Abstract |
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. |
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| Keywords |
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 |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0050608: vanillin dehydrogenase activity |
ECO:0000315: |
F |
Figure 4B: Shows that ligV-inactivation mutant (DLV) did not have significant growth on vanillin, yet the wild-type strain SYK-6 did have significant growth on vanillin |
complete | ||||
|
enables |
GO:0050608: vanillin dehydrogenase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
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