Functional characterization of a vanillin dehydrogenase in Corynebacterium glutamicum

@article{Ding2015FunctionalCO,
  title={Functional characterization of a vanillin dehydrogenase in Corynebacterium glutamicum},
  author={Wei Ding and Meiru Si and Weipeng Zhang and Yaoling Zhang and Can Chen and Lei Zhang and Zhiqiang Lu and Shaolin Chen and Xihui Shen},
  journal={Scientific Reports},
  year={2015},
  volume={5}
}
Vanillin dehydrogenase (VDH) is a crucial enzyme involved in the degradation of lignin-derived aromatic compounds. Herein, the VDH from Corynebacterium glutamicum was characterized. The relative molecular mass (Mr) determined by SDS-PAGE was ~51kDa, whereas the apparent native Mr values revealed by gel filtration chromatography were 49.5, 92.3, 159.0 and 199.2kDa, indicating the presence of dimeric, trimeric and tetrameric forms. Moreover, the enzyme showed its highest level of activity toward… 
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Global Transcriptomic Analysis of the Response of Corynebacterium glutamicum to Vanillin
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