Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate decarboxylase from Bacillus subtilis.

@article{Lupa2008PropertiesOT,
  title={Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate decarboxylase from Bacillus subtilis.},
  author={Boguslaw Lupa and D. Lyon and Lindsey N Shaw and Magdalena Sieprawska-Lupa and Juergen Wiegel},
  journal={Canadian journal of microbiology},
  year={2008},
  volume={54 1},
  pages={
          75-81
        }
}
Bacillus subtilis (ATCC 6051) reversibly decarboxylates vanillate and 4-hydroxybenzoate under both aerobic and anoxic conditions. Thus, we have identified on the basis of gene sequence homology with Sedimentibacter hydroxybenzoicus and Streptomyces sp. strain D7, a putative B. subtilis hydroxybenzoate decarboxylase. The native form of this enzyme is encoded by 3 genes yclBCD (GI Sequence Identification Nos.: 2632649, 2632650, 2632651) that we have renamed during this research as bsdBCD to align… CONTINUE READING
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Purification and characterization of a 4 - hydroxybenzoate decarboxylase from Chlamydophila pneumoniae AR 39

  • X. Zhang, S. Zhou, P. Tao
  • Curr . Microbiol .
  • 2007

Cryptanaerobacter phenolicus

  • R. mur, J. G. Bisaillon
  • 2005

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