A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp. GMD509

@article{Park2007ANE,
  title={A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp. GMD509},
  author={Seon Jeong Park and Jun-Tae Kim and Sung Gyun Kang and Jung-Hee Woo and Jung-Hyun Lee and Hyoung-Tae Choi and Sang-Jin Kim},
  journal={Applied Microbiology and Biotechnology},
  year={2007},
  volume={77},
  pages={107-115}
}
Vibrio sp. GMD509, a marine bacterium isolated from eggs of the sea hare, exhibited lipolytic activity on tributyrin (TBN) plate, and the gene representing lipolytic activity was cloned. As a result, an open reading frame (ORF) consisting of 1,017 bp (338 aa) was found, and the deduced amino acid sequence of the ORF showed low similarity (<20%) to α/β hydrolases such as dienelactone hydrolases and esterase/lipase with G–X1–S–X2–G sequence conserved. Phylogenetic analysis suggested that the… CONTINUE READING
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