Analysis of N- Terminal Amino Acid Sequence of Catechol 2,3-dioxygenase from Aniline Degrading Delftia sp. JK-2

Aniline 분해세균 Delftia sp. JK-2에서 분리된 Catechol 2,3-dioxygenase의 N-말단 아미노산 서열 분석

  • Hwang Seon-Young (Department of Life Science, Soonchunghyang University) ;
  • Kahng Hyung-Yeel (Department of Environmental Education, Sunchon National University) ;
  • Oh Kye-Heon (Department of Life Science, Soonchunghyang University)
  • 황선영 (순천향대학교 자연과학대학 생명과학부) ;
  • 강형일 (순천대학교 환경교육과) ;
  • 오계헌 (순천향대학교 자연과학대학 생명과학부)
  • Published : 2005.03.01


The aim of this work was to investigate the N-terminal amino acid sequence of catechol 2,3-dioxygenase isolated from Delftia sp. JK-2, which could utilize aniline as sole carbon, nitrogen and energy source. Molecular weight of the enzyme was determined to approximately 35 kDa by SDS-PAGE. N-terminal amino acid sequence of C2,3O from strain JK-2 was $^1MGVMRIGHASLKVMDMDAAVRHYENV^{26}$, and exhibited high sequence similarity with that of C2,3O from Pseudomonas sp., Comamonas sp. JS765, Comamonas test-osteroni, or Burkholderia sp. RP007. Approximately 950-bp C2,3O was obtained through PCR using the primers derived from N-terminal amino acid sequence. Analysis of the DNA sequence revealed that the deduced 296 amino acid sequences were determined, and it showed $100\%$ identity with C2,3O from Pseudomonas sp. AW-2 and $97\%$ similarity with Comamonas sp. JS765.


aniline;catechol 2,3-dioxygenase (C2,3O);Delfia sp. JK-2


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