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

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)
Publication Information
Korean Journal of Microbiology / v.41, no.1, 2005 , pp. 13-17 More about this Journal
Abstract
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.
Keywords
aniline; catechol 2,3-dioxygenase (C2,3O); Delfia sp. JK-2;
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