| Title | Cloning and Sequence Analysis of the hpaD Gene Responsible for Homoprotocatechuate 2,3-Dioxygenase from Pseudomonas sp. DJ-12 |
|---|---|
| Author | Sang-Mahn Lee, Jong-Chan Chae 1 , Youngsoo Kim 2 , and Chi-Kyung Kim 1 * |
| Address | Department of Life Science, Chongju University, Cheongju 360-764, Korea; 1 Department of Microbiology and Biotechnology, and 2 Department of Pharmacy, |
| Bibliography | Journal of Microbiology, 39(4),334-337, 2001, |
| DOI | |
| Key Words | hpaD, homoprotocatechuate 2,3-dioxygenase, nucleotide sequence, homology |
| Abstract | The degradative pathway of homoprotocatechuate (HPC) is the bacterial route whereby 3,4-dihydroxyphenylacetic acid is catabolized to pyruvate and succinate by a series of sequential reactions. The HPC is catalized by homoprotocatechuate 2,3-dioxygenase (HPC-2,3O) to form 5-carboxymethyl-2-hydroxy-muco semialdehyde. In this study, the hpaD gene encoding HPC-2,3O was cloned from the chromosomal DNA of Pseudomonas sp. DJ-12 and its nucleotide sequence was analyzed. The open reding frame of hpaD gene was found to be composed of 864 nucleotide pairs and to encode a polypeptide with 287 amino acid residues. The deduced amino acid sequence of the HPC-2,3O from Pseudomonas sp. DJ-12 exhibited 60~64% homology with those of the corresponding enzymes from E. coli, Salmonella enterica, and Klebsiella pneumoniae. |
| Download PDF | 394-15.pdf |