Structure of Catechol 2,3-Dioxygenase Gene fromAlcaligenes eutrophus335
| Autor: | Chi-Kyung Kim, Joo Young Ha, Kyung Rak Min, Bo-Seong Kang, Jong-Chul Lim, Jeongrai Lee, Youngsoo Kim |
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| Rok vydání: | 1998 |
| Předmět: |
DNA
Bacterial Base pair Molecular Sequence Data Biophysics Sequence alignment Biology Biochemistry Catechol 2 3-Dioxygenase Dioxygenases Open Reading Frames chemistry.chemical_compound Dioxygenase Alcaligenes Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence chemistry.chemical_classification Base Sequence Nucleic acid sequence Cell Biology Amino acid Open reading frame chemistry Oxygenases bacteria Sequence Alignment DNA |
| Zdroj: | Biochemical and Biophysical Research Communications. 245:791-796 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1998.8511 |
| Popis: | Catechol 2,3-dioxygenase (C23O), one of extradiol-type dioxygenases cleaving aromatic C-C bond at meta position of dihydroxylated aromatic substrates, catalyzes the conversion of catechol to 2-hydroxymuconic semialdehyde. As our ongoing study to characterize biochemical and genetic properties of the extradiol-type dioxygenases at molecular level, a C23O gene encoded in chromosomal DNA of Alcaligenes eutrophus 335, a strain degrading phenol and p-cresol, was cloned. The C23O gene was localized in an 1.4-kb PstI fragment from A. eutrophus 335, and was expressed in E. coli HB101. The C23O exhibited the highest aromatic ring-fission activity to catechol as a substrate, and its relative activity to other dihydroxylated aromatic substrates was in order of catechol >> 4-methylcatechol > 3-methylcatechol, protocatechuate, 4-chlorocatechol > 3,4-dihydroxy-phenylacetate > 2,3-dihydroxybiphenyl. Nucleotide sequence of the 1.4-kb fragment has revealed that an open reading frame (ORF) corresponding to the C23O gene was composed of 930 base pairs. A putative ribosome-binding sequence of AGGAG was found at about 10 nucleotides upstream the ORF which can encode a polypeptide of molecular weight 34 kDa consisting of 309 amino acid residues. The deduced amino acid sequence of C23O from A. eutrophus 335 exhibited the highest 59% identity with those of corresponding enzymes from Pseudomonas sp. CF600 (p VI150), P. putida HS1 (pDK1), and P. putida PpG7 (NAH7). An alignment of amino acid sequences of extradiol-type dioxygenases including C23O from A. eutrophus 335 has revealed that catalytically and structurally important amino acid residues of the enzymes were conserved during evolution. |
| Databáze: | OpenAIRE |
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