Purification and characterization of an extradiol dioxygenase which preferentially acts on 4-methylcatechol
- Authors
- Ha, YM; Jung, YH; Kwon, DY; Kim, YC; Kim, Y; Kim, CK; Min, KH
- Issue Date
- Jun-1999
- Publisher
- SPRINGER-VERLAG SINGAPORE PTE LTD
- Keywords
- catechol 2,3-dioxygenase; substrate specificity; N-terminal sequence; kinetic studies; Pseudomonas putida SU10
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.9, no.3, pp 249 - 254
- Pages
- 6
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 9
- Number
- 3
- Start Page
- 249
- End Page
- 254
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16838
- ISSN
- 1017-7825
1738-8872
- Abstract
- A catechol 2,3-dioxygenase (C230) was purified to apparent homogeneity from Pseudomonas putida SU10 through several purification steps consisting of ammonium sulfate precipitation and chromatographies on DEAE 5PW, Superdex S-200, and Resource-Q. Gel filtration indicated a molecular mass under nondenaturing conditions of about 130 kDa. The enzyme has a subunit of 34 kDa as was determined by SDS-PAGE. These results suggest that the native enzyme is composed of four identical subunits. The N-terminal amino acid sequence (30 residues) of the enzyme has been determined and exhibits high identity with other extradiol dioxygenases. The reactivity of this enzyme towards catechol and methyl-substituted catechols is somewhat different from that seen for other catechol 2,3-dioxygenases, with 4-methylcatechol cleaved at a higher rate than catechol or 3-methylcatechol. K-m values of the enzyme for these substrates are between 3.5 and 5.7 M.
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