2,4-Dichlorophenoxyacetate/alpha-ketoglutarate dioxygenases from Burkholderia cepacia 2a and Ralstonia eutropha JMP134

Poh, R.P.-C. and Xia, Xiang-Gen and Bruce, Ian J. and Smith, A.R.W. (2001) 2,4-Dichlorophenoxyacetate/alpha-ketoglutarate dioxygenases from Burkholderia cepacia 2a and Ralstonia eutropha JMP134. Microbios, 105 (410). pp. 43-63. ISSN 0026-2633 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Abstract

2,4-Dichlorophenoxyacetate (2,4-D)/alpha -ketoglutarate (alpha -KG) dioxygenase has been purified to apparent homogeneity from Burkholderia cepacia strain 2a, which utilizes 2.4-D as sole carbon source. The enzyme required ferrous ions, and was a homodimer composed of subunits having an M-r of similar to 32,000. The reaction catalysed consumed one mol each of 2,4-D, alpha -KG and dioxygen, with the production of one mol each of succinate, 2,4-dichlorophenol and glyoxylate. Maximum activity was exhibited at pH 7.8 and 25 degreesC, and reactivity was enhanced by the presence of ascorbate and cysteine. Mn2+, Zn2+, Cu2+ Fe3+ and Co2+ were inhibitory, and chemical modification of the dioxygenase revealed that thiol groups were essential for activity. The enzyme was active towards other substituted phenoxyacetates, but reacted most rapidly with 2,4-D. The apparent Michaelis constants for 2,4-D and alpha -KG were 109 and 8.9 muM, respectively. The properties of this enzyme are compared with those of the 2,4-D/alpha -KG dioxygenase from Ralstonia eutropha JMP134, which exhibits a differing N-terminal amino-acid sequence, and a different temperature 'optimum', pH optimum, substrate specificity and sensitivity to thiol-binding reagents.

Item Type: Article
Uncontrolled keywords: 2,4-D/alpha-ketoglutarate dioxygenase; B. cepacia; R. eutropha
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Suzanne Duffy
Date Deposited: 11 Sep 2009 11:50
Last Modified: 16 Jul 2014 13:40
Resource URI: https://kar.kent.ac.uk/id/eprint/22807 (The current URI for this page, for reference purposes)
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