Catabolic role of a three-component salicylate oxygenase from Sphingomonas yanoikuyae B1 in polycyclic aromatic hydrocarbon degradation
- Authors
- Cho, Okyoung; Choi, Ki Young; Zylstra, Gerben J.; Kim, Young-Soo; Kim, Seong-Ki; Lee, Joon H.; Sohn, Ho-Yong; Kwon, Gi-Seok; Kim, Young Min; Kim, Eungbin
- Issue Date
- Feb-2005
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Sphingomonas; salicylate oxygenase; phenanthrene; naphthalene; biphenyl; xylene
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.327, no.3, pp 656 - 662
- Pages
- 7
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 327
- Number
- 3
- Start Page
- 656
- End Page
- 662
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24661
- DOI
- 10.1016/j.bbrc.2004.12.060
- ISSN
- 0006-291X
1090-2104
- Abstract
- Sphingomonas yanoikuyae B1 possesses several different multicomponent oxygenases involved in metabolizing aromatic compounds. Six different pairs of genes encoding large and small subunits of oxygenase iron-sulfur protein components have previously been identified in a gene cluster involved in the degradation of both monocyclic and polycyclic aromatic hydrocarbons. Insertional inactivation of one of the oxygenase large subunit genes, bphA1c, results in a mutant strain unable to grow on naphthalene, phenanthrene, or salicylate. The knockout mutant accumulates salicylate from naphthalene and 1-hydroxy-2-naphthoic acid from phenanthrene indicating the loss of salicylate oxygenase activity. Complementation experiments verify that the salicylate oxygenase in S. yanoikuyae B1 is a three-component enzyme consisting of an oxygenase encoded by bph A2cA1c, a ferredoxin encoded by the adjacent bphA3, and a ferredoxin reductase encoded by bphA4 located over 25 kb away. Expression of bphA3-bphA2c-bphA1c genes in Escherichia coli demonstrated the ability of salicylate oxygenase to convert salicylate to catechol and 3-, 4-, and 5-methylsalicylate to methylcatechols. (C) 2004 Elsevier Inc. All rights reserved.
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Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
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