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Catabolic role of a three-component salicylate oxygenase from Sphingomonas yanoikuyae B1 in polycyclic aromatic hydrocarbon degradation

Authors
 Okyoung Cho  ;  Ki Young Choi  ;  Gerben J. Zylstra  ;  Young-Soo Kim  ;  Seong-Ki Kim  ;  Joon H. Lee  ;  Ho-Yong Sohn  ;  Gi-Seok Kwon  ;  Young Min Kim  ;  Eungbin Kim 
Citation
 Biochemical and Biophysical Research Communications, Vol.327(3) : 656-662, 2005 
Journal Title
 Biochemical and Biophysical Research Communications 
ISSN
 0006-291X 
Issue Date
2005
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 bphA2cA1c, a ferredoxin encoded by the adjacent bphA3, and a ferredoxin reductase encoded by bphA4 located over 25kb 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.
Full Text
http://www.sciencedirect.com/science/article/pii/S0006291X04028591
DOI
10.1016/j.bbrc.2004.12.060
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Ophthalmology (안과학교실) > 1. Journal Papers
Yonsei Authors
이준행(Lee, Joon Haeng)
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/147627
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