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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
MeSH
Biodegradation, Environmental ; Catechols/metabolism ; Cloning, Molecular ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Ferredoxin-NADP Reductase/genetics ; Ferredoxin-NADP Reductase/metabolism ; Ferredoxins/genetics ; Ferredoxins/metabolism ; Hydrocarbons, Aromatic/chemistry ; Hydrocarbons, Aromatic/metabolism ; Multigene Family ; Naphthalenes/metabolism ; Oxygenases/genetics ; Oxygenases/metabolism* ; Phenanthrenes/metabolism ; Polycyclic Aromatic Hydrocarbons/chemistry ; Polycyclic Aromatic Hydrocarbons/metabolism* ; Salicylates/metabolism ; Sphingomonas/chemistry ; Sphingomonas/enzymology* ; Sphingomonas/genetics ; Sphingomonas/metabolism ; Time Factors
Keywords
Sphingomonas ; Salicylate oxygenase ; Phenanthrene ; Naphthalene ; Biphenyl ; Xylene
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
Lee, Joon Haeng(이준행)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/147627
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