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

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

doi:10.1016/j.bbrc.2004.12.060

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

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

Department of Systems Biology

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

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 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.

Original language	English
Pages (from-to)	656-662
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	327
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2004.12.060
Publication status	Published - 2005 Feb 18

Bibliographical note

Funding Information:
This work was supported by a grant from BioGreen 21 Program, Rural Development Administration, Republic of Korea (1000520030096000), and also by a grant from KOSEF through the Advanced Environmental Biotechnology Research Center at POSTECH. G.J.Z. acknowledges the support of NSF through Grants MCB-0078465 and CHE-9810248.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2004.12.060

Cite this

Cho, O., Choi, K. Y., Zylstra, G. J., Kim, Y. S., Kim, S. K., Lee, J. H., Sohn, H. Y., Kwon, G. S., Kim, Y. M., & Kim, E. (2005). Catabolic role of a three-component salicylate oxygenase from Sphingomonas yanoikuyae B1 in polycyclic aromatic hydrocarbon degradation. Biochemical and Biophysical Research Communications, 327(3), 656-662. https://doi.org/10.1016/j.bbrc.2004.12.060

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

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 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.",

author = "Okyoung Cho and Choi, {Ki Young} and Zylstra, {Gerben J.} and Kim, {Young Soo} and Kim, {Seong Ki} and Lee, {Joon H.} and Sohn, {Ho Yong} and Kwon, {Gi Seok} and Kim, {Young Min} and Eungbin Kim",

note = "Funding Information: This work was supported by a grant from BioGreen 21 Program, Rural Development Administration, Republic of Korea (1000520030096000), and also by a grant from KOSEF through the Advanced Environmental Biotechnology Research Center at POSTECH. G.J.Z. acknowledges the support of NSF through Grants MCB-0078465 and CHE-9810248.",

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AU - Kim, Seong Ki

AU - Lee, Joon H.

AU - Sohn, Ho Yong

AU - Kwon, Gi Seok

AU - Kim, Young Min

AU - Kim, Eungbin

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

Abstract

Bibliographical note

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