Molecular characterisation of a Rhodococcus ohp operon

Justin A.C. Powell; John A.C. Archer

doi:10.1023/A:1001784702230

Molecular characterisation of a Rhodococcus ohp operon

Justin A.C. Powell, John A.C. Archer^*

^*Corresponding author for this work

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

16 Scopus citations

Abstract

The ohp operon of Rhodococcus strain V49 consists of five genes, ohpR, ohpA, ohpB, ohpC and ohpD which encode putative regulator and transport proteins and confirmed monooxygenase, hydroxymuconic semialdehyde hydrolase and catechol 2,3-dioxygenase enzymes, respectively. These enzymes catalyse the conversion of 3-(2-hydroxyphenyl) propionic acid to the corresponding linear product via a meta-cleavage pathway. Confirmation that the ohp gene cluster formed an operon was provided by gene disruption during which expression of Bacillus levansucrase was confirmed in Rhodococcus. Following biochemical assays of cell-free extracts from recombinant Escherichia coli expressing ohpB (monooxygenase), ohpC (hydroxymuconic-semialdehyde hydrolase) and ohpD (catechol 2,3-dioxygenase), the ortho-hydroxyphenylpropionic acid catabolic pathway in Rhodococcus strain V49 (ATCC 19070) has been predicted.

Original language	English (US)
Pages (from-to)	175-188
Number of pages	14
Journal	Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
Volume	74
Issue number	1-3
DOIs	https://doi.org/10.1023/A:1001784702230
State	Published - 1998
Externally published	Yes

Keywords

Catechol 2,3-dioxygenase
Gene disruption
Hydroxymuconicsemialdehyde hydrolase
Monooxygenase operon
Rhodococcus

ASJC Scopus subject areas

Microbiology
Molecular Biology

Access to Document

10.1023/A:1001784702230

Cite this

@article{836208777c0a41819a8584406b1798b9,

title = "Molecular characterisation of a Rhodococcus ohp operon",

abstract = "The ohp operon of Rhodococcus strain V49 consists of five genes, ohpR, ohpA, ohpB, ohpC and ohpD which encode putative regulator and transport proteins and confirmed monooxygenase, hydroxymuconic semialdehyde hydrolase and catechol 2,3-dioxygenase enzymes, respectively. These enzymes catalyse the conversion of 3-(2-hydroxyphenyl) propionic acid to the corresponding linear product via a meta-cleavage pathway. Confirmation that the ohp gene cluster formed an operon was provided by gene disruption during which expression of Bacillus levansucrase was confirmed in Rhodococcus. Following biochemical assays of cell-free extracts from recombinant Escherichia coli expressing ohpB (monooxygenase), ohpC (hydroxymuconic-semialdehyde hydrolase) and ohpD (catechol 2,3-dioxygenase), the ortho-hydroxyphenylpropionic acid catabolic pathway in Rhodococcus strain V49 (ATCC 19070) has been predicted.",

keywords = "Catechol 2,3-dioxygenase, Gene disruption, Hydroxymuconicsemialdehyde hydrolase, Monooxygenase operon, Rhodococcus",

author = "Powell, {Justin A.C.} and Archer, {John A.C.}",

year = "1998",

doi = "10.1023/A:1001784702230",

language = "English (US)",

volume = "74",

pages = "175--188",

journal = "Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology",

issn = "0003-6072",

publisher = "Springer Verlag",

number = "1-3",

}

TY - JOUR

T1 - Molecular characterisation of a Rhodococcus ohp operon

AU - Powell, Justin A.C.

AU - Archer, John A.C.

PY - 1998

Y1 - 1998

N2 - The ohp operon of Rhodococcus strain V49 consists of five genes, ohpR, ohpA, ohpB, ohpC and ohpD which encode putative regulator and transport proteins and confirmed monooxygenase, hydroxymuconic semialdehyde hydrolase and catechol 2,3-dioxygenase enzymes, respectively. These enzymes catalyse the conversion of 3-(2-hydroxyphenyl) propionic acid to the corresponding linear product via a meta-cleavage pathway. Confirmation that the ohp gene cluster formed an operon was provided by gene disruption during which expression of Bacillus levansucrase was confirmed in Rhodococcus. Following biochemical assays of cell-free extracts from recombinant Escherichia coli expressing ohpB (monooxygenase), ohpC (hydroxymuconic-semialdehyde hydrolase) and ohpD (catechol 2,3-dioxygenase), the ortho-hydroxyphenylpropionic acid catabolic pathway in Rhodococcus strain V49 (ATCC 19070) has been predicted.

AB - The ohp operon of Rhodococcus strain V49 consists of five genes, ohpR, ohpA, ohpB, ohpC and ohpD which encode putative regulator and transport proteins and confirmed monooxygenase, hydroxymuconic semialdehyde hydrolase and catechol 2,3-dioxygenase enzymes, respectively. These enzymes catalyse the conversion of 3-(2-hydroxyphenyl) propionic acid to the corresponding linear product via a meta-cleavage pathway. Confirmation that the ohp gene cluster formed an operon was provided by gene disruption during which expression of Bacillus levansucrase was confirmed in Rhodococcus. Following biochemical assays of cell-free extracts from recombinant Escherichia coli expressing ohpB (monooxygenase), ohpC (hydroxymuconic-semialdehyde hydrolase) and ohpD (catechol 2,3-dioxygenase), the ortho-hydroxyphenylpropionic acid catabolic pathway in Rhodococcus strain V49 (ATCC 19070) has been predicted.

KW - Catechol 2,3-dioxygenase

KW - Gene disruption

KW - Hydroxymuconicsemialdehyde hydrolase

KW - Monooxygenase operon

KW - Rhodococcus

UR - http://www.scopus.com/inward/record.url?scp=0032461682&partnerID=8YFLogxK

U2 - 10.1023/A:1001784702230

DO - 10.1023/A:1001784702230

M3 - Article

C2 - 10068799

AN - SCOPUS:0032461682

SN - 0003-6072

VL - 74

SP - 175

EP - 188

JO - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

JF - Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology

IS - 1-3

ER -

Molecular characterisation of a Rhodococcus ohp operon

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this