Expression and flavinylation of Arthrobacter oxydans 6-hydroxy-D-nicotine oxidase in Bacillus subtilis
(1989) In Journal of General Microbiology 135(1093-1099).- Abstract
- 6-Hydroxy-d-nicotine oxidase (6-HDNO) of Arthrobacter oxydans, an enzyme inducible by dl-nicotine, contains FAD covalently bound via an 8α-N(3)His linkage. Expression of the gene encoding 6-HDNO and flavinylation of the protein were studied in Bacillus subtilis. In this heterologous system the following findings were made. 1. An enzymically active covalently flavinylated 6-HDNO of normal size can be expressed in B. subtilis. 2. The natural promoter of the 6-HDNO gene appeared inefficient in B. subtilis. The B. subtilis sdh promoter, when inserted upstream of the A. oxydans promoter, increased 6-HDNO expression >50-fold. 3. Expression of the 6-HDNO gene from plasmids in B. subtilis was, independently of the promoter construct used,... (More)
- 6-Hydroxy-d-nicotine oxidase (6-HDNO) of Arthrobacter oxydans, an enzyme inducible by dl-nicotine, contains FAD covalently bound via an 8α-N(3)His linkage. Expression of the gene encoding 6-HDNO and flavinylation of the protein were studied in Bacillus subtilis. In this heterologous system the following findings were made. 1. An enzymically active covalently flavinylated 6-HDNO of normal size can be expressed in B. subtilis. 2. The natural promoter of the 6-HDNO gene appeared inefficient in B. subtilis. The B. subtilis sdh promoter, when inserted upstream of the A. oxydans promoter, increased 6-HDNO expression >50-fold. 3. Expression of the 6-HDNO gene from plasmids in B. subtilis was, independently of the promoter construct used, stimulated more than fivefold by dl-nicotine in the growth medium. It is concluded that flavinylation of 6-HDNO is possibly autocatalytic and mediated by factors generally found in bacterial cells. (Less)
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- author
- Brandsch, Roderich and Hederstedt, Lars LU
- organization
- publishing date
- 1989
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of General Microbiology
- volume
- 135
- issue
- 1093-1099
- publisher
- MAIK Nauka/Interperiodica
- external identifiers
-
- scopus:0024307646
- ISSN
- 0022-1287
- DOI
- 10.1099/00221287-135-5-1093
- language
- English
- LU publication?
- yes
- id
- f55899e7-a39c-42d8-865e-c008320fbebc
- date added to LUP
- 2017-07-18 10:51:39
- date last changed
- 2021-02-07 05:28:57
@article{f55899e7-a39c-42d8-865e-c008320fbebc,
abstract = {{6-Hydroxy-d-nicotine oxidase (6-HDNO) of Arthrobacter oxydans, an enzyme inducible by dl-nicotine, contains FAD covalently bound via an 8α-N(3)His linkage. Expression of the gene encoding 6-HDNO and flavinylation of the protein were studied in Bacillus subtilis. In this heterologous system the following findings were made. 1. An enzymically active covalently flavinylated 6-HDNO of normal size can be expressed in B. subtilis. 2. The natural promoter of the 6-HDNO gene appeared inefficient in B. subtilis. The B. subtilis sdh promoter, when inserted upstream of the A. oxydans promoter, increased 6-HDNO expression >50-fold. 3. Expression of the 6-HDNO gene from plasmids in B. subtilis was, independently of the promoter construct used, stimulated more than fivefold by dl-nicotine in the growth medium. It is concluded that flavinylation of 6-HDNO is possibly autocatalytic and mediated by factors generally found in bacterial cells.}},
author = {{Brandsch, Roderich and Hederstedt, Lars}},
issn = {{0022-1287}},
language = {{eng}},
number = {{1093-1099}},
publisher = {{MAIK Nauka/Interperiodica}},
series = {{Journal of General Microbiology}},
title = {{Expression and flavinylation of <em>Arthrobacter oxydans</em> 6-hydroxy-D-nicotine oxidase in <em>Bacillus subtilis</em>}},
url = {{http://dx.doi.org/10.1099/00221287-135-5-1093}},
doi = {{10.1099/00221287-135-5-1093}},
volume = {{135}},
year = {{1989}},
}