Abstract |
Lack of molybdenum cofactor (MoCo) in Escherichia coli and related microorganisms was found to cause hypersensitivity to certain N-hydroxylated base analogs, such as HAP (6-N-hydroxylaminopurine). This observation has lead to a previous proposal that E. coli contains a molybdoenzyme capable of detoxifying such N-hydroxylated analogs. Here, we show that, unexpectedly, deletion of all known or putative molybdoenzymes in E. coli failed to reveal any base-analog sensitivity, suggesting that a novel type of MoCo-dependent activity is involved. Further, we establish that protection against the analogs does not require the common molybdopterin guanine-dinucleotide (MGD) form of the cofactor, but instead the guanosine monophosphate (GMP)-free version of MoCo (MPT) is sufficient.
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Authors | Stanislav G Kozmin, Roel M Schaaper |
Journal | Mutation research
(Mutat Res)
Vol. 619
Issue 1-2
Pg. 9-15
(Jun 01 2007)
ISSN: 0027-5107 [Print] Netherlands |
PMID | 17349664
(Publication Type: Journal Article, Research Support, N.I.H., Intramural)
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Chemical References |
- Coenzymes
- Escherichia coli Proteins
- Metalloproteins
- Molybdenum Cofactors
- Mutagens
- Pteridines
- mobA protein, E coli
- 6-N-hydroxylaminopurine
- molybdenum cofactor
- Adenine
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Topics |
- Adenine
(analogs & derivatives, toxicity)
- Coenzymes
(chemistry, metabolism)
- Drug Resistance, Bacterial
(genetics)
- Escherichia coli
(drug effects, genetics, metabolism)
- Escherichia coli Proteins
(genetics, metabolism)
- Genes, Bacterial
- Metalloproteins
(chemistry, metabolism)
- Molybdenum Cofactors
- Mutagens
(toxicity)
- Pteridines
(chemistry, metabolism)
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