Nitroreductase

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{{STRUCTURE_1f5v| PDB=1f5v | SIZE=400| SCENE= |right|CAPTION=E. coli nitroreductase dimer containing FMN, [[1f5v]] }}
{{STRUCTURE_1f5v| PDB=1f5v | SIZE=400| SCENE= |right|CAPTION=E. coli nitroreductase dimer containing FMN, [[1f5v]] }}
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== Function ==
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'''Nitroreductase''' (NR) is involved in the reduction of nitrogen-containing compounds including those containing NO<sub>2</sub> group. The NO<sub>2</sub> group is reduced to hydroxylamine<ref>PMID:11491290</ref>. NR uses FMN as cofactor. Among NRs are the oxygen-insensitive NAD(P)H NR and NADH dehydrogenase.
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== Relevance ==
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The NR is of special interest due to its potential use as activator of prodrugs in cancer therapy.
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'''Nitroreductase''' (NR) is involved in the reduction of nitrogen-containing compounds including those containing NO<sub>2</sub> group. The NO<sub>2</sub> group is reduced to hydroxylamine. NR use FMN as cofactor. Among NRs are the oxygen-insensitive NAD(P)H NR and NADH dehydrogenase. The NR is of special interest due to its potential use as activator of prodrugs in cancer therapy.
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==3D structures of nitroreductase==
==3D structures of nitroreductase==
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**[[2wzw]] - MsNR + NADPH
**[[2wzw]] - MsNR + NADPH
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:55, 15 May 2016

Template:STRUCTURE 1f5v

Contents

Function

Nitroreductase (NR) is involved in the reduction of nitrogen-containing compounds including those containing NO2 group. The NO2 group is reduced to hydroxylamine[1]. NR uses FMN as cofactor. Among NRs are the oxygen-insensitive NAD(P)H NR and NADH dehydrogenase.

Relevance

The NR is of special interest due to its potential use as activator of prodrugs in cancer therapy.

3D structures of nitroreductase

Updated on 15-May-2016

References

  1. Lovering AL, Hyde EI, Searle PF, White SA. The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution. J Mol Biol. 2001 May 25;309(1):203-13. PMID:11491290 doi:10.1006/jmbi.2001.4653

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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