AustralieFrV1, Main, Exploration, bibRecordById, PMC:3034190

Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

Identifieur interne : 007807 ( Main/Exploration ); précédent : 007806; suivant : 007808

Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

Auteurs : Matthew C. Taylor [Australie] ; Colin J. Jackson [Australie, France] ; David B. Tattersall [Australie] ; Nigel French [Australie] ; Thomas S. Peat [Australie] ; Janet Newman [Australie] ; Lyndall J. Briggs [Australie] ; Gauri V. Lapalikar [Australie] ; Peter M. Campbell [Australie] ; Colin Scott [Australie] ; Robyn J. Russell [Australie] ; John G. Oakeshott [Australie]

Source :

Molecular microbiology : (Print) [ 0950-382X ] ; 2010.

RBID : Pascal:11-0085740

Descripteurs français

Pascal (Inist)
- Mycobacterium, Identification, Reductase, Aflatoxine.

English descriptors

KwdEn :
- Aflatoxin, Identification, Mycobacterium, Reductase.

Abstract

Aflatoxins are polyaromatic mycotoxins that contaminate a range of food crops as a result of fungal growth and contribute to serious health problems in the developing world because of their toxicity and mutagenicity. Although relatively resistant to biotic degradation, aflatoxins can be metabolized by certain species of Actinomycetales. However, the enzymatic basis for their breakdown has not been reported until now. We have identified nine Mycobacterium smegmatis enzymes that utilize the deazaflavin cofactor F₄₂₀H₂ to catalyse the reduction of the α,β-unsaturated ester moiety of aflatoxins, activating the molecules for spontaneous hydrolysis and detoxification. These enzymes belong to two previously uncharacterized F₄₂₀H₂ dependent reductase (FDR-A and -B) families that are distantly related to the flavin mononucleotide (FMN) dependent pyridoxamine 5'-phosphate oxidases (PNPOxs). We have solved crystal structures of an enzyme from each FDR family and show that they, like the PNPOxs, adopt a split barrel protein fold, although the FDRs also possess an extended and highly charged F₄₂₀H₂ binding groove. A general role for these enzymes in xenobiotic metabolism is discussed, including the observation that the nitro-reductase Rv3547 from Mycobacterium tuberculosis that is responsible for the activation of bicyclic nitroimidazole prodrugs belongs to the FDR-A family.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3034190

Affiliations:

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Identification and characterization of two families of F<sub>420</sub>
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<author><name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J." last="Russell">Robyn J. Russell</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>CSIRO Ecosystem Sciences, GPO Box 1700</s1>
<s2>Canberra, ACT 2601</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
</inist:fA14>
<country>Australie</country>
<wicri:noRegion>Canberra, ACT 2601</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G." last="Oakeshott">John G. Oakeshott</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>CSIRO Ecosystem Sciences, GPO Box 1700</s1>
<s2>Canberra, ACT 2601</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
</inist:fA14>
<country>Australie</country>
<wicri:noRegion>Canberra, ACT 2601</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Molecular microbiology : (Print)</title>
<title level="j" type="abbreviated">Mol. microbiol. : (Print)</title>
<idno type="ISSN">0950-382X</idno>
<imprint><date when="2010">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Molecular microbiology : (Print)</title>
<title level="j" type="abbreviated">Mol. microbiol. : (Print)</title>
<idno type="ISSN">0950-382X</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aflatoxin</term>
<term>Identification</term>
<term>Mycobacterium</term>
<term>Reductase</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Mycobacterium</term>
<term>Identification</term>
<term>Reductase</term>
<term>Aflatoxine</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Aflatoxins are polyaromatic mycotoxins that contaminate a range of food crops as a result of fungal growth and contribute to serious health problems in the developing world because of their toxicity and mutagenicity. Although relatively resistant to biotic degradation, aflatoxins can be metabolized by certain species of Actinomycetales. However, the enzymatic basis for their breakdown has not been reported until now. We have identified nine Mycobacterium smegmatis enzymes that utilize the deazaflavin cofactor F<sub>420</sub>
H<sub>2</sub>
 to catalyse the reduction of the α,β-unsaturated ester moiety of aflatoxins, activating the molecules for spontaneous hydrolysis and detoxification. These enzymes belong to two previously uncharacterized F<sub>420</sub>
H<sub>2</sub>
 dependent reductase (FDR-A and -B) families that are distantly related to the flavin mononucleotide (FMN) dependent pyridoxamine 5'-phosphate oxidases (PNPOxs). We have solved crystal structures of an enzyme from each FDR family and show that they, like the PNPOxs, adopt a split barrel protein fold, although the FDRs also possess an extended and highly charged F<sub>420</sub>
H<sub>2</sub>
 binding groove. A general role for these enzymes in xenobiotic metabolism is discussed, including the observation that the nitro-reductase Rv3547 from Mycobacterium tuberculosis that is responsible for the activation of bicyclic nitroimidazole prodrugs belongs to the FDR-A family.</div>
</front>
</TEI>
<affiliations><list><country><li>Australie</li>
<li>France</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Grenoble</li>
</settlement>
</list>
<tree><country name="Australie"><noRegion><name sortKey="Taylor, Matthew C" sort="Taylor, Matthew C" uniqKey="Taylor M" first="Matthew C." last="Taylor">Matthew C. Taylor</name>
</noRegion>
<name sortKey="Briggs, Lyndall J" sort="Briggs, Lyndall J" uniqKey="Briggs L" first="Lyndall J." last="Briggs">Lyndall J. Briggs</name>
<name sortKey="Campbell, Peter M" sort="Campbell, Peter M" uniqKey="Campbell P" first="Peter M." last="Campbell">Peter M. Campbell</name>
<name sortKey="French, Nigel" sort="French, Nigel" uniqKey="French N" first="Nigel" last="French">Nigel French</name>
<name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J." last="Jackson">Colin J. Jackson</name>
<name sortKey="Lapalikar, Gauri V" sort="Lapalikar, Gauri V" uniqKey="Lapalikar G" first="Gauri V." last="Lapalikar">Gauri V. Lapalikar</name>
<name sortKey="Newman, Janet" sort="Newman, Janet" uniqKey="Newman J" first="Janet" last="Newman">Janet Newman</name>
<name sortKey="Oakeshott, John G" sort="Oakeshott, John G" uniqKey="Oakeshott J" first="John G." last="Oakeshott">John G. Oakeshott</name>
<name sortKey="Peat, Thomas S" sort="Peat, Thomas S" uniqKey="Peat T" first="Thomas S." last="Peat">Thomas S. Peat</name>
<name sortKey="Russell, Robyn J" sort="Russell, Robyn J" uniqKey="Russell R" first="Robyn J." last="Russell">Robyn J. Russell</name>
<name sortKey="Scott, Colin" sort="Scott, Colin" uniqKey="Scott C" first="Colin" last="Scott">Colin Scott</name>
<name sortKey="Tattersall, David B" sort="Tattersall, David B" uniqKey="Tattersall D" first="David B." last="Tattersall">David B. Tattersall</name>
</country>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Jackson, Colin J" sort="Jackson, Colin J" uniqKey="Jackson C" first="Colin J." last="Jackson">Colin J. Jackson</name>
</region>
</country>
</tree>
</affiliations>
</record>

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Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

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