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A kinetic analysis of three modified novel nitroreductases
A kinetic comparison between three nitroreductase enzymes isolated from the genome of Bacillus licheniformis ATCC 14580 for prospective use as immobilised enzymes for explosives detection has been conducted. The genes encoding the three enzymes ( yfkO [BLNfnB] encoding an NfsB-like enzyme; nfrA [BLN...
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| Published in: | Biodegradation (Dordrecht) 2011-04, Vol.22 (2), p.463-474 |
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| Main Authors: | , , , |
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| cited_by | cdi_FETCH-LOGICAL-c499t-1dd61438eed46705f97ce733ec8f26b7d8ea550c1544450cc5e9d4977002b9293 |
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| cites | cdi_FETCH-LOGICAL-c499t-1dd61438eed46705f97ce733ec8f26b7d8ea550c1544450cc5e9d4977002b9293 |
| container_end_page | 474 |
| container_issue | 2 |
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| container_title | Biodegradation (Dordrecht) |
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| creator | Gwenin, Christopher D. Kalaji, Maher Williams, Peter A. Kay, Catherine M. |
| description | A kinetic comparison between three nitroreductase enzymes isolated from the genome of
Bacillus licheniformis
ATCC 14580 for prospective use as immobilised enzymes for explosives detection has been conducted. The genes encoding the three enzymes (
yfkO
[BLNfnB] encoding an NfsB-like enzyme;
nfrA
[BLNfrA1] and
ycnD
[BLNfrA2] encoding PnrA-like enzymes) have been PCR amplified from the native genome and cloned into pET-28a(+) and a modified cysteine
(6)
-tagged pET-28a(+) and subsequently over-expressed, purified, and biochemically characterised. The previously uncharacterised nitroreductases exhibited activity against a wide range of explosives, including cyclic nitramines. Amino acid alignments and overall structural comparisons with other nitroreductase family members suggest that the
B. licheniformis
enzymes are members of the NfsA-Frp/NfsB-FRase I family group. Despite the overall low amino acid identity, regions for flavin mononucleotide binding and active site residues were highly conserved. |
| doi_str_mv | 10.1007/s10532-010-9418-0 |
| format | article |
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Bacillus licheniformis
ATCC 14580 for prospective use as immobilised enzymes for explosives detection has been conducted. The genes encoding the three enzymes (
yfkO
[BLNfnB] encoding an NfsB-like enzyme;
nfrA
[BLNfrA1] and
ycnD
[BLNfrA2] encoding PnrA-like enzymes) have been PCR amplified from the native genome and cloned into pET-28a(+) and a modified cysteine
(6)
-tagged pET-28a(+) and subsequently over-expressed, purified, and biochemically characterised. The previously uncharacterised nitroreductases exhibited activity against a wide range of explosives, including cyclic nitramines. Amino acid alignments and overall structural comparisons with other nitroreductase family members suggest that the
B. licheniformis
enzymes are members of the NfsA-Frp/NfsB-FRase I family group. Despite the overall low amino acid identity, regions for flavin mononucleotide binding and active site residues were highly conserved.</description><identifier>ISSN: 0923-9820</identifier><identifier>EISSN: 1572-9729</identifier><identifier>DOI: 10.1007/s10532-010-9418-0</identifier><identifier>PMID: 20862523</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino acids ; Analysis ; Animal genetic engineering ; Aquatic Pollution ; Bacillus - enzymology ; Bacillus - genetics ; Bacillus licheniformis ; Bacteria ; Biodegradation of pollutants ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Environment and pollution ; Enzymes ; Explosives ; Fundamental and applied biological sciences. Psychology ; Genomics ; Geochemistry ; Hydrogen-Ion Concentration ; Industrial applications and implications. Economical aspects ; Kinetics ; Life Sciences ; Microbiology ; Nitroreductases - genetics ; Nitroreductases - metabolism ; Original Paper ; Pets ; Polymerase Chain Reaction ; Protein Binding ; Soil Science & Conservation ; Terrestrial Pollution ; Waste Management/Waste Technology ; Waste Water Technology ; Water Management ; Water Pollution Control</subject><ispartof>Biodegradation (Dordrecht), 2011-04, Vol.22 (2), p.463-474</ispartof><rights>Springer Science+Business Media B.V. 2010</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2011 Springer</rights><rights>Springer Science+Business Media B.V. 2011</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-1dd61438eed46705f97ce733ec8f26b7d8ea550c1544450cc5e9d4977002b9293</citedby><cites>FETCH-LOGICAL-c499t-1dd61438eed46705f97ce733ec8f26b7d8ea550c1544450cc5e9d4977002b9293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23948345$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20862523$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gwenin, Christopher D.</creatorcontrib><creatorcontrib>Kalaji, Maher</creatorcontrib><creatorcontrib>Williams, Peter A.</creatorcontrib><creatorcontrib>Kay, Catherine M.</creatorcontrib><title>A kinetic analysis of three modified novel nitroreductases</title><title>Biodegradation (Dordrecht)</title><addtitle>Biodegradation</addtitle><addtitle>Biodegradation</addtitle><description>A kinetic comparison between three nitroreductase enzymes isolated from the genome of
Bacillus licheniformis
ATCC 14580 for prospective use as immobilised enzymes for explosives detection has been conducted. The genes encoding the three enzymes (
yfkO
[BLNfnB] encoding an NfsB-like enzyme;
nfrA
[BLNfrA1] and
ycnD
[BLNfrA2] encoding PnrA-like enzymes) have been PCR amplified from the native genome and cloned into pET-28a(+) and a modified cysteine
(6)
-tagged pET-28a(+) and subsequently over-expressed, purified, and biochemically characterised. The previously uncharacterised nitroreductases exhibited activity against a wide range of explosives, including cyclic nitramines. Amino acid alignments and overall structural comparisons with other nitroreductase family members suggest that the
B. licheniformis
enzymes are members of the NfsA-Frp/NfsB-FRase I family group. Despite the overall low amino acid identity, regions for flavin mononucleotide binding and active site residues were highly conserved.</description><subject>Amino acids</subject><subject>Analysis</subject><subject>Animal genetic engineering</subject><subject>Aquatic Pollution</subject><subject>Bacillus - enzymology</subject><subject>Bacillus - genetics</subject><subject>Bacillus licheniformis</subject><subject>Bacteria</subject><subject>Biodegradation of pollutants</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Environment and pollution</subject><subject>Enzymes</subject><subject>Explosives</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genomics</subject><subject>Geochemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Nitroreductases - genetics</subject><subject>Nitroreductases - metabolism</subject><subject>Original Paper</subject><subject>Pets</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Binding</subject><subject>Soil Science & Conservation</subject><subject>Terrestrial Pollution</subject><subject>Waste Management/Waste Technology</subject><subject>Waste Water Technology</subject><subject>Water Management</subject><subject>Water Pollution Control</subject><issn>0923-9820</issn><issn>1572-9729</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqFkV2L1TAQhoMo7nH1B3gjRRGvuk6-msa7w-IXLHij1yEnmaxZ22ZNWmH_vak9uiiKzMXA5HknM_MS8pjCGQVQLwsFyVkLFFotaN_CHbKjUrFWK6bvkh1oxlvdMzghD0q5AgCtgN0nJwz6jknGd-TVvvkSJ5yja-xkh5sSS5NCM3_OiM2YfAwRfTOlbzg0U5xzyugXN9uC5SG5F-xQ8NExn5JPb15_PH_XXnx4-_58f9E6ofXcUu87KniP6EWnQAatHCrO0fWBdQfle7RSgqNSCFGzk6i90EoBsINmmp-SF1vf65y-LlhmM8bicBjshGkppu-A66qk_yelkJ3odFfJp3-QV2nJ9QA_IEq5VrJCzzbo0g5o4hTSnK1bW5q9ooxppvp1vLO_UDU8jtGlCUOs9d8EdBO4nErJGMx1jqPNN4aCWX01m6-m-mpWXw1UzZPjvMthRP9L8dPICjw_ArY4O4RsJxfLLVcv1HOx7sQ2rtSn6RLz7eL__v07T9S2Rg</recordid><startdate>20110401</startdate><enddate>20110401</enddate><creator>Gwenin, Christopher D.</creator><creator>Kalaji, Maher</creator><creator>Williams, Peter A.</creator><creator>Kay, Catherine M.</creator><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7ST</scope><scope>7T7</scope><scope>7UA</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H97</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>SOI</scope><scope>7X8</scope><scope>7QH</scope><scope>7QO</scope></search><sort><creationdate>20110401</creationdate><title>A kinetic analysis of three modified novel nitroreductases</title><author>Gwenin, Christopher D. ; Kalaji, Maher ; Williams, Peter A. ; Kay, Catherine M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-1dd61438eed46705f97ce733ec8f26b7d8ea550c1544450cc5e9d4977002b9293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Analysis</topic><topic>Animal genetic engineering</topic><topic>Aquatic Pollution</topic><topic>Bacillus - enzymology</topic><topic>Bacillus - genetics</topic><topic>Bacillus licheniformis</topic><topic>Bacteria</topic><topic>Biodegradation of pollutants</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Environment and pollution</topic><topic>Enzymes</topic><topic>Explosives</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genomics</topic><topic>Geochemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Nitroreductases - genetics</topic><topic>Nitroreductases - metabolism</topic><topic>Original Paper</topic><topic>Pets</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Binding</topic><topic>Soil Science & Conservation</topic><topic>Terrestrial Pollution</topic><topic>Waste Management/Waste Technology</topic><topic>Waste Water Technology</topic><topic>Water Management</topic><topic>Water Pollution Control</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gwenin, Christopher D.</creatorcontrib><creatorcontrib>Kalaji, Maher</creatorcontrib><creatorcontrib>Williams, Peter A.</creatorcontrib><creatorcontrib>Kay, Catherine M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Water Resources Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Earth, Atmospheric & Aquatic Science</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Aqualine</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Biodegradation (Dordrecht)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gwenin, Christopher D.</au><au>Kalaji, Maher</au><au>Williams, Peter A.</au><au>Kay, Catherine M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A kinetic analysis of three modified novel nitroreductases</atitle><jtitle>Biodegradation (Dordrecht)</jtitle><stitle>Biodegradation</stitle><addtitle>Biodegradation</addtitle><date>2011-04-01</date><risdate>2011</risdate><volume>22</volume><issue>2</issue><spage>463</spage><epage>474</epage><pages>463-474</pages><issn>0923-9820</issn><eissn>1572-9729</eissn><abstract>A kinetic comparison between three nitroreductase enzymes isolated from the genome of
Bacillus licheniformis
ATCC 14580 for prospective use as immobilised enzymes for explosives detection has been conducted. The genes encoding the three enzymes (
yfkO
[BLNfnB] encoding an NfsB-like enzyme;
nfrA
[BLNfrA1] and
ycnD
[BLNfrA2] encoding PnrA-like enzymes) have been PCR amplified from the native genome and cloned into pET-28a(+) and a modified cysteine
(6)
-tagged pET-28a(+) and subsequently over-expressed, purified, and biochemically characterised. The previously uncharacterised nitroreductases exhibited activity against a wide range of explosives, including cyclic nitramines. Amino acid alignments and overall structural comparisons with other nitroreductase family members suggest that the
B. licheniformis
enzymes are members of the NfsA-Frp/NfsB-FRase I family group. Despite the overall low amino acid identity, regions for flavin mononucleotide binding and active site residues were highly conserved.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>20862523</pmid><doi>10.1007/s10532-010-9418-0</doi><tpages>12</tpages></addata></record> |
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| ispartof | Biodegradation (Dordrecht), 2011-04, Vol.22 (2), p.463-474 |
| issn | 0923-9820 1572-9729 |
| language | eng |
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| subjects | Amino acids Analysis Animal genetic engineering Aquatic Pollution Bacillus - enzymology Bacillus - genetics Bacillus licheniformis Bacteria Biodegradation of pollutants Biological and medical sciences Biomedical and Life Sciences Biotechnology Environment and pollution Enzymes Explosives Fundamental and applied biological sciences. Psychology Genomics Geochemistry Hydrogen-Ion Concentration Industrial applications and implications. Economical aspects Kinetics Life Sciences Microbiology Nitroreductases - genetics Nitroreductases - metabolism Original Paper Pets Polymerase Chain Reaction Protein Binding Soil Science & Conservation Terrestrial Pollution Waste Management/Waste Technology Waste Water Technology Water Management Water Pollution Control |
| title | A kinetic analysis of three modified novel nitroreductases |
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