Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome
Glucose hydrolyzing enzymes are essential to determine blood glucose level. A high-throughput screening approach was established to identify NAD(P)-dependent glucose dehydrogenases for the application in test stripes and the respective blood glucose meters. In the current report a glucose hydrolyzin...
Gespeichert in:
| Veröffentlicht in: | PloS one 2014-01, Vol.9 (1), p.e85844-e85844 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e85844 |
|---|---|
| container_issue | 1 |
| container_start_page | e85844 |
| container_title | PloS one |
| container_volume | 9 |
| creator | Basner, Alexander Antranikian, Garabed |
| description | Glucose hydrolyzing enzymes are essential to determine blood glucose level. A high-throughput screening approach was established to identify NAD(P)-dependent glucose dehydrogenases for the application in test stripes and the respective blood glucose meters. In the current report a glucose hydrolyzing enzyme, derived from a metagenomic library by expressing recombinant DNA fragments isolated from hay infusion, was characterized. The recombinant clone showing activity on glucose as substrate exhibited an open reading frame of 987 bp encoding for a peptide of 328 amino acids. The isolated enzyme showed typical sequence motifs of short-chain-dehydrogenases using NAD(P) as a co-factor and had a sequence similarity between 33 and 35% to characterized glucose dehydrogenases from different Bacillus species. The identified glucose dehydrogenase gene was expressed in E. coli, purified and subsequently characterized. The enzyme, belonging to the superfamily of short-chain dehydrogenases, shows a broad substrate range with a high affinity to glucose, xylose and glucose-6-phosphate. Due to its ability to be strongly associated with its cofactor NAD(P), the enzyme is able to directly transfer electrons from glucose oxidation to external electron acceptors by regenerating the cofactor while being still associated to the protein. |
| doi_str_mv | 10.1371/journal.pone.0085844 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1477433272</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A478865631</galeid><doaj_id>oai_doaj_org_article_64272fbe366c4633bc3a54747e36368d</doaj_id><sourcerecordid>A478865631</sourcerecordid><originalsourceid>FETCH-LOGICAL-c692t-6aaf6fcb5a1c1dae4b07fdce82c1cd557e983f94085f16169027b29cc44fc1583</originalsourceid><addsrcrecordid>eNqNk1uL1DAUgIso7jr6D0QLgujDjE1zafMiLIuXgYUFb6_hNE3aDGkzm7Ti-OtNne4ylX2QPDQ95zsn55okz1G2QbhA73Zu9D3Yzd71apNlJS0JeZCcI47zNcsz_PDkfpY8CWGXZRSXjD1OznJCKOGYnif1NjgLg3F9Cn2dVsbJVnVGgk1lCx7koLz5fQScTiFt7ChdUGmt2kPtXaN6iH_auy4qWzikptdjmPBODRDVrlNPk0cabFDP5u8q-f7xw7fLz-ur60_by4urtWQ8H9YMQDMtKwpIohoUqbJC11KVuUSyprRQvMSak5irRgwxnuVFlXMpCdES0RKvkpdHv3vrgpgLFAQiRUEwzos8EtsjUTvYib03HfiDcGDEX4HzjQA_GGmVYCQa6EphxiRhGFcSAyUFKaIEs7KOvt7Pr41Vp2Kc_eDBLpwuNb1pReN-ClxyVMaIVsmb2YF3N6MKg-hMkMpa6JUbp7h5zjhmlEf01T_o_dnNVAMxgdgIF9-Vk1NxQYqyZJRhFKnNPVQ89dT4OE3aRPnC4O3CIDKD-jU0MIYgtl-__D97_WPJvj5hWwV2aOM0jtOwhSVIjqD0LgSv9F2RUSamZbithpiWQczLEM1enDbozuh2-vEfEQ0FWg</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1477433272</pqid></control><display><type>article</type><title>Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Public Library of Science (PLoS) Journals Open Access</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Basner, Alexander ; Antranikian, Garabed</creator><contributor>Permyakov, Eugene A.</contributor><creatorcontrib>Basner, Alexander ; Antranikian, Garabed ; Permyakov, Eugene A.</creatorcontrib><description>Glucose hydrolyzing enzymes are essential to determine blood glucose level. A high-throughput screening approach was established to identify NAD(P)-dependent glucose dehydrogenases for the application in test stripes and the respective blood glucose meters. In the current report a glucose hydrolyzing enzyme, derived from a metagenomic library by expressing recombinant DNA fragments isolated from hay infusion, was characterized. The recombinant clone showing activity on glucose as substrate exhibited an open reading frame of 987 bp encoding for a peptide of 328 amino acids. The isolated enzyme showed typical sequence motifs of short-chain-dehydrogenases using NAD(P) as a co-factor and had a sequence similarity between 33 and 35% to characterized glucose dehydrogenases from different Bacillus species. The identified glucose dehydrogenase gene was expressed in E. coli, purified and subsequently characterized. The enzyme, belonging to the superfamily of short-chain dehydrogenases, shows a broad substrate range with a high affinity to glucose, xylose and glucose-6-phosphate. Due to its ability to be strongly associated with its cofactor NAD(P), the enzyme is able to directly transfer electrons from glucose oxidation to external electron acceptors by regenerating the cofactor while being still associated to the protein.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0085844</identifier><identifier>PMID: 24454935</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Bacillus megaterium ; Bacillus subtilis ; Biocatalysts ; Biology ; Blood ; Blood glucose ; Chains ; Cloning ; Dehydrogenase ; Dehydrogenases ; Deoxyribonucleic acid ; DNA ; E coli ; Enzyme Stability ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Gene expression ; Glucose ; Glucose - metabolism ; Glucose 1-Dehydrogenase - chemistry ; Glucose 1-Dehydrogenase - genetics ; Glucose 1-Dehydrogenase - isolation & purification ; Glucose 1-Dehydrogenase - metabolism ; Glucose dehydrogenase ; Hay ; High-throughput screening ; Hydrolysis ; Kinetics ; Measuring instruments ; Medical screening ; Metagenome ; Molecular Sequence Data ; NAD ; Oxidation ; Oxidoreductases ; Phosphates ; Poaceae - microbiology ; Poaceae - parasitology ; Recombinant DNA ; Sequence Analysis ; Substrate Specificity ; Substrates ; Temperature ; Xylose</subject><ispartof>PloS one, 2014-01, Vol.9 (1), p.e85844-e85844</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Basner, Antranikian. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Basner, Antranikian 2014 Basner, Antranikian</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-6aaf6fcb5a1c1dae4b07fdce82c1cd557e983f94085f16169027b29cc44fc1583</citedby><cites>FETCH-LOGICAL-c692t-6aaf6fcb5a1c1dae4b07fdce82c1cd557e983f94085f16169027b29cc44fc1583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3891874/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3891874/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24454935$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Permyakov, Eugene A.</contributor><creatorcontrib>Basner, Alexander</creatorcontrib><creatorcontrib>Antranikian, Garabed</creatorcontrib><title>Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Glucose hydrolyzing enzymes are essential to determine blood glucose level. A high-throughput screening approach was established to identify NAD(P)-dependent glucose dehydrogenases for the application in test stripes and the respective blood glucose meters. In the current report a glucose hydrolyzing enzyme, derived from a metagenomic library by expressing recombinant DNA fragments isolated from hay infusion, was characterized. The recombinant clone showing activity on glucose as substrate exhibited an open reading frame of 987 bp encoding for a peptide of 328 amino acids. The isolated enzyme showed typical sequence motifs of short-chain-dehydrogenases using NAD(P) as a co-factor and had a sequence similarity between 33 and 35% to characterized glucose dehydrogenases from different Bacillus species. The identified glucose dehydrogenase gene was expressed in E. coli, purified and subsequently characterized. The enzyme, belonging to the superfamily of short-chain dehydrogenases, shows a broad substrate range with a high affinity to glucose, xylose and glucose-6-phosphate. Due to its ability to be strongly associated with its cofactor NAD(P), the enzyme is able to directly transfer electrons from glucose oxidation to external electron acceptors by regenerating the cofactor while being still associated to the protein.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bacillus megaterium</subject><subject>Bacillus subtilis</subject><subject>Biocatalysts</subject><subject>Biology</subject><subject>Blood</subject><subject>Blood glucose</subject><subject>Chains</subject><subject>Cloning</subject><subject>Dehydrogenase</subject><subject>Dehydrogenases</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Gene expression</subject><subject>Glucose</subject><subject>Glucose - metabolism</subject><subject>Glucose 1-Dehydrogenase - chemistry</subject><subject>Glucose 1-Dehydrogenase - genetics</subject><subject>Glucose 1-Dehydrogenase - isolation & purification</subject><subject>Glucose 1-Dehydrogenase - metabolism</subject><subject>Glucose dehydrogenase</subject><subject>Hay</subject><subject>High-throughput screening</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Measuring instruments</subject><subject>Medical screening</subject><subject>Metagenome</subject><subject>Molecular Sequence Data</subject><subject>NAD</subject><subject>Oxidation</subject><subject>Oxidoreductases</subject><subject>Phosphates</subject><subject>Poaceae - microbiology</subject><subject>Poaceae - parasitology</subject><subject>Recombinant DNA</subject><subject>Sequence Analysis</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Temperature</subject><subject>Xylose</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk1uL1DAUgIso7jr6D0QLgujDjE1zafMiLIuXgYUFb6_hNE3aDGkzm7Ti-OtNne4ylX2QPDQ95zsn55okz1G2QbhA73Zu9D3Yzd71apNlJS0JeZCcI47zNcsz_PDkfpY8CWGXZRSXjD1OznJCKOGYnif1NjgLg3F9Cn2dVsbJVnVGgk1lCx7koLz5fQScTiFt7ChdUGmt2kPtXaN6iH_auy4qWzikptdjmPBODRDVrlNPk0cabFDP5u8q-f7xw7fLz-ur60_by4urtWQ8H9YMQDMtKwpIohoUqbJC11KVuUSyprRQvMSak5irRgwxnuVFlXMpCdES0RKvkpdHv3vrgpgLFAQiRUEwzos8EtsjUTvYib03HfiDcGDEX4HzjQA_GGmVYCQa6EphxiRhGFcSAyUFKaIEs7KOvt7Pr41Vp2Kc_eDBLpwuNb1pReN-ClxyVMaIVsmb2YF3N6MKg-hMkMpa6JUbp7h5zjhmlEf01T_o_dnNVAMxgdgIF9-Vk1NxQYqyZJRhFKnNPVQ89dT4OE3aRPnC4O3CIDKD-jU0MIYgtl-__D97_WPJvj5hWwV2aOM0jtOwhSVIjqD0LgSv9F2RUSamZbithpiWQczLEM1enDbozuh2-vEfEQ0FWg</recordid><startdate>20140114</startdate><enddate>20140114</enddate><creator>Basner, Alexander</creator><creator>Antranikian, Garabed</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140114</creationdate><title>Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome</title><author>Basner, Alexander ; Antranikian, Garabed</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-6aaf6fcb5a1c1dae4b07fdce82c1cd557e983f94085f16169027b29cc44fc1583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bacillus megaterium</topic><topic>Bacillus subtilis</topic><topic>Biocatalysts</topic><topic>Biology</topic><topic>Blood</topic><topic>Blood glucose</topic><topic>Chains</topic><topic>Cloning</topic><topic>Dehydrogenase</topic><topic>Dehydrogenases</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Gene expression</topic><topic>Glucose</topic><topic>Glucose - metabolism</topic><topic>Glucose 1-Dehydrogenase - chemistry</topic><topic>Glucose 1-Dehydrogenase - genetics</topic><topic>Glucose 1-Dehydrogenase - isolation & purification</topic><topic>Glucose 1-Dehydrogenase - metabolism</topic><topic>Glucose dehydrogenase</topic><topic>Hay</topic><topic>High-throughput screening</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Measuring instruments</topic><topic>Medical screening</topic><topic>Metagenome</topic><topic>Molecular Sequence Data</topic><topic>NAD</topic><topic>Oxidation</topic><topic>Oxidoreductases</topic><topic>Phosphates</topic><topic>Poaceae - microbiology</topic><topic>Poaceae - parasitology</topic><topic>Recombinant DNA</topic><topic>Sequence Analysis</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Temperature</topic><topic>Xylose</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Basner, Alexander</creatorcontrib><creatorcontrib>Antranikian, Garabed</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Access via ProQuest (Open Access)</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 China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Basner, Alexander</au><au>Antranikian, Garabed</au><au>Permyakov, Eugene A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-01-14</date><risdate>2014</risdate><volume>9</volume><issue>1</issue><spage>e85844</spage><epage>e85844</epage><pages>e85844-e85844</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Glucose hydrolyzing enzymes are essential to determine blood glucose level. A high-throughput screening approach was established to identify NAD(P)-dependent glucose dehydrogenases for the application in test stripes and the respective blood glucose meters. In the current report a glucose hydrolyzing enzyme, derived from a metagenomic library by expressing recombinant DNA fragments isolated from hay infusion, was characterized. The recombinant clone showing activity on glucose as substrate exhibited an open reading frame of 987 bp encoding for a peptide of 328 amino acids. The isolated enzyme showed typical sequence motifs of short-chain-dehydrogenases using NAD(P) as a co-factor and had a sequence similarity between 33 and 35% to characterized glucose dehydrogenases from different Bacillus species. The identified glucose dehydrogenase gene was expressed in E. coli, purified and subsequently characterized. The enzyme, belonging to the superfamily of short-chain dehydrogenases, shows a broad substrate range with a high affinity to glucose, xylose and glucose-6-phosphate. Due to its ability to be strongly associated with its cofactor NAD(P), the enzyme is able to directly transfer electrons from glucose oxidation to external electron acceptors by regenerating the cofactor while being still associated to the protein.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24454935</pmid><doi>10.1371/journal.pone.0085844</doi><tpages>e85844</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-01, Vol.9 (1), p.e85844-e85844 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1477433272 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Amino acids Bacillus megaterium Bacillus subtilis Biocatalysts Biology Blood Blood glucose Chains Cloning Dehydrogenase Dehydrogenases Deoxyribonucleic acid DNA E coli Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Gene expression Glucose Glucose - metabolism Glucose 1-Dehydrogenase - chemistry Glucose 1-Dehydrogenase - genetics Glucose 1-Dehydrogenase - isolation & purification Glucose 1-Dehydrogenase - metabolism Glucose dehydrogenase Hay High-throughput screening Hydrolysis Kinetics Measuring instruments Medical screening Metagenome Molecular Sequence Data NAD Oxidation Oxidoreductases Phosphates Poaceae - microbiology Poaceae - parasitology Recombinant DNA Sequence Analysis Substrate Specificity Substrates Temperature Xylose |
| title | Isolation and biochemical characterization of a glucose dehydrogenase from a hay infusion metagenome |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-22T09%3A39%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Isolation%20and%20biochemical%20characterization%20of%20a%20glucose%20dehydrogenase%20from%20a%20hay%20infusion%20metagenome&rft.jtitle=PloS%20one&rft.au=Basner,%20Alexander&rft.date=2014-01-14&rft.volume=9&rft.issue=1&rft.spage=e85844&rft.epage=e85844&rft.pages=e85844-e85844&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0085844&rft_dat=%3Cgale_plos_%3EA478865631%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1477433272&rft_id=info:pmid/24454935&rft_galeid=A478865631&rft_doaj_id=oai_doaj_org_article_64272fbe366c4633bc3a54747e36368d&rfr_iscdi=true |