High activity catechol 2,3-dioxygenase from the cresols – Degrading Stenotrophomonas maltophilia strain KB2
This study aimed at characterization of catechol 2,3-dioxygenase from Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentra...
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| Veröffentlicht in: | International biodeterioration & biodegradation 2011-09, Vol.65 (6), p.853-858 |
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| creator | Wojcieszyńska, Danuta Hupert-Kocurek, Katarzyna Greń, Izabela Guzik, Urszula |
| description | This study aimed at characterization of catechol 2,3-dioxygenase from
Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentration 6 mM, 7 mM, and 5 mM, respectively. When cells of strain KB2 were growing on methylphenols, catechol 2,3-dioxygenase was induced. Biochemical analysis revealed that the examined enzyme was similar to another catechol 2,3-dioxygenases, but showed extremely high activity. The enzyme was optimally active at 30 °C and pH 7.6. Kinetic studies showed that the value of
K
m
,
V
max and Hill constant was 85.11 μM, 3.08 μM min
−1 and 4.09 respectively. Comparative structural and phylogenetic analysis of catechol 2,3-dioxygenase from
S. maltophilia KB2 had placed the protein with the single-ring substrate subfamily of the extradiol dioxygenase. We observed the presence of externally located α-helices and internally located β-sheets. We also suggest that the Fe
2+ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water.
► Ability to degradation of all cresols by KB2 strain was reported. ► 3-D structure of catechol 2,3-dioxygenase (C23D) from KB2 strain was presented. ► C23D belongs to single-ring substrate subfamily of the extradiol dioxygenase. ► C23D is similar to the other ones, but with extremely high activity. |
| doi_str_mv | 10.1016/j.ibiod.2011.06.006 |
| format | Article |
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Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentration 6 mM, 7 mM, and 5 mM, respectively. When cells of strain KB2 were growing on methylphenols, catechol 2,3-dioxygenase was induced. Biochemical analysis revealed that the examined enzyme was similar to another catechol 2,3-dioxygenases, but showed extremely high activity. The enzyme was optimally active at 30 °C and pH 7.6. Kinetic studies showed that the value of
K
m
,
V
max and Hill constant was 85.11 μM, 3.08 μM min
−1 and 4.09 respectively. Comparative structural and phylogenetic analysis of catechol 2,3-dioxygenase from
S. maltophilia KB2 had placed the protein with the single-ring substrate subfamily of the extradiol dioxygenase. We observed the presence of externally located α-helices and internally located β-sheets. We also suggest that the Fe
2+ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water.
► Ability to degradation of all cresols by KB2 strain was reported. ► 3-D structure of catechol 2,3-dioxygenase (C23D) from KB2 strain was presented. ► C23D belongs to single-ring substrate subfamily of the extradiol dioxygenase. ► C23D is similar to the other ones, but with extremely high activity.</description><identifier>ISSN: 0964-8305</identifier><identifier>EISSN: 1879-0208</identifier><identifier>DOI: 10.1016/j.ibiod.2011.06.006</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Aromatic compounds ; Binding ; Biodegradation ; Carbon ; Catechol ; cresols ; Degradation ; Dioxygenases ; energy ; Enzymes ; glutamic acid ; histidine ; iron ; ligands ; phylogeny ; Residues ; Sole ; Stenotrophomonas ; Stenotrophomonas maltophilia ; Strain</subject><ispartof>International biodeterioration & biodegradation, 2011-09, Vol.65 (6), p.853-858</ispartof><rights>2011 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-d543eee95a4be7dbf09e4dfa9d6867587133b5027e84ea8193f104227324049e3</citedby><cites>FETCH-LOGICAL-c392t-d543eee95a4be7dbf09e4dfa9d6867587133b5027e84ea8193f104227324049e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0964830511001314$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Wojcieszyńska, Danuta</creatorcontrib><creatorcontrib>Hupert-Kocurek, Katarzyna</creatorcontrib><creatorcontrib>Greń, Izabela</creatorcontrib><creatorcontrib>Guzik, Urszula</creatorcontrib><title>High activity catechol 2,3-dioxygenase from the cresols – Degrading Stenotrophomonas maltophilia strain KB2</title><title>International biodeterioration & biodegradation</title><description>This study aimed at characterization of catechol 2,3-dioxygenase from
Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentration 6 mM, 7 mM, and 5 mM, respectively. When cells of strain KB2 were growing on methylphenols, catechol 2,3-dioxygenase was induced. Biochemical analysis revealed that the examined enzyme was similar to another catechol 2,3-dioxygenases, but showed extremely high activity. The enzyme was optimally active at 30 °C and pH 7.6. Kinetic studies showed that the value of
K
m
,
V
max and Hill constant was 85.11 μM, 3.08 μM min
−1 and 4.09 respectively. Comparative structural and phylogenetic analysis of catechol 2,3-dioxygenase from
S. maltophilia KB2 had placed the protein with the single-ring substrate subfamily of the extradiol dioxygenase. We observed the presence of externally located α-helices and internally located β-sheets. We also suggest that the Fe
2+ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water.
► Ability to degradation of all cresols by KB2 strain was reported. ► 3-D structure of catechol 2,3-dioxygenase (C23D) from KB2 strain was presented. ► C23D belongs to single-ring substrate subfamily of the extradiol dioxygenase. ► C23D is similar to the other ones, but with extremely high activity.</description><subject>Aromatic compounds</subject><subject>Binding</subject><subject>Biodegradation</subject><subject>Carbon</subject><subject>Catechol</subject><subject>cresols</subject><subject>Degradation</subject><subject>Dioxygenases</subject><subject>energy</subject><subject>Enzymes</subject><subject>glutamic acid</subject><subject>histidine</subject><subject>iron</subject><subject>ligands</subject><subject>phylogeny</subject><subject>Residues</subject><subject>Sole</subject><subject>Stenotrophomonas</subject><subject>Stenotrophomonas maltophilia</subject><subject>Strain</subject><issn>0964-8305</issn><issn>1879-0208</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kb9uFDEQhy0EEkfgCShwBwW7jO1d21tQQPgTRCSKkNry2bN7Pu2uD9uJuI534A15EhyOOtVopO_3G2k-Qp4zaBkw-Wbfhm2IvuXAWAuyBZAPyIZpNTTAQT8kGxhk12gB_WPyJOc9ALBesw1ZLsK0o9aVcBvKkTpb0O3iTPlr0fgQfx4nXG1GOqa40LJD6hLmOGf659dv-gGnZH1YJ3pVcI0lxcMuLrEG6GLnUrcwB0tzSTas9Ot7_pQ8Gu2c8dn_eUauP338fn7RXH77_OX83WXjxMBL4_tOIOLQ226Lym9HGLDzox281FL1WjEhtj1whbpDq9kgRgYd50rwDroBxRl5eeo9pPjjBnMxS8gO59muGG-y0Voz1vcMKvnqXpIpBYJrJVVFxQl1KeaccDSHFBabjoaBudNg9uafBnOnwYA0VUNNvTilRhuNnVLI5vqqArIqkJxJXom3JwLrR24DJpNdwNWhDwldMT6Gey_8Bal7m48</recordid><startdate>20110901</startdate><enddate>20110901</enddate><creator>Wojcieszyńska, Danuta</creator><creator>Hupert-Kocurek, Katarzyna</creator><creator>Greń, Izabela</creator><creator>Guzik, Urszula</creator><general>Elsevier Ltd</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SE</scope><scope>7SR</scope><scope>8FD</scope><scope>JG9</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20110901</creationdate><title>High activity catechol 2,3-dioxygenase from the cresols – Degrading Stenotrophomonas maltophilia strain KB2</title><author>Wojcieszyńska, Danuta ; Hupert-Kocurek, Katarzyna ; Greń, Izabela ; Guzik, Urszula</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-d543eee95a4be7dbf09e4dfa9d6867587133b5027e84ea8193f104227324049e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Aromatic compounds</topic><topic>Binding</topic><topic>Biodegradation</topic><topic>Carbon</topic><topic>Catechol</topic><topic>cresols</topic><topic>Degradation</topic><topic>Dioxygenases</topic><topic>energy</topic><topic>Enzymes</topic><topic>glutamic acid</topic><topic>histidine</topic><topic>iron</topic><topic>ligands</topic><topic>phylogeny</topic><topic>Residues</topic><topic>Sole</topic><topic>Stenotrophomonas</topic><topic>Stenotrophomonas maltophilia</topic><topic>Strain</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wojcieszyńska, Danuta</creatorcontrib><creatorcontrib>Hupert-Kocurek, Katarzyna</creatorcontrib><creatorcontrib>Greń, Izabela</creatorcontrib><creatorcontrib>Guzik, Urszula</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>Corrosion Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>International biodeterioration & biodegradation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wojcieszyńska, Danuta</au><au>Hupert-Kocurek, Katarzyna</au><au>Greń, Izabela</au><au>Guzik, Urszula</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High activity catechol 2,3-dioxygenase from the cresols – Degrading Stenotrophomonas maltophilia strain KB2</atitle><jtitle>International biodeterioration & biodegradation</jtitle><date>2011-09-01</date><risdate>2011</risdate><volume>65</volume><issue>6</issue><spage>853</spage><epage>858</epage><pages>853-858</pages><issn>0964-8305</issn><eissn>1879-0208</eissn><abstract>This study aimed at characterization of catechol 2,3-dioxygenase from
Stenotrophomonas maltophilia KB2, being able to utilize a wide spectrum of aromatic substrates as a sole carbon and energy source. 2-methylphenol, 3-methylphenol, and 4-methylphenol was completely degraded during 24 h in concentration 6 mM, 7 mM, and 5 mM, respectively. When cells of strain KB2 were growing on methylphenols, catechol 2,3-dioxygenase was induced. Biochemical analysis revealed that the examined enzyme was similar to another catechol 2,3-dioxygenases, but showed extremely high activity. The enzyme was optimally active at 30 °C and pH 7.6. Kinetic studies showed that the value of
K
m
,
V
max and Hill constant was 85.11 μM, 3.08 μM min
−1 and 4.09 respectively. Comparative structural and phylogenetic analysis of catechol 2,3-dioxygenase from
S. maltophilia KB2 had placed the protein with the single-ring substrate subfamily of the extradiol dioxygenase. We observed the presence of externally located α-helices and internally located β-sheets. We also suggest that the Fe
2+ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water.
► Ability to degradation of all cresols by KB2 strain was reported. ► 3-D structure of catechol 2,3-dioxygenase (C23D) from KB2 strain was presented. ► C23D belongs to single-ring substrate subfamily of the extradiol dioxygenase. ► C23D is similar to the other ones, but with extremely high activity.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.ibiod.2011.06.006</doi><tpages>6</tpages></addata></record> |
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| subjects | Aromatic compounds Binding Biodegradation Carbon Catechol cresols Degradation Dioxygenases energy Enzymes glutamic acid histidine iron ligands phylogeny Residues Sole Stenotrophomonas Stenotrophomonas maltophilia Strain |
| title | High activity catechol 2,3-dioxygenase from the cresols – Degrading Stenotrophomonas maltophilia strain KB2 |
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