The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1
Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal st...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2007-01, Vol.352 (4), p.861-866 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 866 |
|---|---|
| container_issue | 4 |
| container_start_page | 861 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 352 |
| creator | Jakoncic, Jean Jouanneau, Yves Meyer, Christine Stojanoff, Vivian |
| description | Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from
Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme. |
| doi_str_mv | 10.1016/j.bbrc.2006.11.117 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1820764</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X06025630</els_id><sourcerecordid>19533541</sourcerecordid><originalsourceid>FETCH-LOGICAL-c576t-6c1c3683e43f21d4b37e31fc6d57451657902cfb2b877a49d7d5341f09caf213</originalsourceid><addsrcrecordid>eNqFUV2r1DAQDaJ416t_wAepL751zSRt0oAIsqhXuCDoPuhTSNPpNmvbrEn24v57U3bx40VhIJmZc05mcgh5CnQNFMTL_bptg10zSsUaIIe8R1ZAFS0Z0Oo-WdHcKZmCL1fkUYx7SgEqoR6SK5BQywbUinzaDlhYk8x4Ss4WB2-_YSp8X6RcD27elcOpC_7HaTQpZ0Xn8n2Hs4lY9MFPxefDkOt-8rlUbG6-lvCYPOjNGPHJ5bwm23dvt5ub8vbj-w-bN7elraVIpbBguWg4Vrxn0FUtl8iht6KrZVWDqKWizPYtaxspTaU62dW8gp4qazKBX5PXZ9nDsZ2wszinYEZ9CG4y4aS9cfrvzuwGvfN3GhpGpaiywPOzgI_J6WhdQjtYP89ok1acghQZ8-LySPDfjxiTnly0OI5mRn-MOs_f1Ew1_wWCqjmvq2Vsdgba4GMM2P-aGKhebNV7vdiqF1s1QA6ZSc_-3PU35eJjBrw6AzB_-J3DsOyDs8XOhWWdzrt_6f8EXjy0Mg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19533541</pqid></control><display><type>article</type><title>The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Jakoncic, Jean ; Jouanneau, Yves ; Meyer, Christine ; Stojanoff, Vivian</creator><creatorcontrib>Jakoncic, Jean ; Jouanneau, Yves ; Meyer, Christine ; Stojanoff, Vivian ; Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><description>Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from
Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.11.117</identifier><identifier>PMID: 17157819</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>BASIC BIOLOGICAL SCIENCES ; Binding Sites ; Bioremediation ; Catalytic Domain ; CATALYTIC EFFECTS ; Dioxygenase ; Dioxygenases - chemistry ; Dioxygenases - genetics ; Dioxygenases - metabolism ; High molecular weight polycyclic aromatic hydrocarbons ; HYDROXYLATION ; MICROORGANISMS ; Models, Molecular ; Mononuclear iron ; national synchrotron light source ; OXYGENASES ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Sphingomonas ; Sphingomonas - enzymology ; Sphingomonas - genetics ; Substrate Specificity</subject><ispartof>Biochemical and biophysical research communications, 2007-01, Vol.352 (4), p.861-866</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-6c1c3683e43f21d4b37e31fc6d57451657902cfb2b877a49d7d5341f09caf213</citedby><cites>FETCH-LOGICAL-c576t-6c1c3683e43f21d4b37e31fc6d57451657902cfb2b877a49d7d5341f09caf213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2006.11.117$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17157819$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/930176$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Jakoncic, Jean</creatorcontrib><creatorcontrib>Jouanneau, Yves</creatorcontrib><creatorcontrib>Meyer, Christine</creatorcontrib><creatorcontrib>Stojanoff, Vivian</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><title>The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from
Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.</description><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding Sites</subject><subject>Bioremediation</subject><subject>Catalytic Domain</subject><subject>CATALYTIC EFFECTS</subject><subject>Dioxygenase</subject><subject>Dioxygenases - chemistry</subject><subject>Dioxygenases - genetics</subject><subject>Dioxygenases - metabolism</subject><subject>High molecular weight polycyclic aromatic hydrocarbons</subject><subject>HYDROXYLATION</subject><subject>MICROORGANISMS</subject><subject>Models, Molecular</subject><subject>Mononuclear iron</subject><subject>national synchrotron light source</subject><subject>OXYGENASES</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Sphingomonas</subject><subject>Sphingomonas - enzymology</subject><subject>Sphingomonas - genetics</subject><subject>Substrate Specificity</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV2r1DAQDaJ416t_wAepL751zSRt0oAIsqhXuCDoPuhTSNPpNmvbrEn24v57U3bx40VhIJmZc05mcgh5CnQNFMTL_bptg10zSsUaIIe8R1ZAFS0Z0Oo-WdHcKZmCL1fkUYx7SgEqoR6SK5BQywbUinzaDlhYk8x4Ss4WB2-_YSp8X6RcD27elcOpC_7HaTQpZ0Xn8n2Hs4lY9MFPxefDkOt-8rlUbG6-lvCYPOjNGPHJ5bwm23dvt5ub8vbj-w-bN7elraVIpbBguWg4Vrxn0FUtl8iht6KrZVWDqKWizPYtaxspTaU62dW8gp4qazKBX5PXZ9nDsZ2wszinYEZ9CG4y4aS9cfrvzuwGvfN3GhpGpaiywPOzgI_J6WhdQjtYP89ok1acghQZ8-LySPDfjxiTnly0OI5mRn-MOs_f1Ew1_wWCqjmvq2Vsdgba4GMM2P-aGKhebNV7vdiqF1s1QA6ZSc_-3PU35eJjBrw6AzB_-J3DsOyDs8XOhWWdzrt_6f8EXjy0Mg</recordid><startdate>20070126</startdate><enddate>20070126</enddate><creator>Jakoncic, Jean</creator><creator>Jouanneau, Yves</creator><creator>Meyer, Christine</creator><creator>Stojanoff, Vivian</creator><general>Elsevier Inc</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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20070126</creationdate><title>The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1</title><author>Jakoncic, Jean ; Jouanneau, Yves ; Meyer, Christine ; Stojanoff, Vivian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c576t-6c1c3683e43f21d4b37e31fc6d57451657902cfb2b877a49d7d5341f09caf213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding Sites</topic><topic>Bioremediation</topic><topic>Catalytic Domain</topic><topic>CATALYTIC EFFECTS</topic><topic>Dioxygenase</topic><topic>Dioxygenases - chemistry</topic><topic>Dioxygenases - genetics</topic><topic>Dioxygenases - metabolism</topic><topic>High molecular weight polycyclic aromatic hydrocarbons</topic><topic>HYDROXYLATION</topic><topic>MICROORGANISMS</topic><topic>Models, Molecular</topic><topic>Mononuclear iron</topic><topic>national synchrotron light source</topic><topic>OXYGENASES</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Sphingomonas</topic><topic>Sphingomonas - enzymology</topic><topic>Sphingomonas - genetics</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jakoncic, Jean</creatorcontrib><creatorcontrib>Jouanneau, Yves</creatorcontrib><creatorcontrib>Meyer, Christine</creatorcontrib><creatorcontrib>Stojanoff, Vivian</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jakoncic, Jean</au><au>Jouanneau, Yves</au><au>Meyer, Christine</au><au>Stojanoff, Vivian</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-01-26</date><risdate>2007</risdate><volume>352</volume><issue>4</issue><spage>861</spage><epage>866</epage><pages>861-866</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from
Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17157819</pmid><doi>10.1016/j.bbrc.2006.11.117</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2007-01, Vol.352 (4), p.861-866 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1820764 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | BASIC BIOLOGICAL SCIENCES Binding Sites Bioremediation Catalytic Domain CATALYTIC EFFECTS Dioxygenase Dioxygenases - chemistry Dioxygenases - genetics Dioxygenases - metabolism High molecular weight polycyclic aromatic hydrocarbons HYDROXYLATION MICROORGANISMS Models, Molecular Mononuclear iron national synchrotron light source OXYGENASES Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Sphingomonas Sphingomonas - enzymology Sphingomonas - genetics Substrate Specificity |
| title | The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T04%3A06%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20catalytic%20pocket%20of%20the%20ring-hydroxylating%20dioxygenase%20from%20Sphingomonas%20CHY-1&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Jakoncic,%20Jean&rft.aucorp=Brookhaven%20National%20Laboratory%20(BNL)%20National%20Synchrotron%20Light%20Source&rft.date=2007-01-26&rft.volume=352&rft.issue=4&rft.spage=861&rft.epage=866&rft.pages=861-866&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2006.11.117&rft_dat=%3Cproquest_pubme%3E19533541%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19533541&rft_id=info:pmid/17157819&rft_els_id=S0006291X06025630&rfr_iscdi=true |