Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations
An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring c...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998, Vol.62 (9), p.1830-1833 |
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container_title | Bioscience, biotechnology, and biochemistry |
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creator | Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) Jeong, E.Y Hwang, T.E Choi, S.H |
description | An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides |
doi_str_mv | 10.1271/bbb.62.1830 |
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CNU961 able to grow with phenol at high concentrations</title><source>Oxford University Press Journals All Titles (1996-Current)</source><source>J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese</source><source>Open Access Titles of Japan</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</creator><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</creatorcontrib><description>An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.62.1830</identifier><identifier>PMID: 27392693</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>ACINETOBACTER ; Acinetobacter sp ; Bacteriology ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; catechol production ; COMPOSE PHENOLIQUE ; COMPUESTOS FENOLICOS ; Fundamental and applied biological sciences. Psychology ; IDENTIFICACION ; IDENTIFICATION ; Metabolism. Enzymes ; Microbiology ; Mission oriented research ; ortho-pathway ; phenol hydroxylase ; phenol tolerance ; PHENOLIC COMPOUNDS ; Physiology and metabolism</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1998, Vol.62 (9), p.1830-1833</ispartof><rights>1998 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 1998</rights><rights>1999 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1998</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-19c9cfc16ea93a56ee1d35b4aab5b47b913648cf292e0d9291cb3dc0b22eac3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1664613$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27392693$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</creatorcontrib><creatorcontrib>Jeong, E.Y</creatorcontrib><creatorcontrib>Hwang, T.E</creatorcontrib><creatorcontrib>Choi, S.H</creatorcontrib><title>Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>An Acinetobacter sp., strain CNU961, with a higher tolerance to phenol was isolated, and identified through a set of taxonomic studies and a genetic complementation test. Enzymatic and mutagenic studies found that the strain dissimulate phenol by hydroxylation to catechol followed by an ortho-ring cleavage pathway to further mineralize it. The phenol hydroxylase, which is an inducible enzyme and requires NADPH for optimum activity, was not inhibited by phenol at concentrations up to 0.5 mM. The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</description><subject>ACINETOBACTER</subject><subject>Acinetobacter sp</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>catechol production</subject><subject>COMPOSE PHENOLIQUE</subject><subject>COMPUESTOS FENOLICOS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>IDENTIFICACION</subject><subject>IDENTIFICATION</subject><subject>Metabolism. Enzymes</subject><subject>Microbiology</subject><subject>Mission oriented research</subject><subject>ortho-pathway</subject><subject>phenol hydroxylase</subject><subject>phenol tolerance</subject><subject>PHENOLIC COMPOUNDS</subject><subject>Physiology and metabolism</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNp90cFrFDEUBvAgil2rJ89KQCmCzJo3yWYmx7JYrRQV1HN4yWR2U2aTbTLLUv96s52tgoiXBB6_fEn4CHkObA51A--MMXNZz6Hl7AGZARdNJZVoHpIZUyCrVizghDzJ-ZqxMljAY3JSN1zVUvEZiZedC6PvvcXRx0AxdNSuMaEdXfI_p2Hs6bn1wY3R3M1p3s7p8vMPJYGiGRwdI12luKd7P67pdu1CHCiOdO1Xa2pjsOWKdBeVn5JHPQ7ZPTvup-Tbxfvvy4_V1ZcPl8vzq8oKIccKlFW2tyAdKo4L6Rx0fGEEoilrYxRwKVrb16p2rFO1Amt4Z5mpa4eWn5I3U-o2xZudy6Pe-GzdMGBwcZc1tIwL0ShQhZ79nzYlXLUH-OoveB13KZRPaBBCicJkU9TbSdkUc06u19vkN5huNTB9qEuXurSs9aGuol8eM3dm47rf9r6fAl4fAWaLQ58wWJ__ZEopJByYnJgPfUwb3Mc0dHrE2yGm-zP83w94MR3sMWpcpeI-fQWlFGPAmob_AldguEc</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Jeong, K.C. 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(Chonnam National Univ., Kwangju (Korea R.)) ; Jeong, E.Y ; Hwang, T.E ; Choi, S.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-19c9cfc16ea93a56ee1d35b4aab5b47b913648cf292e0d9291cb3dc0b22eac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACINETOBACTER</topic><topic>Acinetobacter sp</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>catechol production</topic><topic>COMPOSE PHENOLIQUE</topic><topic>COMPUESTOS FENOLICOS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>IDENTIFICACION</topic><topic>IDENTIFICATION</topic><topic>Metabolism. Enzymes</topic><topic>Microbiology</topic><topic>Mission oriented research</topic><topic>ortho-pathway</topic><topic>phenol hydroxylase</topic><topic>phenol tolerance</topic><topic>PHENOLIC COMPOUNDS</topic><topic>Physiology and metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</creatorcontrib><creatorcontrib>Jeong, E.Y</creatorcontrib><creatorcontrib>Hwang, T.E</creatorcontrib><creatorcontrib>Choi, S.H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jeong, K.C. (Chonnam National Univ., Kwangju (Korea R.))</au><au>Jeong, E.Y</au><au>Hwang, T.E</au><au>Choi, S.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of Acinetobacter sp. 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The different kinetic behaviors of the enzyme activities on NADPH and on phenol reflected that the phenol hydroxylase of strain CNU961 is a multisubunit allosteric enzyme consisting of heterogeneous polypeptides</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>27392693</pmid><doi>10.1271/bbb.62.1830</doi><tpages>4</tpages></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
subjects | ACINETOBACTER Acinetobacter sp Bacteriology Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology catechol production COMPOSE PHENOLIQUE COMPUESTOS FENOLICOS Fundamental and applied biological sciences. Psychology IDENTIFICACION IDENTIFICATION Metabolism. Enzymes Microbiology Mission oriented research ortho-pathway phenol hydroxylase phenol tolerance PHENOLIC COMPOUNDS Physiology and metabolism |
title | Identification and characterization of Acinetobacter sp. CNU961 able to grow with phenol at high concentrations |
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