{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/19956"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/19956","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Purification and characterization of methyl chloride transferase: A novel halogenating enzyme","abstract":"Methyl Chloride is biologically produced at an annual global emission rate of $5\\times10\\sp6$ tons. Production of this molecule is thought to be mostly biological in nature. The established route for production of halometabolites is the hydrogen peroxide-dependent halogenation mechanism common to haloperoxidase enzymes such as chloroperoxidase. No production of monohalomethanes can be detected by the haloperoxidase mechanism. The white rot fungus, Phellinus pomaceus has been known to produce methyl chloride in vivo. After determining appropriate growth conditions for optimal methyl chloride production, we have partially purified an enzyme from this fungus which produces methyl chloride. This enzyme utilizes S-adenosyl methionine (SAM) as a methyl donor in a methyl transferase reaction in which chloride, bromide and iodide are all methyl acceptors.","abstract_html":"Methyl Chloride is biologically produced at an annual global emission rate of $5\\times10\\sp6$ tons. Production of this molecule is thought to be mostly biological in nature. The established route for production of halometabolites is the hydrogen peroxide-dependent halogenation mechanism common to haloperoxidase enzymes such as chloroperoxidase. No production of monohalomethanes can be detected by the haloperoxidase mechanism. The white rot fungus, Phellinus pomaceus has been known to produce methyl chloride in vivo. After determining appropriate growth conditions for optimal methyl chloride production, we have partially purified an enzyme from this fungus which produces methyl chloride. This enzyme utilizes S-adenosyl methionine (SAM) as a methyl donor in a methyl transferase reaction in which chloride, bromide and iodide are all methyl acceptors.","abstract_has_math":true,"creators":["Wuosmaa, Annemarie"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Hager, Lowell P."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:24:06Z","date_published":"2011-05-07T12:24:06Z","updated_at":"2026-07-22T22:25:15Z","subjects":["Chemistry, Biochemistry"],"languages":["eng"],"rights":["Copyright 1994 Wuosmaa, Annemarie"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512602","(UMI)AAI9512602"],"render_values":[{"text":"AAI9512602","href":null,"code":true},{"text":"(UMI)AAI9512602","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/19956","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Hager, Lowell P."]},{"key":"dc:creator","label":"Author","values":["Wuosmaa, Annemarie"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:24:06Z","10000-01-01","1994"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1994 Wuosmaa, Annemarie"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512602","(UMI)AAI9512602","http://hdl.handle.net/2142/19956"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Methyl Chloride is biologically produced at an annual global emission rate of $5\\times10\\sp6$ tons. Production of this molecule is thought to be mostly biological in nature. The established route for production of halometabolites is the hydrogen peroxide-dependent halogenation mechanism common to haloperoxidase enzymes such as chloroperoxidase. No production of monohalomethanes can be detected by the haloperoxidase mechanism. The white rot fungus, Phellinus pomaceus has been known to produce methyl chloride in vivo. After determining appropriate growth conditions for optimal methyl chloride production, we have partially purified an enzyme from this fungus which produces methyl chloride. This enzyme utilizes S-adenosyl methionine (SAM) as a methyl donor in a methyl transferase reaction in which chloride, bromide and iodide are all methyl acceptors.","A survey of marine algae detected in vivo methyl chloride production by 20 of 31 algae species collected. Subsequently, in vitro production of methyl iodide was studied in five of these species. In all species studied, the reaction occurred by the methylation route described in the fungus. The enzyme has been purified from one algae species, Endocladia muricata. The enzyme from this source has a Km for bromide of, 40 mMolar, for chloride, 4 mMolar and for SAM 16 $\\mu$Molar. The pH maximum for the enzyme from this source is 7.6.","Methyl chloride transferase activity was also detected in the halophytic plant, Batis maritima. The enzyme from this plant can be induced by salt stress and has been purified to homogeneity. We hope to clone the gene for this enzyme and further study its possible role in salt tolerance.","Made available in DSpace on 2011-05-07T12:24:06Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9512602.pdf: 3158549 bytes, checksum: b916a644e88697757678325bd0eec933 (MD5) Previous issue date: 1994","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:40:34Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:17:25-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["Purification and characterization of methyl chloride transferase: A novel halogenating enzyme"]}]}],"canonical_facts":{"dc:contributor":["Hager, Lowell P."],"dc:creator":["Wuosmaa, Annemarie"],"dc:date":["2011-05-07T12:24:06Z","10000-01-01","1994"],"dc:description":["Methyl Chloride is biologically produced at an annual global emission rate of $5\\times10\\sp6$ tons. Production of this molecule is thought to be mostly biological in nature. The established route for production of halometabolites is the hydrogen peroxide-dependent halogenation mechanism common to haloperoxidase enzymes such as chloroperoxidase. No production of monohalomethanes can be detected by the haloperoxidase mechanism. The white rot fungus, Phellinus pomaceus has been known to produce methyl chloride in vivo. After determining appropriate growth conditions for optimal methyl chloride production, we have partially purified an enzyme from this fungus which produces methyl chloride. This enzyme utilizes S-adenosyl methionine (SAM) as a methyl donor in a methyl transferase reaction in which chloride, bromide and iodide are all methyl acceptors.","A survey of marine algae detected in vivo methyl chloride production by 20 of 31 algae species collected. Subsequently, in vitro production of methyl iodide was studied in five of these species. In all species studied, the reaction occurred by the methylation route described in the fungus. The enzyme has been purified from one algae species, Endocladia muricata. The enzyme from this source has a Km for bromide of, 40 mMolar, for chloride, 4 mMolar and for SAM 16 $\\mu$Molar. The pH maximum for the enzyme from this source is 7.6.","Methyl chloride transferase activity was also detected in the halophytic plant, Batis maritima. The enzyme from this plant can be induced by salt stress and has been purified to homogeneity. We hope to clone the gene for this enzyme and further study its possible role in salt tolerance.","Made available in DSpace on 2011-05-07T12:24:06Z (GMT). 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