Isolation and characterization of a novel nonheme chloroperoxidase
Chloroperoxidase, purified from the fermentation of Curvularia inaequalis , had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (M r 66,000). The enzyme was specific for I −, Br − and Cl −, and inactive toward F −. The optimum pH of the enzyme...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1987-01, Vol.142 (2), p.329-333 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Ernie Liu, Te-Ning M'Timkulu, Thabiso Geigert, John Wolf, Beverly Neidleman, Saul L. Silva, Deborah Hunter-Cevera, Jennie C. |
| description | Chloroperoxidase, purified from the fermentation of
Curvularia
inaequalis
, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (M
r 66,000). The enzyme was specific for I
−, Br
− and Cl
−, and inactive toward F
−. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no hemelike compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable. |
| doi_str_mv | 10.1016/0006-291X(87)90277-4 |
| format | Article |
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Curvularia
inaequalis
, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (M
r 66,000). The enzyme was specific for I
−, Br
− and Cl
−, and inactive toward F
−. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no hemelike compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(87)90277-4</identifier><identifier>PMID: 3814138</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Applied sciences ; Chloride Peroxidase - analysis ; Chloride Peroxidase - isolation & purification ; chloroperoxidase ; Curvularia inaequalis ; Exact sciences and technology ; Heme - analysis ; Mitosporic Fungi - enzymology ; Other techniques and industries ; Peroxidases - isolation & purification</subject><ispartof>Biochemical and biophysical research communications, 1987-01, Vol.142 (2), p.329-333</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-8402bebd8393d84d698f1a9db1827f3df0d546dc9f32e823a34bfb5143b86abe3</citedby><cites>FETCH-LOGICAL-c417t-8402bebd8393d84d698f1a9db1827f3df0d546dc9f32e823a34bfb5143b86abe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X87902774$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7528946$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3814138$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ernie Liu, Te-Ning</creatorcontrib><creatorcontrib>M'Timkulu, Thabiso</creatorcontrib><creatorcontrib>Geigert, John</creatorcontrib><creatorcontrib>Wolf, Beverly</creatorcontrib><creatorcontrib>Neidleman, Saul L.</creatorcontrib><creatorcontrib>Silva, Deborah</creatorcontrib><creatorcontrib>Hunter-Cevera, Jennie C.</creatorcontrib><title>Isolation and characterization of a novel nonheme chloroperoxidase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Chloroperoxidase, purified from the fermentation of
Curvularia
inaequalis
, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (M
r 66,000). The enzyme was specific for I
−, Br
− and Cl
−, and inactive toward F
−. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no hemelike compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable.</description><subject>Applied sciences</subject><subject>Chloride Peroxidase - analysis</subject><subject>Chloride Peroxidase - isolation & purification</subject><subject>chloroperoxidase</subject><subject>Curvularia inaequalis</subject><subject>Exact sciences and technology</subject><subject>Heme - analysis</subject><subject>Mitosporic Fungi - enzymology</subject><subject>Other techniques and industries</subject><subject>Peroxidases - isolation & purification</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rGzEQQEVJcByn_6ABH0JJD5toVvJKugRa0w-DIZcEehNaaURU1itHWps0v75ybXxMLjMw82aYeYR8AnoDFJpbSmlT1Qp-X0vxRdFaiIp_IGOgilY1UH5CxkfkjJzn_IdSAN6oERkxCRyYHJNvixw7M4TYT03vpvbJJGMHTOF1X4x-aqZ93GJXYv-EKyxMF1NcY4ovwZmMF-TUmy7jx0OekMcf3x_mv6rl_c_F_OuyshzEUElO6xZbJ5liTnLXKOnBKNeCrIVnzlM3442zyrMaZc0M461vZ8BZKxvTIpuQz_u96xSfN5gHvQrZYteZHuMmayGYlKyh74LFAZTnoYB8D9oUc07o9TqFlUl_NVC9c6x3AvVOoJZC_3eseRm7POzftCt0x6GD1NK_OvRNtqbzyfQ25CMmZrVUvCnY3R7DIm0bMOlsA_YWXUhoB-1iePuOf6SymDk</recordid><startdate>19870130</startdate><enddate>19870130</enddate><creator>Ernie Liu, Te-Ning</creator><creator>M'Timkulu, Thabiso</creator><creator>Geigert, John</creator><creator>Wolf, Beverly</creator><creator>Neidleman, Saul L.</creator><creator>Silva, Deborah</creator><creator>Hunter-Cevera, Jennie C.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>M7N</scope><scope>7X8</scope></search><sort><creationdate>19870130</creationdate><title>Isolation and characterization of a novel nonheme chloroperoxidase</title><author>Ernie Liu, Te-Ning ; M'Timkulu, Thabiso ; Geigert, John ; Wolf, Beverly ; Neidleman, Saul L. ; Silva, Deborah ; Hunter-Cevera, Jennie C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-8402bebd8393d84d698f1a9db1827f3df0d546dc9f32e823a34bfb5143b86abe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Applied sciences</topic><topic>Chloride Peroxidase - analysis</topic><topic>Chloride Peroxidase - isolation & purification</topic><topic>chloroperoxidase</topic><topic>Curvularia inaequalis</topic><topic>Exact sciences and technology</topic><topic>Heme - analysis</topic><topic>Mitosporic Fungi - enzymology</topic><topic>Other techniques and industries</topic><topic>Peroxidases - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ernie Liu, Te-Ning</creatorcontrib><creatorcontrib>M'Timkulu, Thabiso</creatorcontrib><creatorcontrib>Geigert, John</creatorcontrib><creatorcontrib>Wolf, Beverly</creatorcontrib><creatorcontrib>Neidleman, Saul L.</creatorcontrib><creatorcontrib>Silva, Deborah</creatorcontrib><creatorcontrib>Hunter-Cevera, Jennie C.</creatorcontrib><collection>Pascal-Francis</collection><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ernie Liu, Te-Ning</au><au>M'Timkulu, Thabiso</au><au>Geigert, John</au><au>Wolf, Beverly</au><au>Neidleman, Saul L.</au><au>Silva, Deborah</au><au>Hunter-Cevera, Jennie C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of a novel nonheme chloroperoxidase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1987-01-30</date><risdate>1987</risdate><volume>142</volume><issue>2</issue><spage>329</spage><epage>333</epage><pages>329-333</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Chloroperoxidase, purified from the fermentation of
Curvularia
inaequalis
, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (M
r 66,000). The enzyme was specific for I
−, Br
− and Cl
−, and inactive toward F
−. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no hemelike compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3814138</pmid><doi>10.1016/0006-291X(87)90277-4</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1987-01, Vol.142 (2), p.329-333 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Applied sciences Chloride Peroxidase - analysis Chloride Peroxidase - isolation & purification chloroperoxidase Curvularia inaequalis Exact sciences and technology Heme - analysis Mitosporic Fungi - enzymology Other techniques and industries Peroxidases - isolation & purification |
| title | Isolation and characterization of a novel nonheme chloroperoxidase |
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