Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans
Catalase plays a key role in protecting cells against toxic reactive oxygen species. Here we report on the cloning, purification and characterization of a catalase (KatA, DR1998) from the extremely radioresistant bacterium Deinococcus radiodurans. The size of purified D. radiodurans KatA monomer was...
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| Veröffentlicht in: | Journal of bioscience and bioengineering 2006-04, Vol.101 (4), p.315-321 |
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| creator | Kobayashi, Issei Tamura, Takashi Sghaier, Haitham Narumi, Issay Yamaguchi, Shotaro Umeda, Koichi Inagaki, Kenji |
| description | Catalase plays a key role in protecting cells against toxic reactive oxygen species. Here we report on the cloning, purification and characterization of a catalase (KatA, DR1998) from the extremely radioresistant bacterium
Deinococcus radiodurans. The size of purified
D. radiodurans KatA monomer was 65 kDa while gel filtration revealed that the size of the enzyme was 240 kDa, suggesting that KatA formed a homotetramer in solution. Purified KatA displayed a final specific activity of 68,800 U/mg of protein. The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole. The absorption spectrum of KatA exhibited a Soret band at 408 nm. The position of the spectral peak remained unchanged following reduction of KatA with dithionite. No peroxidase activity was found for KatA. These results demonstrate that
D. radiodurans KatA is a typical monofunctional heme-containing catalase. The stability of KatA with respect to H
2O
2 stress was superior to that of commercially available
Aspergillus niger and bovine liver catalases. The relative abundance of KatA in cells in addition to the H
2O
2 resistance property may play a role in the survival strategy of
D. radiodurans against oxidative damage. |
| doi_str_mv | 10.1263/jbb.101.315 |
| format | Article |
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Deinococcus radiodurans. The size of purified
D. radiodurans KatA monomer was 65 kDa while gel filtration revealed that the size of the enzyme was 240 kDa, suggesting that KatA formed a homotetramer in solution. Purified KatA displayed a final specific activity of 68,800 U/mg of protein. The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole. The absorption spectrum of KatA exhibited a Soret band at 408 nm. The position of the spectral peak remained unchanged following reduction of KatA with dithionite. No peroxidase activity was found for KatA. These results demonstrate that
D. radiodurans KatA is a typical monofunctional heme-containing catalase. The stability of KatA with respect to H
2O
2 stress was superior to that of commercially available
Aspergillus niger and bovine liver catalases. The relative abundance of KatA in cells in addition to the H
2O
2 resistance property may play a role in the survival strategy of
D. radiodurans against oxidative damage.</description><identifier>ISSN: 1389-1723</identifier><identifier>EISSN: 1347-4421</identifier><identifier>DOI: 10.1263/jbb.101.315</identifier><identifier>PMID: 16716939</identifier><identifier>CODEN: JFBIEX</identifier><language>eng</language><publisher>Amsterdarm: Elsevier B.V</publisher><subject>Amino Acid Sequence ; antioxidant ; Aspergillus niger ; BACTERIA ; Biological and medical sciences ; Biotechnology ; CATALASA ; CATALASE ; Catalase - chemistry ; Chromatography, Gel ; Cloning, Molecular ; Deinococcus - enzymology ; Deinococcus radiodurans ; DNA, Bacterial - chemistry ; Escherichia coli - metabolism ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. Psychology ; GENE EXPRESSION ; HYDROGEN PEROXIDE ; Hydrogen Peroxide - chemistry ; hydrogen peroxide resistance ; Molecular Sequence Data ; PEROXIDO DE HIDROGENO ; PEROXYDE D'HYDROGENE ; Plasmids - metabolism ; Proteins - chemistry ; RADIOSENSIBILIDAD ; RADIOSENSIBILITE ; RADIOSENSITIVITY ; Sequence Homology, Amino Acid ; TOLERANCE ; TOLERANCIA</subject><ispartof>Journal of bioscience and bioengineering, 2006-04, Vol.101 (4), p.315-321</ispartof><rights>2006 The Society for Biotechnology, Japan</rights><rights>2006 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c535t-e45a0b56f8527e40404e2d9d6c66181c58cde908f0942c0787a743dee40aca9a3</citedby><cites>FETCH-LOGICAL-c535t-e45a0b56f8527e40404e2d9d6c66181c58cde908f0942c0787a743dee40aca9a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1389172306705874$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17732004$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16716939$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobayashi, Issei</creatorcontrib><creatorcontrib>Tamura, Takashi</creatorcontrib><creatorcontrib>Sghaier, Haitham</creatorcontrib><creatorcontrib>Narumi, Issay</creatorcontrib><creatorcontrib>Yamaguchi, Shotaro</creatorcontrib><creatorcontrib>Umeda, Koichi</creatorcontrib><creatorcontrib>Inagaki, Kenji</creatorcontrib><title>Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans</title><title>Journal of bioscience and bioengineering</title><addtitle>J Biosci Bioeng</addtitle><description>Catalase plays a key role in protecting cells against toxic reactive oxygen species. Here we report on the cloning, purification and characterization of a catalase (KatA, DR1998) from the extremely radioresistant bacterium
Deinococcus radiodurans. The size of purified
D. radiodurans KatA monomer was 65 kDa while gel filtration revealed that the size of the enzyme was 240 kDa, suggesting that KatA formed a homotetramer in solution. Purified KatA displayed a final specific activity of 68,800 U/mg of protein. The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole. The absorption spectrum of KatA exhibited a Soret band at 408 nm. The position of the spectral peak remained unchanged following reduction of KatA with dithionite. No peroxidase activity was found for KatA. These results demonstrate that
D. radiodurans KatA is a typical monofunctional heme-containing catalase. The stability of KatA with respect to H
2O
2 stress was superior to that of commercially available
Aspergillus niger and bovine liver catalases. The relative abundance of KatA in cells in addition to the H
2O
2 resistance property may play a role in the survival strategy of
D. radiodurans against oxidative damage.</description><subject>Amino Acid Sequence</subject><subject>antioxidant</subject><subject>Aspergillus niger</subject><subject>BACTERIA</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>CATALASA</subject><subject>CATALASE</subject><subject>Catalase - chemistry</subject><subject>Chromatography, Gel</subject><subject>Cloning, Molecular</subject><subject>Deinococcus - enzymology</subject><subject>Deinococcus radiodurans</subject><subject>DNA, Bacterial - chemistry</subject><subject>Escherichia coli - metabolism</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE EXPRESSION</subject><subject>HYDROGEN PEROXIDE</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>hydrogen peroxide resistance</subject><subject>Molecular Sequence Data</subject><subject>PEROXIDO DE HIDROGENO</subject><subject>PEROXYDE D'HYDROGENE</subject><subject>Plasmids - metabolism</subject><subject>Proteins - chemistry</subject><subject>RADIOSENSIBILIDAD</subject><subject>RADIOSENSIBILITE</subject><subject>RADIOSENSITIVITY</subject><subject>Sequence Homology, Amino Acid</subject><subject>TOLERANCE</subject><subject>TOLERANCIA</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0Mur1TAQB-AiivehK9dKQa4b6TGTR9MuL8e3F3Sh6zBNJ5pD21yTVNC_3hx64IJIFpkwH8PkV1VPgO2At-LVYRh2wGAnQN2rzkFI3UjJ4f6x7voGNBdn1UVKB8ZAMw0PqzNoNbS96M8rt_-BEW2m6P9g9mGpg6vnsAS3Lvb4xqm2mHHCRPUnzNe1i2GuI44-REo-ZVxyPWwT1rl-TX4JNli7pg2Na8QlPaoeOJwSPT7dl9W3t2--7t83N5_ffdhf3zRWCZUbkgrZoFrXKa5JsnKIj_3Y2raFDqzq7Eg96xzrJbdMdxq1FCMVihZ7FJfVi23ubQw_V0rZzD5ZmiZcKKzJcMY1ZwoKfP4PPIQ1lt8mA1KCECBUV9TLTdkYUorkzG30M8bfBpg5hm9K-KUGU8Iv-tlp5jrMNN7ZU9oFXJ0AJouTK8lYn-6c1oIzJot7ujmHweD3WMzHL6WjGeNC8dJXW59KlL88RZOsp8XS6CPZbMbg_7vgX7mYqCg</recordid><startdate>20060401</startdate><enddate>20060401</enddate><creator>Kobayashi, Issei</creator><creator>Tamura, Takashi</creator><creator>Sghaier, Haitham</creator><creator>Narumi, Issay</creator><creator>Yamaguchi, Shotaro</creator><creator>Umeda, Koichi</creator><creator>Inagaki, Kenji</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier Limited</general><scope>FBQ</scope><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>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope></search><sort><creationdate>20060401</creationdate><title>Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans</title><author>Kobayashi, Issei ; Tamura, Takashi ; Sghaier, Haitham ; Narumi, Issay ; Yamaguchi, Shotaro ; Umeda, Koichi ; Inagaki, Kenji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c535t-e45a0b56f8527e40404e2d9d6c66181c58cde908f0942c0787a743dee40aca9a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>antioxidant</topic><topic>Aspergillus niger</topic><topic>BACTERIA</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>CATALASA</topic><topic>CATALASE</topic><topic>Catalase - chemistry</topic><topic>Chromatography, Gel</topic><topic>Cloning, Molecular</topic><topic>Deinococcus - enzymology</topic><topic>Deinococcus radiodurans</topic><topic>DNA, Bacterial - chemistry</topic><topic>Escherichia coli - metabolism</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE EXPRESSION</topic><topic>HYDROGEN PEROXIDE</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>hydrogen peroxide resistance</topic><topic>Molecular Sequence Data</topic><topic>PEROXIDO DE HIDROGENO</topic><topic>PEROXYDE D'HYDROGENE</topic><topic>Plasmids - metabolism</topic><topic>Proteins - chemistry</topic><topic>RADIOSENSIBILIDAD</topic><topic>RADIOSENSIBILITE</topic><topic>RADIOSENSITIVITY</topic><topic>Sequence Homology, Amino Acid</topic><topic>TOLERANCE</topic><topic>TOLERANCIA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobayashi, Issei</creatorcontrib><creatorcontrib>Tamura, Takashi</creatorcontrib><creatorcontrib>Sghaier, Haitham</creatorcontrib><creatorcontrib>Narumi, Issay</creatorcontrib><creatorcontrib>Yamaguchi, Shotaro</creatorcontrib><creatorcontrib>Umeda, Koichi</creatorcontrib><creatorcontrib>Inagaki, Kenji</creatorcontrib><collection>AGRIS</collection><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of bioscience and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kobayashi, Issei</au><au>Tamura, Takashi</au><au>Sghaier, Haitham</au><au>Narumi, Issay</au><au>Yamaguchi, Shotaro</au><au>Umeda, Koichi</au><au>Inagaki, Kenji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans</atitle><jtitle>Journal of bioscience and bioengineering</jtitle><addtitle>J Biosci Bioeng</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>101</volume><issue>4</issue><spage>315</spage><epage>321</epage><pages>315-321</pages><issn>1389-1723</issn><eissn>1347-4421</eissn><coden>JFBIEX</coden><abstract>Catalase plays a key role in protecting cells against toxic reactive oxygen species. Here we report on the cloning, purification and characterization of a catalase (KatA, DR1998) from the extremely radioresistant bacterium
Deinococcus radiodurans. The size of purified
D. radiodurans KatA monomer was 65 kDa while gel filtration revealed that the size of the enzyme was 240 kDa, suggesting that KatA formed a homotetramer in solution. Purified KatA displayed a final specific activity of 68,800 U/mg of protein. The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole. The absorption spectrum of KatA exhibited a Soret band at 408 nm. The position of the spectral peak remained unchanged following reduction of KatA with dithionite. No peroxidase activity was found for KatA. These results demonstrate that
D. radiodurans KatA is a typical monofunctional heme-containing catalase. The stability of KatA with respect to H
2O
2 stress was superior to that of commercially available
Aspergillus niger and bovine liver catalases. The relative abundance of KatA in cells in addition to the H
2O
2 resistance property may play a role in the survival strategy of
D. radiodurans against oxidative damage.</abstract><cop>Amsterdarm</cop><pub>Elsevier B.V</pub><pmid>16716939</pmid><doi>10.1263/jbb.101.315</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Journal of bioscience and bioengineering, 2006-04, Vol.101 (4), p.315-321 |
| issn | 1389-1723 1347-4421 |
| language | eng |
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| subjects | Amino Acid Sequence antioxidant Aspergillus niger BACTERIA Biological and medical sciences Biotechnology CATALASA CATALASE Catalase - chemistry Chromatography, Gel Cloning, Molecular Deinococcus - enzymology Deinococcus radiodurans DNA, Bacterial - chemistry Escherichia coli - metabolism EXPRESION GENICA EXPRESSION DES GENES Fundamental and applied biological sciences. Psychology GENE EXPRESSION HYDROGEN PEROXIDE Hydrogen Peroxide - chemistry hydrogen peroxide resistance Molecular Sequence Data PEROXIDO DE HIDROGENO PEROXYDE D'HYDROGENE Plasmids - metabolism Proteins - chemistry RADIOSENSIBILIDAD RADIOSENSIBILITE RADIOSENSITIVITY Sequence Homology, Amino Acid TOLERANCE TOLERANCIA |
| title | Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans |
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