Cloning and Expression of Gene Encoding a Novel Endoglycoceramidase of Rhodococcus sp. Strain C9
Endoglycoceramidase (EGCase) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. We previously reported that the Asn-Glu-Pro (NEP) sequence is part of the active site of EGCase of Rhodococcus sp. strain M-777. This paper descr...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2000-07, Vol.128 (1), p.145-152 |
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| creator | Sakaguchi, Keishi Okino, Nozomu Sueyoshi, Noriyuki Izu, Hiroyuki Ito, Makoto |
| description | Endoglycoceramidase (EGCase) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. We previously reported that the Asn-Glu-Pro (NEP) sequence is part of the active site of EGCase of Rhodococcus sp. strain M-777. This paper describes the molecular cloning of a new EGCase gene utilising the NEP sequence front the genomic library of Rhodococcus sp. strain C9, which was clearly distinguishable from M-777 by 16S rDNA analysis. C9 EGCase possessed an open reading frame of 1,446 bp encoding 482 amino acids, and showed 78% and 76% identity to M-777 EGCase II at the nucleotide and amino acid levels, respectively. Interestingly, C9 EGCase showed the different specificity to the M-777 enzyme: it hydrolyzed b-series gangliotetraosylceramides more slowly than the M-777 enzyme, whereas both enzymes hydrolyzed a-series gangliosides and neutral glycosphingolipids to the same extent |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a022725 |
| format | Article |
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C9 EGCase possessed an open reading frame of 1,446 bp encoding 482 amino acids, and showed 78% and 76% identity to M-777 EGCase II at the nucleotide and amino acid levels, respectively. Interestingly, C9 EGCase showed the different specificity to the M-777 enzyme: it hydrolyzed b-series gangliotetraosylceramides more slowly than the M-777 enzyme, whereas both enzymes hydrolyzed a-series gangliosides and neutral glycosphingolipids to the same extent</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a022725</identifier><identifier>PMID: 10876169</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Base Sequence ; Carbohydrate Sequence ; Cloning, Molecular ; endoglycoceramidase ; gangliosides ; Gangliosides - metabolism ; Gene Expression Regulation, Enzymologic ; Glycoside Hydrolases - genetics ; Glycoside Hydrolases - metabolism ; glycosphingolipids ; homology cloning ; Hydrogen-Ion Concentration ; Kinetics ; Molecular Sequence Data ; NEP sequence ; Rhodococcus - enzymology ; Rhodococcus - genetics ; Sequence Analysis ; Sequence Homology, Amino Acid ; Substrate Specificity</subject><ispartof>Journal of biochemistry (Tokyo), 2000-07, Vol.128 (1), p.145-152</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-1380b71ec2f4636282f9b3b743f2d5d721bb9e7bf6003a4d5b3be002546f9b8b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10876169$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sakaguchi, Keishi</creatorcontrib><creatorcontrib>Okino, Nozomu</creatorcontrib><creatorcontrib>Sueyoshi, Noriyuki</creatorcontrib><creatorcontrib>Izu, Hiroyuki</creatorcontrib><creatorcontrib>Ito, Makoto</creatorcontrib><title>Cloning and Expression of Gene Encoding a Novel Endoglycoceramidase of Rhodococcus sp. Strain C9</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Endoglycoceramidase (EGCase) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. We previously reported that the Asn-Glu-Pro (NEP) sequence is part of the active site of EGCase of Rhodococcus sp. strain M-777. This paper describes the molecular cloning of a new EGCase gene utilising the NEP sequence front the genomic library of Rhodococcus sp. strain C9, which was clearly distinguishable from M-777 by 16S rDNA analysis. C9 EGCase possessed an open reading frame of 1,446 bp encoding 482 amino acids, and showed 78% and 76% identity to M-777 EGCase II at the nucleotide and amino acid levels, respectively. Interestingly, C9 EGCase showed the different specificity to the M-777 enzyme: it hydrolyzed b-series gangliotetraosylceramides more slowly than the M-777 enzyme, whereas both enzymes hydrolyzed a-series gangliosides and neutral glycosphingolipids to the same extent</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Carbohydrate Sequence</subject><subject>Cloning, Molecular</subject><subject>endoglycoceramidase</subject><subject>gangliosides</subject><subject>Gangliosides - metabolism</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Glycoside Hydrolases - genetics</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>glycosphingolipids</subject><subject>homology cloning</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>NEP sequence</subject><subject>Rhodococcus - enzymology</subject><subject>Rhodococcus - genetics</subject><subject>Sequence Analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1P3DAQhn0oKrDtX6h8Kbcs_kji5NBDtVoWJETLlqqoF9cfE8iS2Iu9Qcu_x9usEJysmfcZ2_Mg9JWSKSU1P_Xbxge78kNwqovTlTb30E8VYUyw4gM6IoTRrGb57SE6jnG1KxnnH9EhJZUoaVkfoX-zzrvW3WHlLJ5v1wFibL3DvsELcIDnznj7P8dX_gm61LD-rns23kBQfWtVhB28vPfWp6YZIo7rKf61Cap1eFZ_QgdN-hx83p8T9PtsfjM7zy5_LC5m3y8zUzC-ySiviBYUDGvykpesYk2tuRY5b5gtrGBU6xqEbkpCuMptkUJICxV5mcBK8wk6Ge9dB_84QNzIvo0Guk458EOUgrKkpagS-G0ETfAxBmjkOrS9Cs-SErnTKt9rlaNWudea5r_sHxp0D_bN9Og0AdkItHED29dchQdZCi4KeX77V95c_zn7uSQLKfgLSQKNRQ</recordid><startdate>20000701</startdate><enddate>20000701</enddate><creator>Sakaguchi, Keishi</creator><creator>Okino, Nozomu</creator><creator>Sueyoshi, Noriyuki</creator><creator>Izu, Hiroyuki</creator><creator>Ito, Makoto</creator><general>Oxford University Press</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20000701</creationdate><title>Cloning and Expression of Gene Encoding a Novel Endoglycoceramidase of Rhodococcus sp. Strain C9</title><author>Sakaguchi, Keishi ; Okino, Nozomu ; Sueyoshi, Noriyuki ; Izu, Hiroyuki ; Ito, Makoto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-1380b71ec2f4636282f9b3b743f2d5d721bb9e7bf6003a4d5b3be002546f9b8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Carbohydrate Sequence</topic><topic>Cloning, Molecular</topic><topic>endoglycoceramidase</topic><topic>gangliosides</topic><topic>Gangliosides - metabolism</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Glycoside Hydrolases - genetics</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>glycosphingolipids</topic><topic>homology cloning</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>NEP sequence</topic><topic>Rhodococcus - enzymology</topic><topic>Rhodococcus - genetics</topic><topic>Sequence Analysis</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sakaguchi, Keishi</creatorcontrib><creatorcontrib>Okino, Nozomu</creatorcontrib><creatorcontrib>Sueyoshi, Noriyuki</creatorcontrib><creatorcontrib>Izu, Hiroyuki</creatorcontrib><creatorcontrib>Ito, Makoto</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sakaguchi, Keishi</au><au>Okino, Nozomu</au><au>Sueyoshi, Noriyuki</au><au>Izu, Hiroyuki</au><au>Ito, Makoto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Expression of Gene Encoding a Novel Endoglycoceramidase of Rhodococcus sp. Strain C9</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2000-07-01</date><risdate>2000</risdate><volume>128</volume><issue>1</issue><spage>145</spage><epage>152</epage><pages>145-152</pages><issn>0021-924X</issn><abstract>Endoglycoceramidase (EGCase) is an enzyme capable of cleaving the glycosidic linkage between oligosaccharides and ceramides of various glycosphingolipids. We previously reported that the Asn-Glu-Pro (NEP) sequence is part of the active site of EGCase of Rhodococcus sp. strain M-777. This paper describes the molecular cloning of a new EGCase gene utilising the NEP sequence front the genomic library of Rhodococcus sp. strain C9, which was clearly distinguishable from M-777 by 16S rDNA analysis. C9 EGCase possessed an open reading frame of 1,446 bp encoding 482 amino acids, and showed 78% and 76% identity to M-777 EGCase II at the nucleotide and amino acid levels, respectively. Interestingly, C9 EGCase showed the different specificity to the M-777 enzyme: it hydrolyzed b-series gangliotetraosylceramides more slowly than the M-777 enzyme, whereas both enzymes hydrolyzed a-series gangliosides and neutral glycosphingolipids to the same extent</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>10876169</pmid><doi>10.1093/oxfordjournals.jbchem.a022725</doi><tpages>8</tpages></addata></record> |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Base Sequence Carbohydrate Sequence Cloning, Molecular endoglycoceramidase gangliosides Gangliosides - metabolism Gene Expression Regulation, Enzymologic Glycoside Hydrolases - genetics Glycoside Hydrolases - metabolism glycosphingolipids homology cloning Hydrogen-Ion Concentration Kinetics Molecular Sequence Data NEP sequence Rhodococcus - enzymology Rhodococcus - genetics Sequence Analysis Sequence Homology, Amino Acid Substrate Specificity |
| title | Cloning and Expression of Gene Encoding a Novel Endoglycoceramidase of Rhodococcus sp. Strain C9 |
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