Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum
Phospholipase D (PLD), secreted into the culture medium of an actinomycete, Streptoverticillium cinnamoneum, has been purified to homogeneity and characterized. The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphati...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1999-02, Vol.125 (2), p.263-269 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Ogino, Chiaki Negi, Yukinari Matsumiya, Toshiko Nakaoka, Koichi Kondo, Akihiko Kuroda, Shun'ichi Tokuyama, Shinji Kikkawa, Ushio Yamane, Tsuneo Fukuda, Hideki |
| description | Phospholipase D (PLD), secreted into the culture medium of an actinomycete, Streptoverticillium cinnamoneum, has been purified to homogeneity and characterized. The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholine (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially Al3+. Nucleotide and amino acid sequence determination of the Stv. cinnamoneum PLD revealed the presence of common structural motifs identified in all PLD sequences from various species. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a022282 |
| format | Article |
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The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholine (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially Al3+. Nucleotide and amino acid sequence determination of the Stv. cinnamoneum PLD revealed the presence of common structural motifs identified in all PLD sequences from various species.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a022282</identifier><identifier>PMID: 9990122</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Aluminum - metabolism ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA, Bacterial - analysis ; Hydrolysis ; Mannosidases - isolation & purification ; Mannosidases - metabolism ; Metals - metabolism ; Molecular Sequence Data ; phospholipase D (PLD) ; Phospholipase D - genetics ; Phospholipase D - isolation & purification ; Phospholipase D - metabolism ; Sequence Homology, Amino Acid ; Streptomycetaceae - enzymology ; Streptomycetaceae - genetics ; Streptoverticillium cinnamoneum ; Substrate Specificity ; transphosphatidylation</subject><ispartof>Journal of biochemistry (Tokyo), 1999-02, Vol.125 (2), p.263-269</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-735d223b929d1b45f033bb4b0ba1d04686b11fe9c86d780aaa587b14f2aade1b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9990122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogino, Chiaki</creatorcontrib><creatorcontrib>Negi, Yukinari</creatorcontrib><creatorcontrib>Matsumiya, Toshiko</creatorcontrib><creatorcontrib>Nakaoka, Koichi</creatorcontrib><creatorcontrib>Kondo, Akihiko</creatorcontrib><creatorcontrib>Kuroda, Shun'ichi</creatorcontrib><creatorcontrib>Tokuyama, Shinji</creatorcontrib><creatorcontrib>Kikkawa, Ushio</creatorcontrib><creatorcontrib>Yamane, Tsuneo</creatorcontrib><creatorcontrib>Fukuda, Hideki</creatorcontrib><title>Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Phospholipase D (PLD), secreted into the culture medium of an actinomycete, Streptoverticillium cinnamoneum, has been purified to homogeneity and characterized. The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholine (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially Al3+. Nucleotide and amino acid sequence determination of the Stv. cinnamoneum PLD revealed the presence of common structural motifs identified in all PLD sequences from various species.</description><subject>Aluminum - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial - analysis</subject><subject>Hydrolysis</subject><subject>Mannosidases - isolation & purification</subject><subject>Mannosidases - metabolism</subject><subject>Metals - metabolism</subject><subject>Molecular Sequence Data</subject><subject>phospholipase D (PLD)</subject><subject>Phospholipase D - genetics</subject><subject>Phospholipase D - isolation & purification</subject><subject>Phospholipase D - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Streptomycetaceae - enzymology</subject><subject>Streptomycetaceae - genetics</subject><subject>Streptoverticillium cinnamoneum</subject><subject>Substrate Specificity</subject><subject>transphosphatidylation</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhn0AldLyEyrlAiey-COJ4wMHWKCt1BVFpVLFxfLHROslsVM7QV1-PS4bVeLEyRo_78zYehB6TfCKYMHehYcuRLsLc_SqT6udNlsYVgpTSlv6DB1jTEkpaHX3Ar1MafdYUsaO0JEQAhNKj9H-eo6uc0ZNLvi3xXqrojITRPd7uVHeFjdwP4M3UHyCjAbn_7IidMX1NqRxG3o3qpRxTpqYM7bQ--JmijBO4RfEyRnX924eCuO8V0PwMA-n6HmXHw2vlvME3X75_H19UV59Pb9cf7gqTU3bqeSstpQyLaiwRFd1hxnTutJYK2Jx1bSNJqQDYdrG8hYrpeqWa1J1VCkLRLMT9OYwd4whfyNNcnDJQN8rD2FOshE1FzXj_w0SzgSvSJWD7w9BE0NKETo5RjeouJcEy0cv8l8v8uBFLl5y_9myaNYD2KfuRUrm5YG7NMHDE1bxp2w447W8uPshN_X5ZvPx20ZW7A9wLKYg</recordid><startdate>19990201</startdate><enddate>19990201</enddate><creator>Ogino, Chiaki</creator><creator>Negi, Yukinari</creator><creator>Matsumiya, Toshiko</creator><creator>Nakaoka, Koichi</creator><creator>Kondo, Akihiko</creator><creator>Kuroda, Shun'ichi</creator><creator>Tokuyama, Shinji</creator><creator>Kikkawa, Ushio</creator><creator>Yamane, Tsuneo</creator><creator>Fukuda, Hideki</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19990201</creationdate><title>Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum</title><author>Ogino, Chiaki ; Negi, Yukinari ; Matsumiya, Toshiko ; Nakaoka, Koichi ; Kondo, Akihiko ; Kuroda, Shun'ichi ; Tokuyama, Shinji ; Kikkawa, Ushio ; Yamane, Tsuneo ; Fukuda, Hideki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-735d223b929d1b45f033bb4b0ba1d04686b11fe9c86d780aaa587b14f2aade1b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Aluminum - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial - analysis</topic><topic>Hydrolysis</topic><topic>Mannosidases - isolation & purification</topic><topic>Mannosidases - metabolism</topic><topic>Metals - metabolism</topic><topic>Molecular Sequence Data</topic><topic>phospholipase D (PLD)</topic><topic>Phospholipase D - genetics</topic><topic>Phospholipase D - isolation & purification</topic><topic>Phospholipase D - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Streptomycetaceae - enzymology</topic><topic>Streptomycetaceae - genetics</topic><topic>Streptoverticillium cinnamoneum</topic><topic>Substrate Specificity</topic><topic>transphosphatidylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogino, Chiaki</creatorcontrib><creatorcontrib>Negi, Yukinari</creatorcontrib><creatorcontrib>Matsumiya, Toshiko</creatorcontrib><creatorcontrib>Nakaoka, Koichi</creatorcontrib><creatorcontrib>Kondo, Akihiko</creatorcontrib><creatorcontrib>Kuroda, Shun'ichi</creatorcontrib><creatorcontrib>Tokuyama, Shinji</creatorcontrib><creatorcontrib>Kikkawa, Ushio</creatorcontrib><creatorcontrib>Yamane, Tsuneo</creatorcontrib><creatorcontrib>Fukuda, Hideki</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogino, Chiaki</au><au>Negi, Yukinari</au><au>Matsumiya, Toshiko</au><au>Nakaoka, Koichi</au><au>Kondo, Akihiko</au><au>Kuroda, Shun'ichi</au><au>Tokuyama, Shinji</au><au>Kikkawa, Ushio</au><au>Yamane, Tsuneo</au><au>Fukuda, Hideki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1999-02-01</date><risdate>1999</risdate><volume>125</volume><issue>2</issue><spage>263</spage><epage>269</epage><pages>263-269</pages><issn>0021-924X</issn><abstract>Phospholipase D (PLD), secreted into the culture medium of an actinomycete, Streptoverticillium cinnamoneum, has been purified to homogeneity and characterized. The Stv. cinnamoneum PLD efficiently catalyzes both the hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholine (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially Al3+. Nucleotide and amino acid sequence determination of the Stv. cinnamoneum PLD revealed the presence of common structural motifs identified in all PLD sequences from various species.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>9990122</pmid><doi>10.1093/oxfordjournals.jbchem.a022282</doi><tpages>7</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 | Aluminum - metabolism Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial - analysis Hydrolysis Mannosidases - isolation & purification Mannosidases - metabolism Metals - metabolism Molecular Sequence Data phospholipase D (PLD) Phospholipase D - genetics Phospholipase D - isolation & purification Phospholipase D - metabolism Sequence Homology, Amino Acid Streptomycetaceae - enzymology Streptomycetaceae - genetics Streptoverticillium cinnamoneum Substrate Specificity transphosphatidylation |
| title | Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum |
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