Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes
We have previously reported that Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing...
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| Veröffentlicht in: | FEMS microbiology letters 2003-12, Vol.229 (2), p.217-222 |
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| creator | Vernal, Javier José Cazzulo, Juan Nowicki, Cristina |
| description | We have previously reported that
Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing in
Escherichia coli the recombinant active protein. The amino acid sequence of BSAT shares over 40% identity with other eukaryotic and prokaryotic aspartate aminotransferases, thus showing that the enzyme belongs to the subfamily Iα of aminotransferases, and has only 6% identity with the tyrosine aminotransferase from
Trypanosoma cruzi, which has a similar substrate specificity. The production of recombinant active enzyme in good yields opens up the possibility of obtaining its 3D-structure, in order to investigate the structural basis of the broad substrate specificity. |
| doi_str_mv | 10.1016/S0378-1097(03)00824-3 |
| format | Article |
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Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing in
Escherichia coli the recombinant active protein. The amino acid sequence of BSAT shares over 40% identity with other eukaryotic and prokaryotic aspartate aminotransferases, thus showing that the enzyme belongs to the subfamily Iα of aminotransferases, and has only 6% identity with the tyrosine aminotransferase from
Trypanosoma cruzi, which has a similar substrate specificity. The production of recombinant active enzyme in good yields opens up the possibility of obtaining its 3D-structure, in order to investigate the structural basis of the broad substrate specificity.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/S0378-1097(03)00824-3</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Elsevier B.V</publisher><subject>aminotransferase ; Aminotransferases ; Biological and medical sciences ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Heterologous expression ; Leishmania mexicana ; Microbiology ; transaminate ; Trypanosoma cruzi</subject><ispartof>FEMS microbiology letters, 2003-12, Vol.229 (2), p.217-222</ispartof><rights>2003 Federation of European Microbiological Societies</rights><rights>2003 Federation of European Microbiological Societies 2003</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-b352c03ee913e3bdf568fc6aeabc5cd563aa05b46300605b5423973af3792e1d3</citedby><cites>FETCH-LOGICAL-c409t-b352c03ee913e3bdf568fc6aeabc5cd563aa05b46300605b5423973af3792e1d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16126551$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Vernal, Javier</creatorcontrib><creatorcontrib>José Cazzulo, Juan</creatorcontrib><creatorcontrib>Nowicki, Cristina</creatorcontrib><title>Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes</title><title>FEMS microbiology letters</title><description>We have previously reported that
Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing in
Escherichia coli the recombinant active protein. The amino acid sequence of BSAT shares over 40% identity with other eukaryotic and prokaryotic aspartate aminotransferases, thus showing that the enzyme belongs to the subfamily Iα of aminotransferases, and has only 6% identity with the tyrosine aminotransferase from
Trypanosoma cruzi, which has a similar substrate specificity. The production of recombinant active enzyme in good yields opens up the possibility of obtaining its 3D-structure, in order to investigate the structural basis of the broad substrate specificity.</description><subject>aminotransferase</subject><subject>Aminotransferases</subject><subject>Biological and medical sciences</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heterologous expression</subject><subject>Leishmania mexicana</subject><subject>Microbiology</subject><subject>transaminate</subject><subject>Trypanosoma cruzi</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkMFu1DAQhi0EEkvhEZB8AdFDyjiOneSE0IpCpZV6AM7WxJlsjRI7eLKofXuy3QqEhNTT-PD9_4w_IV4ruFCg7PuvoOumUNDW70CfAzRlVegnYqNMXRW2tc1TsfmDPBcvmH8AQFWC3Yh5O6YY4l5i7OUNLZTTmPbpwJJu50zMIUWZBomyywl7yTP5MAQfljuJU4hpyRh5oIxMR25HgW8mjAHlRLfBY0Q55zQhL2GfFuKX4tmAI9Orh3kmvl9--rb9UuyuP19tP-4KX0G7FJ02pQdN1CpNuusHY5vBWyTsvPG9sRoRTFdZDWDXh6lK3dYaB123Jalen4m3p951-88D8eKmwJ7GESOt33OqbhrbtHYFzQn0OTFnGtycw4T5zilwR7_u3q87ynOg3b1fp9fcm4cFyB7HYfXgA_8NW1VaY9TKwYlLh_n_1cU_1cWx-sMpQqugX4GyYx8oeupDJr-4PoVHjvsN6zefpg</recordid><startdate>20031212</startdate><enddate>20031212</enddate><creator>Vernal, Javier</creator><creator>José Cazzulo, Juan</creator><creator>Nowicki, Cristina</creator><general>Elsevier B.V</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20031212</creationdate><title>Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes</title><author>Vernal, Javier ; José Cazzulo, Juan ; Nowicki, Cristina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-b352c03ee913e3bdf568fc6aeabc5cd563aa05b46300605b5423973af3792e1d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>aminotransferase</topic><topic>Aminotransferases</topic><topic>Biological and medical sciences</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heterologous expression</topic><topic>Leishmania mexicana</topic><topic>Microbiology</topic><topic>transaminate</topic><topic>Trypanosoma cruzi</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vernal, Javier</creatorcontrib><creatorcontrib>José Cazzulo, Juan</creatorcontrib><creatorcontrib>Nowicki, Cristina</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vernal, Javier</au><au>José Cazzulo, Juan</au><au>Nowicki, Cristina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes</atitle><jtitle>FEMS microbiology letters</jtitle><date>2003-12-12</date><risdate>2003</risdate><volume>229</volume><issue>2</issue><spage>217</spage><epage>222</epage><pages>217-222</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>We have previously reported that
Leishmania mexicana promastigotes possess a broad substrate specificity aminotransferase (BSAT), able to transaminate aspartate, aromatic amino acids, methionine and leucine. We have confirmed now this unusual substrate specificity by cloning its gene and expressing in
Escherichia coli the recombinant active protein. The amino acid sequence of BSAT shares over 40% identity with other eukaryotic and prokaryotic aspartate aminotransferases, thus showing that the enzyme belongs to the subfamily Iα of aminotransferases, and has only 6% identity with the tyrosine aminotransferase from
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| ispartof | FEMS microbiology letters, 2003-12, Vol.229 (2), p.217-222 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | aminotransferase Aminotransferases Biological and medical sciences Escherichia coli Fundamental and applied biological sciences. Psychology Heterologous expression Leishmania mexicana Microbiology transaminate Trypanosoma cruzi |
| title | Cloning and heterologous expression of a broad specificity aminotransferase of Leishmania mexicana promastigotes |
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