Plasmodium falciparum: Isolation and Characterisation of a Gene Encoding Protozoan GMP Synthase
McConkey, G. 2000. Plasmodium falciparum: Isolation and characterisation of a gene encoding protozoan GMP synthase. Experimental Parasitology94, 23–32. The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a proto...
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| description | McConkey, G. 2000. Plasmodium falciparum: Isolation and characterisation of a gene encoding protozoan GMP synthase. Experimental Parasitology94, 23–32. The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a protozoan GMP synthase. The deduced amino acid sequence from Plasmodium falciparum shares 40% identity with yeast GMP synthase and contains motifs conserved in catalysis. Expression of the gene is regulated through the parasite's development in human red blood cells with maximal expression during the point of DNA replication. Psicofuranine, which inhibits GMP synthase, interrupts parasite growth, supporting the role of this enzyme. These findings will aid development of inhibitors of purine salvage in malaria parasites. |
| doi_str_mv | 10.1006/expr.1999.4467 |
| format | Article |
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Plasmodium falciparum: Isolation and characterisation of a gene encoding protozoan GMP synthase. Experimental Parasitology94, 23–32. The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a protozoan GMP synthase. The deduced amino acid sequence from Plasmodium falciparum shares 40% identity with yeast GMP synthase and contains motifs conserved in catalysis. Expression of the gene is regulated through the parasite's development in human red blood cells with maximal expression during the point of DNA replication. Psicofuranine, which inhibits GMP synthase, interrupts parasite growth, supporting the role of this enzyme. These findings will aid development of inhibitors of purine salvage in malaria parasites.</description><identifier>ISSN: 0014-4894</identifier><identifier>EISSN: 1090-2449</identifier><identifier>DOI: 10.1006/expr.1999.4467</identifier><identifier>PMID: 10631077</identifier><identifier>CODEN: EXPAAA</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Carbon-Nitrogen Ligases - chemistry ; Carbon-Nitrogen Ligases - genetics ; Conserved Sequence ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Enzymologic ; glutamine amidotransferase ; GMP (guanosine 5′-monophosphate) ; GMP synthase ; GMP synthase (EC 6.3.4.1) ; Humans ; hypoxanthine-guanine phosphoribosyltransferase (HGPRT) ; IMP (inosine 5′-monophosphate) ; IMP dehydrogenase (IMPDH) ; Life cycle. Host-agent relationship. Pathogenesis ; Molecular Sequence Data ; Plasmodium falciparum ; Plasmodium falciparum (P. falciparum) ; Plasmodium falciparum - enzymology ; Plasmodium falciparum - genetics ; Protozoa ; Psicofuranine ; purine ; RACE (random amplification of cDNA ends) ; Sequence Alignment ; XMP (xanthosine 5′-monophosphate)</subject><ispartof>Experimental parasitology, 2000-01, Vol.94 (1), p.23-32</ispartof><rights>2000 Academic Press</rights><rights>2000 INIST-CNRS</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-13deb9ce6703022c83bd975284f8941cbbccd784d64788c1d6a80c6d33bed0513</citedby><cites>FETCH-LOGICAL-c400t-13deb9ce6703022c83bd975284f8941cbbccd784d64788c1d6a80c6d33bed0513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014489499944673$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1252407$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10631077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McConkey, Glenn A.</creatorcontrib><title>Plasmodium falciparum: Isolation and Characterisation of a Gene Encoding Protozoan GMP Synthase</title><title>Experimental parasitology</title><addtitle>Exp Parasitol</addtitle><description>McConkey, G. 2000. Plasmodium falciparum: Isolation and characterisation of a gene encoding protozoan GMP synthase. Experimental Parasitology94, 23–32. The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a protozoan GMP synthase. The deduced amino acid sequence from Plasmodium falciparum shares 40% identity with yeast GMP synthase and contains motifs conserved in catalysis. Expression of the gene is regulated through the parasite's development in human red blood cells with maximal expression during the point of DNA replication. Psicofuranine, which inhibits GMP synthase, interrupts parasite growth, supporting the role of this enzyme. These findings will aid development of inhibitors of purine salvage in malaria parasites.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbon-Nitrogen Ligases - chemistry</subject><subject>Carbon-Nitrogen Ligases - genetics</subject><subject>Conserved Sequence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>glutamine amidotransferase</subject><subject>GMP (guanosine 5′-monophosphate)</subject><subject>GMP synthase</subject><subject>GMP synthase (EC 6.3.4.1)</subject><subject>Humans</subject><subject>hypoxanthine-guanine phosphoribosyltransferase (HGPRT)</subject><subject>IMP (inosine 5′-monophosphate)</subject><subject>IMP dehydrogenase (IMPDH)</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Molecular Sequence Data</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum (P. falciparum)</subject><subject>Plasmodium falciparum - enzymology</subject><subject>Plasmodium falciparum - genetics</subject><subject>Protozoa</subject><subject>Psicofuranine</subject><subject>purine</subject><subject>RACE (random amplification of cDNA ends)</subject><subject>Sequence Alignment</subject><subject>XMP (xanthosine 5′-monophosphate)</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMGL1DAUxoMo7rh69Sg5iLeOL22mTbzJsI4LKw6o55C-vLqRNhmTVnb9623tgF7E04PH7_v4-DH2XMBWANSv6e6UtkJrvZWybh6wjQANRSmlfsg2AEIWUml5wZ7k_A0AlCjlY3YhoK4ENM2GmWNv8xCdnwbe2R79yaZpeMOvc-zt6GPgNji-v7XJ4kjJ5_UZO275gQLxq4BzOnzlxxTH-DPawA8fjvzTfRhvbaan7NFcm-nZ-V6yL--uPu_fFzcfD9f7tzcFSoCxEJWjViPVDVRQlqiq1ulmVyrZzfMFti2ia5R0tWyUQuFqqwBrV1UtOdiJ6pK9WntPKX6fKI9m8Bmp722gOGXTgKpFuVP_BYX6LUnP4HYFMcWcE3XmlPxg070RYBb3ZnFvFvdmcT8HXpybp3Yg9xe-yp6Bl2fAZrR9l2xAn_9w5a6UsGBqxWj29cNTMhk9BSTnE-FoXPT_mvAL1WagCg</recordid><startdate>200001</startdate><enddate>200001</enddate><creator>McConkey, Glenn A.</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>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200001</creationdate><title>Plasmodium falciparum: Isolation and Characterisation of a Gene Encoding Protozoan GMP Synthase</title><author>McConkey, Glenn A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-13deb9ce6703022c83bd975284f8941cbbccd784d64788c1d6a80c6d33bed0513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbon-Nitrogen Ligases - chemistry</topic><topic>Carbon-Nitrogen Ligases - genetics</topic><topic>Conserved Sequence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>glutamine amidotransferase</topic><topic>GMP (guanosine 5′-monophosphate)</topic><topic>GMP synthase</topic><topic>GMP synthase (EC 6.3.4.1)</topic><topic>Humans</topic><topic>hypoxanthine-guanine phosphoribosyltransferase (HGPRT)</topic><topic>IMP (inosine 5′-monophosphate)</topic><topic>IMP dehydrogenase (IMPDH)</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Molecular Sequence Data</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum (P. falciparum)</topic><topic>Plasmodium falciparum - enzymology</topic><topic>Plasmodium falciparum - genetics</topic><topic>Protozoa</topic><topic>Psicofuranine</topic><topic>purine</topic><topic>RACE (random amplification of cDNA ends)</topic><topic>Sequence Alignment</topic><topic>XMP (xanthosine 5′-monophosphate)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McConkey, Glenn A.</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>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McConkey, Glenn A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plasmodium falciparum: Isolation and Characterisation of a Gene Encoding Protozoan GMP Synthase</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>2000-01</date><risdate>2000</risdate><volume>94</volume><issue>1</issue><spage>23</spage><epage>32</epage><pages>23-32</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>McConkey, G. 2000. Plasmodium falciparum: Isolation and characterisation of a gene encoding protozoan GMP synthase. Experimental Parasitology94, 23–32. The final step in guanylate nucleotide biosynthesis is catalysed by GMP synthase. This paper presents the first isolation of a gene encoding a protozoan GMP synthase. The deduced amino acid sequence from Plasmodium falciparum shares 40% identity with yeast GMP synthase and contains motifs conserved in catalysis. Expression of the gene is regulated through the parasite's development in human red blood cells with maximal expression during the point of DNA replication. Psicofuranine, which inhibits GMP synthase, interrupts parasite growth, supporting the role of this enzyme. These findings will aid development of inhibitors of purine salvage in malaria parasites.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>10631077</pmid><doi>10.1006/expr.1999.4467</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Biological and medical sciences Carbon-Nitrogen Ligases - chemistry Carbon-Nitrogen Ligases - genetics Conserved Sequence Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic glutamine amidotransferase GMP (guanosine 5′-monophosphate) GMP synthase GMP synthase (EC 6.3.4.1) Humans hypoxanthine-guanine phosphoribosyltransferase (HGPRT) IMP (inosine 5′-monophosphate) IMP dehydrogenase (IMPDH) Life cycle. Host-agent relationship. Pathogenesis Molecular Sequence Data Plasmodium falciparum Plasmodium falciparum (P. falciparum) Plasmodium falciparum - enzymology Plasmodium falciparum - genetics Protozoa Psicofuranine purine RACE (random amplification of cDNA ends) Sequence Alignment XMP (xanthosine 5′-monophosphate) |
| title | Plasmodium falciparum: Isolation and Characterisation of a Gene Encoding Protozoan GMP Synthase |
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