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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1994-8-22
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pubmed:databankReference |
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pubmed:abstractText |
The enzyme dihydropteroate synthetase (DHPS) from Plasmodium falciparum is involved in the mechanism of action of the sulfone/sulfonamide group of drugs. We describe the cloning and sequencing of the gene encoding the P. falciparum DHPS enzyme and show that it is a bifunctional enzyme that includes dihydro-6-hydroxymethylpterin pyrophosphokinase (PPPK) at the N terminus of DHPS. The gene encodes a putative protein of 83 kDa that contains two domains that are homologous with the DHPS and PPPK enzymes of other organisms. The PPPK-DHPS gene is encoded on chromosome 8 and has two introns. An antibody raised to the PPPK region of the protein was found to recognize a 68-kDa protein that is expressed throughout the asexual life cycle of the parasite. We have determined the sequence of the DHPS portion of the gene from sulfadoxine-sensitive and -resistant P. falciparum clones and identified sequence differences that may have a role in sulfone/sulfonamide resistance.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-1313386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-1325970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-1400191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-1522070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-1775161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2024960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2123867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2168367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2185424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2643036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2690004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-2873508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-3047011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-3057499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-3095842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-3114239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-338184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-351412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-3538420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-4354403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-4435732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-4602912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-8232427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041761-8397083
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
91
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pubmed:geneSymbol |
PPPK-DHPS
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7149-53
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8041761-Amino Acid Sequence,
pubmed-meshheading:8041761-Animals,
pubmed-meshheading:8041761-Base Sequence,
pubmed-meshheading:8041761-Chromosome Mapping,
pubmed-meshheading:8041761-Cloning, Molecular,
pubmed-meshheading:8041761-DNA, Protozoan,
pubmed-meshheading:8041761-Dihydropteroate Synthase,
pubmed-meshheading:8041761-Diphosphotransferases,
pubmed-meshheading:8041761-Genes, Protozoan,
pubmed-meshheading:8041761-Molecular Sequence Data,
pubmed-meshheading:8041761-Plasmodium falciparum,
pubmed-meshheading:8041761-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Primary structure and expression of the dihydropteroate synthetase gene of Plasmodium falciparum.
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pubmed:affiliation |
Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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