Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-3-23
pubmed:databankReference
pubmed:abstractText
A cDNA encoding farnesyl diphosphate synthase, an enzyme that synthesizes C15 isoprenoid diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate, was cloned from an Arabidopsis thaliana cDNA library by complementation of a mutant of Saccharomyces cerevisiae deficient in this enzyme. The A. thaliana cDNA was also able to complement the lethal phenotype of the erg20 deletion yeast mutant. As deduced from the full-length 1.22 kb cDNA nucleotide sequence, the polypeptide contains 343 amino acids and has a relative molecular mass of 39,689. The predicted amino acid sequence presents about 50% identity with the yeast, rat and human FPP synthases. Southern blot analyses indicate that A. thaliana probably contains a single gene for farnesyl diphosphate synthase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3,3-dimethylallyl pyrophosphate, http://linkedlifedata.com/resource/pubmed/chemical/Alkyl and Aryl Transferases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Ergosterol, http://linkedlifedata.com/resource/pubmed/chemical/Geranyltranstransferase, http://linkedlifedata.com/resource/pubmed/chemical/Hemiterpenes, http://linkedlifedata.com/resource/pubmed/chemical/Organophosphorus Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Polyisoprenyl Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Sesquiterpenes, http://linkedlifedata.com/resource/pubmed/chemical/Transferases, http://linkedlifedata.com/resource/pubmed/chemical/farnesyl pyrophosphate, http://linkedlifedata.com/resource/pubmed/chemical/isopentenyl pyrophosphate
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1867-73
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7858223-Alkyl and Aryl Transferases, pubmed-meshheading:7858223-Amino Acid Sequence, pubmed-meshheading:7858223-Arabidopsis, pubmed-meshheading:7858223-Base Sequence, pubmed-meshheading:7858223-Cloning, Molecular, pubmed-meshheading:7858223-DNA, Complementary, pubmed-meshheading:7858223-Ergosterol, pubmed-meshheading:7858223-Genetic Complementation Test, pubmed-meshheading:7858223-Geranyltranstransferase, pubmed-meshheading:7858223-Hemiterpenes, pubmed-meshheading:7858223-Molecular Sequence Data, pubmed-meshheading:7858223-Organophosphorus Compounds, pubmed-meshheading:7858223-Plant Proteins, pubmed-meshheading:7858223-Polyisoprenyl Phosphates, pubmed-meshheading:7858223-Saccharomyces cerevisiae, pubmed-meshheading:7858223-Sequence Homology, Amino Acid, pubmed-meshheading:7858223-Sesquiterpenes, pubmed-meshheading:7858223-Transferases
pubmed:year
1994
pubmed:articleTitle
Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate synthase by functional complementation in yeast.
pubmed:affiliation
Laboratoire de Génétique Physiologique et Moléculaire, Université de Poitiers, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't