Linked Life Data

7920700

Source:http://linkedlifedata.com/resource/pubmed/id/7920700

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-10-25
pubmed:databankReference
pubmed:abstractText
Glycinamide ribonucleotide (GAR) synthetase, GAR transformylase and aminoimidazole ribonucleotide (AIR) synthetase are the second, third and fifth enzymes in the 10-step de novo purine biosynthetic pathway. From a cDNA library of Arabidopsis thaliana, cDNAs encoding the above three enzymes were cloned by functional complementation of corresponding Escherichia coli mutants. Each of the cDNAs encode peptides comprising the complete enzymatic domain of either GAR synthetase, GAR transformylase or AIR synthetase. Comparisons of the three Arabidopsis purine biosynthetic enzymes with corresponding enzymes/polypeptide-fragments from procaryotic and eucaryotic sources indicate a high degree of conserved homology at the amino acid level, in particular with procaryotic enzymes. Assays from extracts of E. coli expressing the complementing clones verified the specific enzymatic activity of Arabidopsis GAR synthetase and GAR transformylase. Sequence analysis, as well as Northern blot analysis indicate that Arabidopsis has single and monofunctional enzymes. In this respect the organization of these three plant purine biosynthesis genes is fundamentally different from the multifunctional purine biosynthesis enzymes characteristic of other eucaryotes and instead resembles the one gene, one enzyme relationship found in procaryotes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7920700-Acyltransferases, pubmed-meshheading:7920700-Amino Acid Sequence, pubmed-meshheading:7920700-Arabidopsis, pubmed-meshheading:7920700-Base Sequence, pubmed-meshheading:7920700-Carbon-Nitrogen Ligases, pubmed-meshheading:7920700-Cloning, Molecular, pubmed-meshheading:7920700-DNA, Complementary, pubmed-meshheading:7920700-Escherichia coli, pubmed-meshheading:7920700-Gene Library, pubmed-meshheading:7920700-Genetic Complementation Test, pubmed-meshheading:7920700-Hydroxymethyl and Formyl Transferases, pubmed-meshheading:7920700-Ligases, pubmed-meshheading:7920700-Molecular Sequence Data, pubmed-meshheading:7920700-Mutagenesis, pubmed-meshheading:7920700-Phosphoribosylglycinamide Formyltransferase, pubmed-meshheading:7920700-Purines, pubmed-meshheading:7920700-Recombinant Proteins
pubmed:year
1994
pubmed:articleTitle
Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes.
pubmed:affiliation
Laboratoire de Biologie Cellulaire, INRA, Centre de Recherches de Versailles, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't