Linked Life Data

20383010

Source:http://linkedlifedata.com/resource/pubmed/id/20383010

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2010-4-12
pubmed:abstractText
Aspartate aminotransferases (EC 2.6.1.1) catalyse the conversion of aspartate and alpha-ketoglutarate to oxaloacetate and glutamate in a reversible manner. Thus, the aspartate aminotransferase of Plasmodium falciparum (PfAspAT) plays a central role in the transamination of amino acids. Recent findings suggest that PfAspAT may also play a pivotal role in energy metabolism and the de novo biosynthesis of pyrimidines. While therapeutics based upon the inhibition of other proteins in these pathways are already used in the treatment of malaria, the advent of multidrug-resistant strains has limited their efficacy. The presence of PfAspAT in these pathways may offer additional opportunities for the development of novel therapeutics. In order to gain a deeper understanding of the function and role of PfAspAT, it has been expressed and purified to homogeneity. The successful crystallization of PfAspAT, the collection of a 2.8 A diffraction data set and initial attempts to solve the structure using molecular replacement are reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
409-12
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Purification, crystallization and preliminary X-ray analysis of the aspartate aminotransferase of Plasmodium falciparum.
pubmed:affiliation
European Molecular Biology Laboratory Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't