Linked Life Data

18809372

Source:http://linkedlifedata.com/resource/pubmed/id/18809372

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-10-30
pubmed:abstractText
Biotin protein ligase (BPL) is an essential enzyme responsible for the activation of biotin-dependent enzymes through the covalent attachment of biotin. In yeast, disruption of BPL affects important metabolic pathways such as fatty acid biosynthesis and gluconeogenesis. This makes BPL an attractive drug target for new antifungal agents. Here we report the cloning, recombinant expression and purification of BPL from the fungal pathogen Candida albicans. The biotin domains of acetyl CoA carboxylase and pyruvate carboxylase were also cloned and characterised as substrates for BPL. A novel assay was established thereby allowing examination of the enzyme's properties. These findings will facilitate future structural studies as well as screening efforts to identify potential inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1096-0384
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
479
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-9
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Biotin protein ligase from Candida albicans: expression, purification and development of a novel assay.
pubmed:affiliation
School of Molecular and Biomedical Science, University of Adelaide, Molecular Lifesciences Building, North Tce, Adelaide, SA 5005, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't