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Biotin protein ligase from Candida albicans: Expression, purification and development of a novel assay
- Source :
- Archives of Biochemistry and Biophysics. 479:163-169
- Publication Year :
- 2008
- Publisher :
- Elsevier BV, 2008.
-
Abstract
- 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. © 2008 Elsevier Inc. All rights reserved. Refereed/Peer-reviewed
- Subjects :
- assay development
Antifungal Agents
Drug Evaluation, Preclinical
Biophysics
Biotin
Biology
Biochemistry
Fungal Proteins
chemistry.chemical_compound
Candida albicans
Carbon-Nitrogen Ligases
biotin protein ligase
Enzyme Inhibitors
Molecular Biology
Pyruvate Carboxylase
chemistry.chemical_classification
Fungal protein
DNA ligase
Fatty Acids
Gluconeogenesis
Acetyl-CoA carboxylase
biology.organism_classification
fungicide, drug discovery
Molecular biology
Recombinant Proteins
Protein Structure, Tertiary
Pyruvate carboxylase
Metabolic pathway
Enzyme
chemistry
protein structure and function
candida albicans
Biological Assay
Acetyl-CoA Carboxylase
Subjects
Details
- ISSN :
- 00039861
- Volume :
- 479
- Database :
- OpenAIRE
- Journal :
- Archives of Biochemistry and Biophysics
- Accession number :
- edsair.doi.dedup.....9d4bb9d7d8ad29c2a74fa94957d1a276