Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/50903
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | Biotin protein ligase from Candida albicans: Expression, purification and development of a novel assay |
Author: | Pendini, N. Bailey, L. Booker, G. Wilce, M. Wallace, J. Polyak, S. |
Citation: | Archives of Biochemistry and Biophysics, 2008; 479(2):163-169 |
Publisher: | Academic Press Inc |
Issue Date: | 2008 |
ISSN: | 0003-9861 1096-0384 |
Statement of Responsibility: | Nicole R. Pendini, Lisa M. Bailey, Grant W. Booker, Matthew C.J. Wilce, John C. Wallace and Steven W. Polyak |
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. |
Keywords: | Biotin protein ligase Candida albicans Fungicide, drug discovery Protein structure and function Assay development |
Description: | Copyright © 2008 Elsevier Inc. All rights reserved. |
DOI: | 10.1016/j.abb.2008.08.021 |
Grant ID: | NHMRC ARC |
Published version: | http://dx.doi.org/10.1016/j.abb.2008.08.021 |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.