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L,L-diaminopimelate aminotransferase (DapL): a putative target for the development of narrow-spectrum antibacterial compounds

Triassi, Alexander J, Wheatley, Matthew S, Savka, Michael A, Gan, Han Ming, Dobson, Renwick CJ and Hudson, André O 2014, L,L-diaminopimelate aminotransferase (DapL): a putative target for the development of narrow-spectrum antibacterial compounds, Frontiers in microbiology, vol. 5, pp. 1-10, doi: 10.3389/fmicb.2014.00509.

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Title L,L-diaminopimelate aminotransferase (DapL): a putative target for the development of narrow-spectrum antibacterial compounds
Author(s) Triassi, Alexander J
Wheatley, Matthew S
Savka, Michael A
Gan, Han MingORCID iD for Gan, Han Ming orcid.org/0000-0001-7987-738X
Dobson, Renwick CJ
Hudson, André O
Journal name Frontiers in microbiology
Volume number 5
Article ID 509
Start page 1
End page 10
Total pages 10
Publisher Frontiers Media
Place of publication Lausanne, Switzerland
Publication date 2014-09
ISSN 1664-302X
Keyword(s) L,L-diaminopimelate aminotransferase
amino acid
antibacterial
antibiotic
diaminopimelate
lysine
peptidoglycan
pyridoxal-5′-phosphate
Summary Despite the urgent need for sustained development of novel antibacterial compounds to combat the drastic rise in antibiotic resistant and emerging bacterial infections, only a few clinically relevant antibacterial drugs have been recently developed. One of the bottlenecks impeding the development of novel antibacterial compounds is the identification of new enzymatic targets. The nutritionally essential amino acid anabolic pathways, for example lysine biosynthesis, provide an opportunity to explore the development of antibacterial compounds, since human genomes do not possess the genes necessary to synthesize these amino acids de novo. The diaminopimelate (DAP)/lysine (lys) anabolic pathways are attractive targets for antibacterial development since the penultimate lys precursor meso-DAP (m-DAP) is a cross-linking amino acid in the peptidoglycan (PG) cell wall of most Gram-negative bacteria and lys plays a similar role in the PG of most Gram-positive bacteria, in addition to its role as one of the 20 proteogenic amino acids. The L,L-diaminopimelate aminotransferase (DapL) pathway was recently identified as a novel variant of the DAP/lys anabolic pathways. The DapL pathway has been identified in the pathogenic bacteria belonging to the genus; Chlamydia, Leptospira, and Treponema. The dapL gene has been identified in the genomes of 381 or approximately 13% of the 2771 bacteria that have been sequenced, annotated and reposited in the NCBI database, as of May 23, 2014. The narrow distribution of the DapL pathway in the bacterial domain provides an opportunity for the development and or discovery of narrow spectrum antibacterial compounds.
Language eng
DOI 10.3389/fmicb.2014.00509
Field of Research 060503 Microbial Genetics
110801 Medical Bacteriology
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2014, Triassi, Wheatley, Savka, Gan, Dobson and Hudson
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30101917

Document type: Journal Article
Collections: School of Life and Environmental Sciences
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.