One of the WHO's
three critical priority pathogens, Acinetobacter baumannii, for which new
antibiotics are urgently needed is one step closer to being tackled, as
researchers from the Department of Chemistry -- University of Warwick have made
a breakthrough in understanding the enzymes that assemble the antibiotic
enacyloxin.
In a
previous paper, researchers at the University of Warwick and Cardiff University
showed that a molecule called enacyloxin is effective against Acinetobacter
baumannii. However, the molecule needs to be engineered to make it suitable for
treating infections caused by the pathogen in humans.
The
first step to achieving this is to understand the molecular mechanisms used to
assemble enacyloxin by the bacterium that makes it. In their paper 'A dual
transacylation mechanism for polyketide synthase chain release in enacyloxin
antibiotic biosynthesis' published in the journal Nature Chemistry, the
researchers identify the enzymes responsible for joining the two components of
the antibiotic together.
The
key enzyme in this process was found to be promiscuous, suggesting it could be
harnessed to produce structurally modified versions of the antibiotic.
See:
Posted by Dr. Tim Sandle, Pharmaceutical Microbiology
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