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detection of unique gene LYS1 for rapid identification of pathogenic fungi, LYS1 gene is a possible target for selective inhibition of growth of pathogenic fungi in vivo
novel glutarate biosynthetic pathway by incorporation of a +1 carbon chain extension pathway from 2-oxoglutarate in combination with 2-oxo acid decarboxylation pathway in Escherichia coli. Introduction of homocitrate synthase, homoaconitase and homoisocitrate dehydrogenase from Saccharomyces cerevisiae into Escherichia coli enables +1 carbon extension from 2-oxoglutarate to 2-oxoadipate, which is subsequently converted into glutarate by a promiscuous 2-oxo acid decarboxylase (KivD) and a succinate semialdehyde dehydrogenase (GabD). The recombinant Escherichia coli coexpressing all five genes produces 0.3 g/l glutarate from glucose. To further improve the titers, 2-oxoglutarate is rechanneled into carbon chain extension pathway via the clustered regularly interspersed palindromic repeats system mediated interference (CRISPRi) of essential genes sucA and sucB in tricarboxylic acid cycle. The final strain can produce 0.42 g/l glutarate, which is increased by 40% compared with the parental strain. Glutarate is one of the most potential building blocks for bioplastics
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