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- W1566607639 endingPage "4476" @default.
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- W1566607639 abstract "Phenylalanine and tyrosine ammonia-lyases form cinnamic acid and p-coumaric acid, which are precursors of a wide range of aromatic compounds of biotechnological interest. Lack of highly active and specific tyrosine ammonia-lyases has previously been a limitation in metabolic engineering approaches. We therefore identified 22 sequences in silico using synteny information and aiming for sequence divergence. We performed a comparative in vivo study, expressing the genes intracellularly in bacteria and yeast. When produced heterologously, some enzymes resulted in significantly higher production of p-coumaric acid in several different industrially important production organisms. Three novel enzymes were found to have activity exclusively for phenylalanine, including an enzyme from the low-GC Gram-positive bacterium Brevibacillus laterosporus, a bacterial-type enzyme from the amoeba Dictyostelium discoideum, and a phenylalanine ammonia-lyase from the moss Physcomitrella patens (producing 230 μM cinnamic acid per unit of optical density at 600 nm [OD600]) in the medium using Escherichia coli as the heterologous host). Novel tyrosine ammonia-lyases having higher reported substrate specificity than previously characterized enzymes were also identified. Enzymes from Herpetosiphon aurantiacus and Flavobacterium johnsoniae resulted in high production of p-coumaric acid in Escherichia coli (producing 440 μM p-coumaric acid OD600 unit(-1) in the medium) and in Lactococcus lactis. The enzymes were also efficient in Saccharomyces cerevisiae, where p-coumaric acid accumulation was improved 5-fold over that in strains expressing previously characterized tyrosine ammonia-lyases." @default.
- W1566607639 created "2016-06-24" @default.
- W1566607639 creator A5007657971 @default.
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- W1566607639 creator A5090181935 @default.
- W1566607639 date "2015-07-01" @default.
- W1566607639 modified "2023-10-16" @default.
- W1566607639 title "Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in Bacteria and Saccharomyces cerevisiae" @default.
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- W1566607639 doi "https://doi.org/10.1128/aem.00405-15" @default.
- W1566607639 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4475877" @default.
- W1566607639 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25911487" @default.
- W1566607639 hasPublicationYear "2015" @default.