Genetic Breeding of<scp>l</scp>-Tyrosine Producer from<i>Bvevihactevium lactofermentum</i>

Ito, Hisao; Sakurai, S.; Tanaka, Takashi; Sato, Katsuaki; Enei, Hitoshi

doi:10.1080/00021369.1990.10870028

Cited by 5 publications

(1 citation statement)

References 4 publications

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“…28) Hence various overproducing strains of L-tyrosine, including Arthrobacter globiformis, Brevibacterium lactofermentum, and Corynebacterium glutamicum, have been engineered by traditional mutagenesis. [29][30][31] L-Tyrosine-overproducing E. coli have also been metabolically engineered using different strategies. 28,[32][33][34] E. coli is one of the most thoroughly studied organisms, and its genome can be manipulated by a range of molecular genetic methods, enabling the construction of desired mutants for the overproduction of aromatic amino acids.…”

Section: Fermentative Production Of Bias From Simple Carbon Sourcesmentioning

confidence: 99%

Fermentative Production of Plant Benzylisoquinoline Alkaloids in Microbes

Minami

2013

Bioscience, Biotechnology, and Biochemistry

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Higher plants produce diverse chemicals, including alkaloids, terpenoids, and phenolic compounds (phenylpropanoids and flavonoids) as secondary metabolites. These chemicals are widely used for human health and nutrition. Alkaloids, for example, are valued in medicine due to their high biological activities, but most of these metabolites accumulate at low levels in plant cells, resulting in poor extraction yields. Increasingly, attention is devoted to the production of plant metabolites by reconstructing plant biosynthetic pathways in microorganisms. This technology has been aided by advances in synthetic biology and metabolic engineering. Here, the review a fermentation platform for low-cost production of numerous alkaloids using bioengineered Escherichia coli and/or Saccharomyces cerevisiae.

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Section: Fermentative Production Of Bias From Simple Carbon Sourcesmentioning

confidence: 99%

Fermentative Production of Plant Benzylisoquinoline Alkaloids in Microbes

Minami

2013

Bioscience, Biotechnology, and Biochemistry

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Molecular breeding of a Brevibacterium lactofermentum l-phenylalanine producer using a cloned prephenate dehydratase gene

Ito

Sato

Matsui

et al. 1990

Appl Microbiol Biotechnol

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The prephenate dehydratase gene was cloned from a mutant of Brevibacterium lactofermenturn, AJl1957 that produced enzyme free from feedback inhibition. The recombinant plasmids pPHI 1 and pPH14 complemented a phenylalanine auxotroph of B. lactofermenturn, A-15, provided the transformant with the desensitized enzyme and caused an increased level of the enzyme compared to that of a wild strain. Plasmid pPH14 was introduced into L-phenylalanine producers genetically induced from Bo lactofermentum; MF358 and FP-1 excreting L-tyrosine and anthranilate, respectively, as by-products. Both transformants predominantly accumulated L-phenylalanine at the expense of by-product formation. Co-existence of pPH14 and pTAR16, a recombinant plasmid expressing desensitized 3-deoxy-D-arabino-hepturosonate-7-phosphate synthase had a marked effect on further improvement in L-phenylalanine productivity, accompanied by an increase in the corresponding enzyme activity. The parent, MF358, accumulating 5.5g/1 L-phenylalanine, 6.8 g/1 L-tyrosine and 0.3 g/1 anthranilate turned into a potent L-phenylalanine producer producing 18.2 g/1 Lphenylalanine and 1.0 g/1 L-tyrosine by-product.

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Unraveling the specific regulation of the shikimate pathway for tyrosine accumulation in Bacillus licheniformis

Zhang

et al. 2019

Journal of Industrial Microbiology and Biotechnology

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l-Tyrosine serves as a common precursor for multiple valuable secondary metabolites. Synthesis of this aromatic amino acid in Bacillus licheniformis occurs via the shikimate pathway, but the underlying mechanisms involving metabolic regulation remain unclear. In this work, improved l-tyrosine accumulation was achieved in B. licheniformis via co-overexpression of aroGfbr and tyrAfbr from Escherichia coli to yield strain 45A12, and the l-tyrosine titer increased to 1005 mg/L with controlled glucose feeding. Quantitative RT-PCR results indicated that aroA, encoding DAHP synthase, and aroK, encoding shikimate kinase, were feedback-repressed by the end product l-tyrosine in the modified strain. Therefore, the native aroK was first expressed with multiple copies to yield strain 45A13, which could accumulate 1201 mg/L l-tyrosine. Compared with strain 45A12, the expression of aroB and aroF in strain 45A13 was upregulated by 21% and 27%, respectively, which may also have resulted in the improvement of l-tyrosine production. Furthermore, supplementation with 5 g/L shikimate enhanced the l-tyrosine titers of 45A12 and 45A13 by 29.1% and 24.0%, respectively. However, the yield of l-tyrosine per unit of shikimate decreased from 0.365 to 0.198 mol/mol after aroK overexpression in strain 45A12, which suggested that the gene product was also involved in uncharacterized pathways. This study provides a good starting point for further modification to achieve industrial-scale production of l-tyrosine using B. licheniformis, a generally recognized as safe workhorse.

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Genetic Breeding ofl-Tyrosine Producer fromBvevihactevium lactofermentum

Cited by 5 publications

References 4 publications

Fermentative Production of Plant Benzylisoquinoline Alkaloids in Microbes

Fermentative Production of Plant Benzylisoquinoline Alkaloids in Microbes

Molecular breeding of a Brevibacterium lactofermentum l-phenylalanine producer using a cloned prephenate dehydratase gene

Unraveling the specific regulation of the shikimate pathway for tyrosine accumulation in Bacillus licheniformis

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