Hyperproduction of 3,4-Dihydroxyphenyl-<scp>L</scp>-alanine (<scp>L</scp>-Dopa) Using<i>Erwinia herbicola</i>Cells Carrying a Mutant Transcriptional Regulator TyrR

Koyanagi, Takashi; Katayama, Takane; Suzuki, Hideyuki; Onishi, Akira; Yokozeki, Kenzo; Kumagai, Hidehiko

doi:10.1271/bbb.90019

Cited by 20 publications

(10 citation statements)

References 11 publications

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“…In the second step, TTPL from thermophilic microorganism S. toebii [5b], was selected for the C–C coupling reaction, since it is much more stable than TPLs from Citrobacter freundii and Erwinia herbicola . However, we found the enzyme has a very narrow substrate scope, which failed to catalyze the conversion of phenol derivatives of interest such as o ‐chlorophenol 3d , o ‐bromophenol 3e , o ‐methylphenol 3f , and guaiacol 3g (Table ).…”

Section: Resultsmentioning

confidence: 99%

Biocascade Synthesis of L‐Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol‐Lyase and L‐Lactate Oxidase

Lian

Xue

et al. 2020

Eur J Org Chem

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A one‐pot biocascade of two enzymatic steps catalyzed by an l‐lactate oxidase and a tyrosine phenol‐lyase has been successfully developed in the present study. The reaction provides an efficient method for the synthesis of l‐tyrosine derivatives, which exhibits readily available starting materials and excellent yields. In the first step, an in situ generation of pyruvate from readily available bio‐based l‐lactate catalyzed by a highly active l‐lactate oxidase from Aerococcus viridans (AvLOX) was developed (using oxygen as oxidant and catalase as hydrogen peroxide removing reagent). Pyruvate thus produced underwent C–C coupling with phenol derivatives as acceptor substrate using specially designed thermophilic tyrosine phenol‐lyase mutants from Symbiobacterium toebii (TTPL). Overall, this cascade avoids the high cost and easy decomposition of pyruvate and offered an efficient and environmentally friendly procedure for l‐tyrosine derivatives synthesis.

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Section: Resultsmentioning

confidence: 99%

Biocascade Synthesis of L‐Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol‐Lyase and L‐Lactate Oxidase

Lian

Xue

et al. 2020

Eur J Org Chem

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“…In addition to showing that both σ S and Lrp contribute to the regulation of stlA expression, we have also shown that a LysR-type transcriptional regulator, TyrR, is absolutely required for the expression of stlA . TyrR has been shown to regulate the expression of genes involved in aromatic amino acid metabolism and transport in a number of bacteria, including E. coli , Shewanella and Erwinia [ 31 , 51 , 52 ]. The activity of TyrR in E. coli is itself modulated by the presence and/or absence of aromatic amino acids [ 30 , 31 , 53 ].…”

Section: Discussionmentioning

confidence: 99%

The Expression of stlA in Photorhabdus luminescens Is Controlled by Nutrient Limitation

et al. 2013

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Photorhabdus is a genus of Gram-negative entomopathogenic bacteria that also maintain a mutualistic association with nematodes from the family Heterorhabditis. Photorhabdus has an extensive secondary metabolism that is required for the interaction between the bacteria and the nematode. A major component of this secondary metabolism is a stilbene molecule, called ST. The first step in ST biosynthesis is the non-oxidative deamination of phenylalanine resulting in the production of cinnamic acid. This reaction is catalyzed by phenylalanine-ammonium lyase, an enzyme encoded by the stlA gene. In this study we show, using a stlA-gfp transcriptional fusion, that the expression of stlA is regulated by nutrient limitation through a regulatory network that involves at least 3 regulators. We show that TyrR, a LysR-type transcriptional regulator that regulates gene expression in response to aromatic amino acids in E. coli, is absolutely required for stlA expression. We also show that stlA expression is modulated by σS and Lrp, regulators that are implicated in the regulation of the response to nutrient limitation in other bacteria. This work is the first that describes pathway-specific regulation of secondary metabolism in Photorhabdus and, therefore, our study provides an initial insight into the complex regulatory network that controls secondary metabolism, and therefore mutualism, in this model organism.

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“…Therefore, it is necessary to solve the separation difficulties caused by the addition of l-tyrosine. Consequently, Koyanagi et al [34] found that the induced expression of TPL was regulated by TyrR protein and randomly mutagenized it. Eventually, a mutant reduced the dependence of l-tyrosine, but a certain amount of l-tyrosine should be added in this process.…”

Section: Discussionmentioning

confidence: 99%

Constitutive expression of tyrosine phenol-lyase from Erwinia herbicola in Escherichia coli for l-DOPA production

Tang

Bai

Fan

et al. 2021

Syst Microbiol and Biomanuf

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l-DOPA is a major drug for the treatment of Parkinson's disease, and microbial enzymatic synthesis is an essential way for its industrial production. The expression of tyrosine phenol-lyase (TPL) derived from Erwinia herbicola under six different constitutive promoters in Escherichia coli was studied. The recombinant strain 5 can express TPL well with growth. The optimal medium composition of this strain was as follows: tryptone 18 g/L, yeast extract 28 g/L, glycerol 10 g/L. After the cell culture is completed, the collected cells were used to catalyze the production of l-DOPA, and the concentration can reach 67.9 g/L.

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Hyperproduction of 3,4-Dihydroxyphenyl-L-alanine (L-Dopa) UsingErwinia herbicolaCells Carrying a Mutant Transcriptional Regulator TyrR

Cited by 20 publications

References 11 publications

Biocascade Synthesis of L‐Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol‐Lyase and L‐Lactate Oxidase

Biocascade Synthesis of L‐Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol‐Lyase and L‐Lactate Oxidase

The Expression of stlA in Photorhabdus luminescens Is Controlled by Nutrient Limitation

Constitutive expression of tyrosine phenol-lyase from Erwinia herbicola in Escherichia coli for l-DOPA production

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