scholarly journals Identification of Phenylalanine 3-Hydroxylase formeta-Tyrosine Biosynthesis

Biochemistry ◽  
2011 ◽  
Vol 50 (24) ◽  
pp. 5401-5403 ◽  
Author(s):  
Wenjun Zhang ◽  
Brian D. Ames ◽  
Christopher T. Walsh
Keyword(s):  
Tyrosine Biosynthesis

scholarly journals Biosynthesis of resveratrol derivatives and evaluation of their anti-inflammatory activity

2021 ◽  
Vol 64 (1) ◽  
Author(s):  
Yoojin Chong ◽  
Hye Lim Lee ◽  
Jihyeon Song ◽  
Youngshim Lee ◽  
Bong-Gyu Kim ◽  
...  
Keyword(s):  
Biological Activities ◽  
Stilbene Synthase ◽  
Inflammatory Activity ◽  
E Coli ◽  
Prephenate Dehydrogenase ◽  
Coa Ligase ◽  
Final Yield ◽  
Resveratrol Derivatives ◽  
Anti Inflammatory ◽  
Tyrosine Biosynthesis

AbstractResveratrol is a typical plant phenolic compound whose derivatives are synthesized through hydroxylation, O-methylation, prenylation, and oligomerization. Resveratrol and its derivatives exhibit anti-neurodegenerative, anti-rheumatoid, and anti-inflammatory effects. Owing to the diverse biological activities of these compounds and their importance in human health, this study attempted to synthesize five resveratrol derivatives (isorhapontigenin, pterostilbene, 4-methoxyresveratrol, piceatannol, and rhapontigenin) using Escherichia coli. Two-culture system was used to improve the final yield of resveratrol derivatives. Resveratrol was synthesized in the first E. coli cell that harbored genes for resveratrol biosynthesis including TAL (tyrosine ammonia lyase), 4CL (4-coumaroyl CoA ligase), STS (stilbene synthase) and genes for tyrosine biosynthesis such as aroG (deoxyphosphoheptonate aldolase) and tyrA (prephenate dehydrogenase). Thereafter, culture filtrate from the first cell was used for the modification reaction carried out using the second E. coli harboring hydroxylase and/or O-methyltransferase. Approximately, 89.8 mg/L of resveratrol was synthesized and using the same, five derivatives were prepared with a conversion rate of 88.2% to 22.9%. Using these synthesized resveratrol derivatives, we evaluated their anti-inflammatory activity. 4-Methoxyresveratrol, pterostilbene and isorhapontigenin showed the anti-inflammatory effects without any toxicity. In addition, pterostilbene exhibited the enhanced anti-inflammatory effects for macrophages compared to resveratrol.

Phenylalanine and Tyrosine Biosynthesis in Sporeforming Members of the Order Actinomycetales

1987 ◽  
Vol 42 (4) ◽  
pp. 387-393 ◽  
Author(s):  
Hilda-K. Hund ◽  
Brigitte Keller ◽  
Franz Lingens
Keyword(s):  
Anion Exchange ◽  
Deae Cellulose ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Chorismate Mutase ◽  
Biosynthetic Enzymes ◽  
Prephenate Dehydratase ◽  
Prephenate Dehydrogenase ◽  
Arogenate Dehydrogenase ◽  
Tyrosine Biosynthesis

Abstract The enzymes of the terminal steps of phenylalanine and tyrosine biosynthesis, chorismate mutase, prephenate dehydratase, arogenate dehydratase, prephenate dehydrogenase and aroge­ nate dehydrogenase were studied in 13 sporeforming members of the order Actinomycetales. In these organisms tyrosine is synthesized exclusively via arogenate, phenylalanine, however, via phenylpyruvate. The regulation pattern of the corresponding enzymes was determined: No feed­ back inhibition of arogenate dehydrogenase by L-phenylalanine and ʟ-tyrosine was observed. Chorismate mutase was found to be inhibited in all organisms by ʟ-tyrosine and in most organisms by ʟ-tryptophan. ʟ-Phenylalanine was shown to inhibit prephenate dehydratase in the majority of bacteria tested and ʟ-tyrosine activated this enzyme in most cases. The elution profiles for the phenylalanine and tyrosine biosynthetic enzymes were studied in three members of the order Actinomycetales by anion exchange chromatography on DEAE-cellulose.

Tyrosine Biosynthesis in Sorghum bicolor: Characteristics of Prephenate Aminotransferase

1986 ◽  
Vol 41 (1-2) ◽  
pp. 79-86 ◽  
Author(s):  
Daniel L. Siehl ◽  
James A. Connelly ◽  
Eric E. Conn
Keyword(s):  
Reaction Rate ◽  
Deae Cellulose ◽  
Forward Direction ◽  
Reverse Direction ◽  
Aminotransferase Activity ◽  
Forward Reaction ◽  
High Affinity ◽  
Sorghum Plant ◽  
Arogenate Dehydrogenase ◽  
Tyrosine Biosynthesis

Abstract A stable activity which transfers the amino group from glutamate to prephenate was extracted from 4-day old etiolated shoots of sorghum. The activity was retained on DEAE cellulose and eluted as a single peak. Prephenate aminotransferase co-eluted with a very abundant α-ketoglutarate: aspartate aminotransferase, but heating at 70 °C resulted in loss of α-ketoglutarate: aspar­tate activity with nearly full retention of prephenate: glutamate aminotransferase activity. The heated enzyme displayed high affinity and specificity for prephenate. Among 7 donors tested, only glutamate, and aspartate at less than 20% the rate with glutamate, supported prephenate aminotransferase activity. In the reverse direction, a reaction rate comparable to that in the forward direction was unchanged as the concentration of α-ketoglutarate was reduced from 1.0 to 0.09 mᴍ. The apparent Km for arogenate was 0.8 mᴍ. The forward reaction was unaffected by the inclusion of tyrosine, phenylalanine or tryptophan. Together with the discovery of arogenate dehydrogenase in sorghum [3], these data indicate that, in the sorghum plant, tyrosine derives from prephenate by transamination and aromatization. rather than the reverse sequence.

scholarly journals The Tyrosine Aminomutase TAM1 Is Required for β-Tyrosine Biosynthesis in Rice

2015 ◽  
Vol 27 (4) ◽  
pp. 1265-1278 ◽  
Author(s):  
Jian Yan ◽  
Takako Aboshi ◽  
Masayoshi Teraishi ◽  
Susan R. Strickler ◽  
Jennifer E. Spindel ◽  
...  
Keyword(s):  
Tyrosine Biosynthesis

scholarly journals Simultaneous Multiplex Genome Engineering via Accelerated Natural Transformation in Bacillus subtilis

2021 ◽  
Vol 12 ◽  
Author(s):  
Aihua Deng ◽  
Zhaopeng Sun ◽  
Tiantian Wang ◽  
Di Cui ◽  
Lai Li ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Synthetic Biology ◽  
High Throughput Screening ◽  
Large Scale ◽  
Genome Engineering ◽  
Natural Transformation ◽  
Efficient Design ◽  
Accelerated Evolution ◽  
One Step ◽  
Tyrosine Biosynthesis

Multiplex engineering at the scale of whole genomes has become increasingly important for synthetic biology and biotechnology applications. Although several methods have been reported for engineering microbe genomes, their use is limited by their complex procedures using multi-cycle transformations. Natural transformation, involving in species evolution by horizontal gene transfer in many organisms, indicates its potential as a genetic tool. Here, we aimed to develop simultaneous multiplex genome engineering (SMGE) for the simple, rapid, and efficient design of bacterial genomes via one-step of natural transformation in Bacillus subtilis. The transformed DNA, competency factors, and recombinases were adapted to improved co-editing frequencies above 27-fold. Single to octuplet variants with genetic diversity were simultaneously generated using all-in-one vectors harboring multi-gene cassettes. To demonstrate its potential application, the tyrosine biosynthesis pathway was further optimized for producing commercially important resveratrol by high-throughput screening of variant pool in B. subtilis. SMGE represents an accelerated evolution platform that generates diverse multiplex mutations for large-scale genetic engineering and synthetic biology in B. subtilis.

scholarly journals Microbiome-Specific Statistical Modeling Identifies Interplay Between Gastrointestinal Microbiome and Neurobehavioral Outcomes in Patients With Autism: A Case Control Study

2021 ◽  
Vol 12 ◽  
Author(s):  
Minshi Huang ◽  
Jun Liu ◽  
Kevin Liu ◽  
Jierong Chen ◽  
Zhen Wei ◽  
...  
Keyword(s):  
Dietary Habits ◽  
Neurodevelopmental Disorder ◽  
Gastrointestinal Symptoms ◽  
Autism Spectrum ◽  
Case Control ◽  
Living Environment ◽  
Degree Relative ◽  
Gastrointestinal Microbiome ◽  
Core Symptoms ◽  
Tyrosine Biosynthesis

Autism Spectrum Disorder (ASD) is a neurodevelopmental disorder with unclear mechanisms of pathogenesis. Gastrointestinal microbiome alterations were found to correlate with ASD core symptoms, but its specific role in ASD pathogenesis has not been determined. In this study, we used a case-control strategy that simultaneously compared the ASD gastrointestinal microbiome with that from age-sex matched controls and first-degree relative controls, using a statistical framework accounting for confounders such as age. Enterobacteriaceae (including Escherichia/Shigella) and Phyllobacterium were significantly enriched in the ASD group, with their relative abundances all following a pattern of ASD > first degree relative control > healthy control, consistent with our hypothesis of living environment and shared microbial and immunological exposures as key drivers of ASD gastrointestinal microbiome dysbiosis. Using multivariable omnibus testing, we identified clinical factors including ADOS scores, dietary habits, and gastrointestinal symptoms that covary with overall microbiome structure within the ASD cohort. A microbiome-specific multivariate modeling approach (MaAsLin2) demonstrated microbial taxa, such as Lachnoclostridium and Tyzzerella, are significantly associated with ASD core symptoms measured by ADOS. Finally, we identified alterations in predicted biological functions, including tryptophan and tyrosine biosynthesis/metabolism potentially relevant to the pathophysiology of the gut-brain-axis. Overall, our results identified gastrointestinal microbiome signature changes in patients with ASD, highlighted associations between gastrointestinal microbiome and clinical characteristics related to the gut-brain axis and identified contributors to the heterogeneity of gastrointestinal microbiome within the ASD population.

scholarly journals tyrR, A Regulatory Gene of Tyrosine Biosynthesis in Salmonella typhimurium

1973 ◽  
Vol 115 (3) ◽  
pp. 1094-1102 ◽  
Author(s):  
E. G. Gollub ◽  
K. P. Liu ◽  
D. B. Sprinson
Keyword(s):  
Salmonella Typhimurium ◽  
Regulatory Gene ◽  
Tyrosine Biosynthesis

scholarly journals Enzymology of l-Tyrosine Biosynthesis in Mung Bean (Vigna radiata [L.] Wilczek)

1979 ◽  
Vol 64 (5) ◽  
pp. 727-734 ◽  
Author(s):  
Judith L. Rubin ◽  
Roy A. Jensen
Keyword(s):  
Vigna Radiata ◽  
Mung Bean ◽  
Tyrosine Biosynthesis
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