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[PMID]:29178637
[Au] Autor:Majumdar R; Yori A; Rush PW; Raymond K; Gavrilov D; Tortorelli S; Matern D; Rinaldo P; Feldman GL; Oglesbee D
[Ad] Endereço:Mayo Clinic College of Medicine, Rochester, Minnesota.
[Ti] Título:Allelic spectrum of formiminotransferase-cyclodeaminase gene variants in individuals with formiminoglutamic aciduria.
[So] Source:Mol Genet Genomic Med;5(6):795-799, 2017 11.
[Is] ISSN:2324-9269
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Elevated plasma and urine formiminoglutamic acid (FIGLU) levels are commonly indicative of formiminoglutamic aciduria (OMIM #229100), a poorly understood autosomal recessive disorder of histidine and folate metabolism, resulting from formiminotransferase-cyclodeaminase (FTCD) deficiency, a bifunctional enzyme encoded by FTCD. METHODS: In order to further understanding about the molecular alterations that contribute to FIGLU-uria, we sequenced FTCD in 20 individuals with putative FTCD deficiency and varying laboratory findings, including increased FIGLU excretion. RESULTS: Individuals tested had biallelic loss-of-function variants in protein-coding regions of FTCD. The FTCD allelic spectrum comprised of 12 distinct variants including 5 missense alterations that replace conserved amino acid residues (c.223A>C, c.266A>G, c.319T>C, c.430G>A, c.514G>T), an in-frame deletion (c.1373_1375delTGG), with the remaining alterations predicted to affect mRNA processing/stability. These included two frameshift variants (c.990dup, c.1366dup) and four nonsense variants (c.337C>T, c.451A>T, c.763C>T, c.1607T>A). CONCLUSION: We observed additional FTCD alleles leading to urinary FIGLU elevations, and thus, providing molecular evidence of FTCD deficiency in cases identified by newborn screening or clinical biochemical genetic laboratory testing.
[Mh] Termos MeSH primário: Amônia-Liases/genética
Glutamato Formimidoiltransferase/deficiência
Erros Inatos do Metabolismo/genética
[Mh] Termos MeSH secundário: Alelos
Sequência de Aminoácidos
Códon sem Sentido
Mutação da Fase de Leitura
Deleção de Genes
Genótipo
Glutamato Formimidoiltransferase/genética
Seres Humanos
Erros Inatos do Metabolismo/diagnóstico
Mutação de Sentido Incorreto
Fases de Leitura Aberta/genética
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); EC 2.1.2.5 (Glutamate Formimidoyltransferase); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.4 (formiminotetrahydrofolate cyclodeaminase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1002/mgg3.333


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[PMID]:28347340
[Au] Autor:Ying H; Tao S; Wang J; Ma W; Chen K; Wang X; Ouyang P
[Ad] Endereço:State Key Laboratory of Materials Oriented Chemical Engineering, Nanjing, 211816, People's Republic of China.
[Ti] Título:Expanding metabolic pathway for de novo biosynthesis of the chiral pharmaceutical intermediate L-pipecolic acid in Escherichia coli.
[So] Source:Microb Cell Fact;16(1):52, 2017 Mar 27.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The six-carbon circular non-proteinogenic compound L-pipecolic acid is an important chiral drug intermediate with many applications in the pharmaceutical industry. In the present study, we developed a metabolically engineered strain of Escherichia coli for the overproduction of L-pipecolic acid from glucose. RESULTS: The metabolic pathway from L-lysine to L-pipecolic acid was constructed initially by introducing lysine cyclodeaminase (LCD). Next, L-lysine metabolic flux from glucose was amplified by the plasmid-based overexpression of dapA, lysC, and lysA under the control of the strong trc promoter to increase the biosynthetic pool of the precursor L-lysine. Additionally, since the catalytic efficiency of the key enzyme LCD is limited by the cofactor NAD , the intracellular pyridine nucleotide concentration was rebalanced by expressing the pntAB gene encoding the transhydrogenase, which elevated the proportion of LCD with bound NAD and enhanced L-pipecolic acid production significantly. Further, optimization of Fe and surfactant in the fermentation process resulted in 5.33 g/L L-pipecolic acid, with a yield of 0.13 g/g of glucose via fed-batch cultivation. CONCLUSIONS: We expanded the metabolic pathway for the synthesis of the chiral pharmaceutical intermediate L-pipecolic acid in E. coli. Using the engineered E. coli, a fast and efficient fermentative production of L-pipecolic acid was achieved. This strategy could be applied to the biosynthesis of other commercially and industrially important chiral compounds containing piperidine rings.
[Mh] Termos MeSH primário: Escherichia coli/genética
Escherichia coli/metabolismo
Engenharia Metabólica/métodos
Redes e Vias Metabólicas/genética
Ácidos Pipecólicos/metabolismo
[Mh] Termos MeSH secundário: Amônia-Liases/genética
Técnicas de Cultura Celular por Lotes
Proteínas de Escherichia coli/genética
Fermentação
Expressão Gênica
Glucose/metabolismo
NAD/metabolismo
NADP Trans-Hidrogenases/genética
Ácidos Pipecólicos/química
Plasmídeos
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Pipecolic Acids); 0U46U6E8UK (NAD); EC 1.6.1.- (NADP Transhydrogenases); EC 1.6.1.2 (pntB protein, E coli); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (lysine cyclodeaminase); H254GW7PVV (pipecolic acid); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0666-0


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[PMID]:28274102
[Au] Autor:Kim EJ; Cha MN; Kim BG; Ahn JH
[Ad] Endereço:Department of Integrative Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul 05029, Republic of Korea.
[Ti] Título:Production of Curcuminoids in .
[So] Source:J Microbiol Biotechnol;27(5):975-982, 2017 May 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:Curcumin, a hydrophobic polyphenol derived from the rhizome of the herb , possesses diverse pharmacological properties, including anti-inflammatory, antioxidant, antiproliferative, and antiangiogenic activities. Two curcuminoids (dicinnamoylmethane and bisdemethoxycurcumin) were synthesized from glucose in . (phenylalanine ammonia lyase) or (tyrosine ammonia lyase), along with ( -coumaroyl-CoA ligase) and (curcumin synthase) genes, were introduced into , and each strain produced dicinnamoylmethane or bisdemethoxycurcumin, respectively. In order to increase the production of curcuminoids in , the shikimic acid biosynthesis pathway, which increases the substrates for curcuminoid biosynthesis, was engineered. Using the engineered strains, the production of bisdemethoxycurcumin increased from 0.32 to 4.63 mg/l, and that of dicinnamoylmethane from 1.24 to 6.95 mg/l.
[Mh] Termos MeSH primário: Curcumina/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Engenharia Metabólica/métodos
[Mh] Termos MeSH secundário: Amônia-Liases/genética
Amônia-Liases/metabolismo
Arabidopsis/genética
Vias Biossintéticas/genética
Meios de Cultura
Curcumina/análogos & derivados
Curcumina/química
Regulação Bacteriana da Expressão Gênica
Glucose/metabolismo
Microbiologia Industrial
Ligases/genética
Ligases/metabolismo
Fenilalanina Amônia-Liase/genética
Fenilalanina Amônia-Liase/metabolismo
Ácido Chiquímico/metabolismo
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (dicinnamoylmethane); 29MS2WI2NU (Shikimic Acid); 2EFO1BP34R (bis(4-hydroxycinnamoyl)methane); 42HK56048U (Tyrosine); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); EC 4.3.1.24 (Phenylalanine Ammonia-Lyase); EC 6.- (Ligases); EC 6.- (curcuminoid synthase, Curcuma longa); IT942ZTH98 (Curcumin); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1701.01030


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[PMID]:28202018
[Au] Autor:Heo KT; Kang SY; Hong YS
[Ad] Endereço:Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, 30 Yeongudanji-ro, Ochang-eup, Chungbuk, 363-883, Republic of Korea.
[Ti] Título:De novo biosynthesis of pterostilbene in an Escherichia coli strain using a new resveratrol O-methyltransferase from Arabidopsis.
[So] Source:Microb Cell Fact;16(1):30, 2017 Feb 15.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pterostilbene, a structural analog of resveratrol, has higher oral bioavailability and bioactivity than that of the parent compound; but is far less abundant in natural sources. Thus, to efficiently obtain this bioactive resveratrol analog, it is necessary to develop new bioproduction systems. RESULTS: We identified a resveratrol O-methyltransferase (ROMT) function from a multifunctional caffeic acid O-methyltransferase (COMT) originating from Arabidopsis, which catalyzes the transfer of a methyl group to resveratrol resulting in pterostilbene production. In addition, we constructed a biological platform to produce pterostilbene with this ROMT gene. Pterostilbene can be synthesized from intracellular L-tyrosine, which requires the activities of four enzymes: tyrosine ammonia lyase (TAL), p-coumarate:CoA ligase (CCL), stilbene synthase (STS) and resveratrol O-methyltransferase (ROMT). For the efficient production of pterostilbene in E. coli, we used an engineered E. coli strain to increase the intracellular pool of L-tyrosine, which is the initial precursor of pterostilbene. Next, we tried to produce pterostilbene in the engineered E. coli strain using L-methionine containing media, which is used to increase the intracellular pool of S-adenosyl-L-methionine (SAM). According to this result, pterostilbene production as high as 33.6 ± 4.1 mg/L was achieved, which was about 3.6-fold higher compared with that in the parental E. coli strain harboring a plasmid for pterostilbene biosynthesis. CONCLUSION: As a potential phytonutrient, pterostilbene was successfully produced in E. coli from a glucose medium using a single vector system, and its production titer was also significantly increased using a L-methionine containing medium in combination with a strain that had an engineered metabolic pathway for L-tyrosine. Additionally, we provide insights into the dual functions of COMT from A. thaliana which was characterized as a ROMT enzyme.
[Mh] Termos MeSH primário: Arabidopsis/enzimologia
Escherichia coli/genética
Engenharia Metabólica/métodos
Metiltransferases/genética
Metiltransferases/metabolismo
Estilbenos/metabolismo
[Mh] Termos MeSH secundário: Aciltransferases/metabolismo
Amônia-Liases/metabolismo
Biocatálise
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Escherichia coli/metabolismo
Redes e Vias Metabólicas
Metionina/farmacologia
S-Adenosilmetionina/metabolismo
Estilbenos/química
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Stilbenes); 26R60S6A5I (pterostilbene); 42HK56048U (Tyrosine); 7LP2MPO46S (S-Adenosylmethionine); AE28F7PNPL (Methionine); EC 2.1.1.- (Methyltransferases); EC 2.1.1.68 (caffeate O-methyltransferase); EC 2.3.- (Acyltransferases); EC 2.3.1.- (stilbene synthase); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); Q369O8926L (resveratrol)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0644-6


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[PMID]:28071035
[Au] Autor:Swieca M
[Ad] Endereço:Department of Biochemistry and Food Chemistry, University of Life Sciences in Lublin, Poland.
[Ti] Título:Elicitation and treatment with precursors of phenolics synthesis improve low-molecular antioxidants and antioxidant capacity of buckwheat sprouts.
[So] Source:Acta Sci Pol Technol Aliment;15(1):17-28, 2016 Jan-Mar.
[Is] ISSN:1898-9594
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Recently, an increase of interest in the modification of food products on each step of production (breeding, production technology, storage condition) is observed. Nutritional properties as well as level and activity of bioactive compounds in plant-origin food may be modified using a range of technological and biotechnological practices and elicitation should be mentioned between them. METHODS: Elicitation with willow bark infusion supported by feeding with the phenylpropanoid pathway precursors were used for improving the quality of buckwheat sprouts. Special emphasis has been placed on the metabolomic and biochemical changes and the mechanism of overproduction of low-molecular antioxidants. RESULTS: The accumulation of phenolics is caused by stimulation of two main enzymes the phenylpropanoid pathway (tyrosine ammonia-lyase and phenylalanine ammonia-lyase). Tyrosine ammonia-lyase activities were effectively induced by feeding with tyrosine (about four times that of the control), whereas phenylalanine ammonia-lyase activity was the highest in the elicited control sprouts and those fed with shikimic acid (an increase by 60% compared to the control). Shikimic acid feeding (both elicited and non-elicited sprouts) effectively improved the total phenolics (by about 10% and 20%, respectively), condensed tannins (by about 30% and 28%, respectively), and flavonoids (by about 46% and 70%, respectively). Significant increase of vitexin, rutin, chlorogenic acid and isoorientin contents was also observed. The treatments increased the ascorbic acid content, too. Total antioxidant capacity of sprouts was most effectively increased by feeding with shikimic acid and further elicitation. CONCLUSIONS: The studies transfer biotechnology commonly used for the induction of overproduction of secondary metabolites in plant cell line systems to low-processed food production. The obtained results could be used for better understanding of the effect of elicitation and precursor feeding on antioxidants production and contribute to improving the buckwheat sprouts quality.
[Mh] Termos MeSH primário: Amônia-Liases/biossíntese
Antioxidantes/metabolismo
Fagopyrum/metabolismo
Flavonoides/biossíntese
Fenilalanina Amônia-Liase/biossíntese
Plântulas/metabolismo
Ácido Chiquímico/metabolismo
[Mh] Termos MeSH secundário: Agroquímicos/metabolismo
Amônia-Liases/química
Antioxidantes/análise
Antioxidantes/química
Ácido Ascórbico/análise
Ácido Ascórbico/biossíntese
Ácido Clorogênico/análise
Ácido Clorogênico/metabolismo
Indução Enzimática
Fagopyrum/química
Fagopyrum/crescimento & desenvolvimento
Flavonoides/análise
Qualidade dos Alimentos
Alimentos Orgânicos/análise
Hidroponia
Peso Molecular
Fenilalanina Amônia-Liase/química
Casca de Planta/química
Extratos Vegetais/metabolismo
Proteínas de Plantas/agonistas
Proteínas de Plantas/biossíntese
Polônia
Proantocianidinas/análise
Proantocianidinas/biossíntese
Salix/química
Plântulas/química
Plântulas/crescimento & desenvolvimento
Tirosina/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Agrochemicals); 0 (Antioxidants); 0 (Flavonoids); 0 (Plant Extracts); 0 (Plant Proteins); 0 (Proanthocyanidins); 29MS2WI2NU (Shikimic Acid); 318ADP12RI (Chlorogenic Acid); 42HK56048U (Tyrosine); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); EC 4.3.1.24 (Phenylalanine Ammonia-Lyase); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170111
[St] Status:MEDLINE
[do] DOI:10.17306/J.AFS.2016.1.2


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[PMID]:27401923
[Au] Autor:Zhou S; Liu P; Chen J; Du G; Li H; Zhou J
[Ad] Endereço:Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.
[Ti] Título:Characterization of mutants of a tyrosine ammonia-lyase from Rhodotorula glutinis.
[So] Source:Appl Microbiol Biotechnol;100(24):10443-10452, 2016 Dec.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In the phenylpropanoid production process, p-coumaric acid is the most important intermediate metabolite. It is generally accepted that the activity of tyrosine ammonia-lyase (TAL), which converts L-tyrosine to p-coumaric acid, represents the rate-limiting step. Therefore, an error-prone PCR-based random mutagenesis strategy was utilized for screening variants with higher catalytic activity. After rounds of screening, three variant enzymes were obtained, exhibiting improved production rates of 41.2, 37.1, and 38.0 %, respectively. Variants associated with increased expression level (S9N), improved catalytic efficiency (A11T), and enhanced affinity between TAL and L-tyrosine (E518V) were identified as beneficial amino acid substitutions by site-directed mutagenesis. Combining all of the beneficial amino acid substitutions, a variant, MT-S9N/-A11T/-E518V, exhibiting the highest catalytic activity was obtained. The K value of MT-S9N/-A11T/-E518V decreased by 25.4 % compare to that of wild-type, while the activity, k /K , and p-coumaric-acid yield were improved by 36.5, 31.2, and 65.9 %, respectively. Furthermore, the secondary structure of the 5'-end of MT-S9N mRNA and the three-dimensional protein structure of MT-E518V were modeled. Therefore, two potential mechanisms were speculated: (1) a simplified mRNA 5'-end secondary structure promotes TAL expression and (2) anchoring the flexible loop region (Glu325-Arg336) to maintain the active-site pocket opening ensures easy access by the L-tyrosine to the active site and thus improves p-coumaric acid yields.
[Mh] Termos MeSH primário: Amônia-Liases/genética
Amônia-Liases/metabolismo
Proteínas Mutantes/genética
Proteínas Mutantes/metabolismo
Rhodotorula/enzimologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Amônia-Liases/química
Biotransformação
Ácidos Cumáricos/metabolismo
Cinética
Modelos Moleculares
Mutagênese
Proteínas Mutantes/química
Reação em Cadeia da Polimerase
Propionatos
Conformação Proteica
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coumaric Acids); 0 (Mutant Proteins); 0 (Propionates); 42HK56048U (Tyrosine); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); IBS9D1EU3J (trans-3-(4'-hydroxyphenyl)-2-propenoic acid)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160713
[St] Status:MEDLINE


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[PMID]:27331921
[Au] Autor:Wang J; Liang S; Ma H; Zhang P; Shi W
[Ad] Endereço:College of Life Science, Northwest Agriculture and Forestry Univ, Yangling, Shaanxi, 712100, China.
[Ti] Título:Effects of Ethephon on Fresh In-Husk Walnut Preservation and its Possible Relationship with Phenol Metabolism.
[So] Source:J Food Sci;81(8):C1921-7, 2016 Aug.
[Is] ISSN:1750-3841
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fresh walnuts (Juglans regia L.) are in demand due to their high nutrition value and unique flavor of the kernel. In this study the effects of ethephon on decay control and kernel quality of fresh walnuts and its possible relationship with phenolic metabolism were investigated. Fresh in-husk walnuts treated with 0, 10, 500, and 800 mg/L ethephon were stored at 0 ± 0.5 °C for 42 d. Decay incidence, total phenolic (TP) compounds, phenylalanine ammonialyase (PAL), polyphenol-oxidase (PPO), and peroxidase (POD) activities of green husks, and acid values (AV) and peroxide values (PV) of kernels were assessed at 6-d intervals. The respiration rate of the whole walnut was assessed at 3-d intervals. Treatment with 500 mg/L ethephon enhanced respiration, reduced the decay index, and inhibited PPO and POD activity and browning of green husks, and also promoted PAL activity and TP content of green husks. This treatment also reduced the PV and AV of kernels. A concentration of 10 mg/L ethephonhad similar, but weaker, effects on walnuts. Treatment with 8000 mg/L ethephon, however, had opposite effects. These data indicate ethephon treatment at a proper concentration can extend storage life and maintain kernel quality of fresh in-husk walnuts through the manipulation of phenolic metabolism.
[Mh] Termos MeSH primário: Manipulação de Alimentos/métodos
Conservação de Alimentos/métodos
Juglans
Nozes/efeitos dos fármacos
Compostos Organofosforados/farmacologia
Fenóis/metabolismo
Reguladores de Crescimento de Planta/farmacologia
[Mh] Termos MeSH secundário: Amônia-Liases/metabolismo
Catecol Oxidase/metabolismo
Seres Humanos
Nozes/metabolismo
Oxirredução
Peroxidase/metabolismo
Fenilalanina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organophosphorus Compounds); 0 (Phenols); 0 (Plant Growth Regulators); 47E5O17Y3R (Phenylalanine); EC 1.10.3.1 (Catechol Oxidase); EC 1.11.1.7 (Peroxidase); EC 4.3.1.- (Ammonia-Lyases); XU5R5VQ87S (ethephon)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160623
[St] Status:MEDLINE
[do] DOI:10.1111/1750-3841.13370


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[PMID]:27206340
[Au] Autor:Fujiwara R; Noda S; Kawai Y; Tanaka T; Kondo A
[Ad] Endereço:Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan.
[Ti] Título:4-Vinylphenol production from glucose using recombinant Streptomyces mobaraense expressing a tyrosine ammonia lyase from Rhodobacter sphaeroides.
[So] Source:Biotechnol Lett;38(9):1543-9, 2016 Sep.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To find a novel host for the production of 4-vinylphenol (4VPh) by screening Streptomyces species. RESULTS: The conversion of p-coumaric acid (pHCA) to 4VPh in Streptomyces mobaraense was evaluated using a medium containing pHCA. S. mobaraense readily assimilated pHCA after 24 h of cultivation to produce 4VPh. A phenolic acid decarboxylase, derived from S. mobaraense (SmPAD), was purified following heterologous expression in Escherichia coli. SmPAD was evaluated under various conditions, and the enzyme's kcat/Km value was 0.54 mM (-1) s(-1). Using intergenetic conjugation, a gene from Rhodobacter sphaeroides encoding a tyrosine ammonia lyase, which catalyzes the conversion of L-tyrosine to p-coumaric acid, was introduced into S. mobaraense. The resulting S. mobaraense transformant produced 273 mg 4VPh l(-1) from 10 g glucose l(-1). CONCLUSION: A novel strain suitable for the production of 4VPh and potentially other aromatic compounds was isolated.
[Mh] Termos MeSH primário: Amônia-Liases/metabolismo
Glucose/metabolismo
Fenóis/metabolismo
Rhodobacter sphaeroides/enzimologia
Streptomyces/enzimologia
Streptomyces/metabolismo
[Mh] Termos MeSH secundário: Amônia-Liases/genética
Ácidos Cumáricos/metabolismo
Propionatos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coumaric Acids); 0 (Phenols); 0 (Propionates); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); IBS9D1EU3J (trans-3-(4'-hydroxyphenyl)-2-propenoic acid); IY9XDZ35W2 (Glucose); OA7V1SM8YL (4-vinylphenol)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160522
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2126-z


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[PMID]:27010356
[Au] Autor:Ernst DC; Anderson ME; Downs DM
[Ad] Endereço:Department of Microbiology, University of Georgia, Athens, GA, 30602-2605, USA.
[Ti] Título:L-2,3-diaminopropionate generates diverse metabolic stresses in Salmonella enterica.
[So] Source:Mol Microbiol;101(2):210-23, 2016 Jul.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Unchecked amino acid accumulation in living cells has the potential to cause stress by disrupting normal metabolic processes. Thus, many organisms have evolved degradation strategies that prevent endogenous accumulation of amino acids. L-2,3-diaminopropionate (Dap) is a non-protein amino acid produced in nature where it serves as a precursor to siderophores, neurotoxins and antibiotics. Dap accumulation in Salmonella enterica was previously shown to inhibit growth by unknown mechanisms. The production of diaminopropionate ammonia-lyase (DpaL) alleviated Dap toxicity in S. enterica by catalyzing the degradation of Dap to pyruvate and ammonia. Here, we demonstrate that Dap accumulation in S. enterica elicits a proline requirement for growth and specifically inhibits coenzyme A and isoleucine biosynthesis. Additionally, we establish that the DpaL-dependent degradation of Dap to pyruvate proceeds through an unbound 2-aminoacrylate (2AA) intermediate, thus contributing to 2AA stress inside the cell. The reactive intermediate deaminase, RidA, is shown to prevent 2AA damage caused by DpaL-dependent Dap degradation by enhancing the rate of 2AA hydrolysis. The results presented herein inform our understanding of the effects Dap has on metabolism in S. enterica, and likely other organisms, and highlight the critical role played by RidA in preventing 2AA stress stemming from Dap detoxification.
[Mh] Termos MeSH primário: Amônia-Liases/química
Amônia-Liases/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Aminoidrolases/metabolismo
Amônia-Liases/efeitos dos fármacos
Amônia-Liases/farmacologia
Proteínas de Bactérias/metabolismo
Prolina/biossíntese
Prolina/metabolismo
Ácido Pirúvico/metabolismo
Salmonella enterica/metabolismo
Estresse Fisiológico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Bacterial Proteins); 8558G7RUTR (Pyruvic Acid); 9DLQ4CIU6V (Proline); EC 3.5.4.- (Aminohydrolases); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (diaminopropionate ammonia-lyase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160325
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13384


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[PMID]:26845578
[Au] Autor:Tantong S; Incharoensakdi A; Sirikantaramas S; Lindblad P
[Ad] Endereço:Program in Biotechnology, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand; Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand. Electronic address: supaluk.tan@student.chula.ac.th.
[Ti] Título:Potential of Synechocystis PCC 6803 as a novel cyanobacterial chassis for heterologous expression of enzymes in the trans-resveratrol biosynthetic pathway.
[So] Source:Protein Expr Purif;121:163-8, 2016 May.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selected model strains of phototrophic cyanobacteria have been genetically engineered for heterologous expression of numerous enzymes. In the present study, we initially explored the heterologous expression of enzymes involved in trans-resveratrol production, namely, the production of tyrosine ammonia-lyase, coumaroyl CoA-ligase, and stilbene synthase, in the unicellular cyanobacterium Synechocystis PCC 6803. Under the promoters Ptrc1Ocore and Ptrc1O, the respective genes were transcribed and translated into the corresponding soluble proteins at concentrations of 16-34 µg L(-1). The expression levels of these enzymes did not affect the growth rate of the cyanobacterial cells. Interestingly, coumaroyl CoA-ligase expression slightly increased the chlorophyll a content of the cells. Overall, our results suggest that the complete pathway of trans-resveratrol production can be engineered in Synechocystis PCC 6803.
[Mh] Termos MeSH primário: Vias Biossintéticas
Estilbenos/metabolismo
Synechocystis/genética
[Mh] Termos MeSH secundário: Aciltransferases/biossíntese
Aciltransferases/genética
Amônia-Liases/biossíntese
Amônia-Liases/genética
Expressão Gênica
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Stilbenes); EC 2.3.- (Acyltransferases); EC 2.3.1.- (resveratrol synthase); EC 2.3.1.- (stilbene synthase); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.- (L-tyrosine ammonia-lyase); Q369O8926L (resveratrol)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160205
[St] Status:MEDLINE



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