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Pesquisa : D08.811.520.224.900 [Categoria DeCS]
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  1 / 103 MEDLINE  
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[PMID]:26804162
[Au] Autor:Thompson B; Machas M; Nielsen DR
[Ad] Endereço:Chemical Engineering, School for Engineering of Matter, Transport, and Energy, University of Arizona State, Tempe, Arizona.
[Ti] Título:Engineering and comparison of non-natural pathways for microbial phenol production.
[So] Source:Biotechnol Bioeng;113(8):1745-54, 2016 Aug.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The non-renewable petrochemical phenol is used as a precursor to produce numerous fine and commodity chemicals, including various pharmaceuticals and phenolic resins. Microbial phenol biosynthesis has previously been established, stemming from endogenous tyrosine via tyrosine phenol lyase (TPL). TPL, however, suffers from feedback inhibition and equilibrium limitations, both of which contribute to reduced flux through the overall pathway. To address these limitations, two novel and non-natural phenol biosynthesis pathways, both stemming instead from chorismate, were constructed and comparatively evaluated. The first proceeds to phenol in one heterologous step via the intermediate p-hydroxybenzoic acid, while the second involves two heterologous steps and the associated intermediates isochorismate and salicylate. Maximum phenol titers achieved via these two alternative pathways reached as high as 377 ± 14 and 259 ± 31 mg/L in batch shake flask cultures, respectively. In contrast, under analogous conditions, phenol production via the established TPL-dependent route reached 377 ± 23 mg/L, which approaches the maximum achievable output reported to date under batch conditions. Additional strain development and optimization of relevant culture conditions with respect to each individual pathway is ultimately expected to result in further improved phenol production. Biotechnol. Bioeng. 2016;113: 1745-1754. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Bactérias/genética
Engenharia Metabólica/métodos
Fenol/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Técnicas de Cultura Celular por Lotes
Escherichia coli/genética
Escherichia coli/metabolismo
Glucose/metabolismo
Redes e Vias Metabólicas
Tirosina/metabolismo
Tirosina Fenol-Liase/genética
Tirosina Fenol-Liase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 339NCG44TV (Phenol); 42HK56048U (Tyrosine); EC 4.1.99.2 (Tyrosine Phenol-Lyase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE
[do] DOI:10.1002/bit.25942


  2 / 103 MEDLINE  
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[PMID]:25615531
[Au] Autor:Phillips RS
[Ad] Endereço:Department of Chemistry, University of Georgia, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA. Electronic address: plp@uga.edu.
[Ti] Título:Chemistry and diversity of pyridoxal-5'-phosphate dependent enzymes.
[So] Source:Biochim Biophys Acta;1854(9):1167-74, 2015 Sep.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pyridoxal-5'-phosphate (PLP) is a versatile cofactor that enzymes use to catalyze a wide variety of reactions of amino acids, including transamination, decarboxylation, racemization, ß- and γ-eliminations and substitutions, retro-aldol and Claisen reactions. These reactions depend on the ability of PLP to stabilize, to a varying degree, α-carbanionic intermediates. Furthermore, oxidative decarboxylations and rearrangements suggest that PLP can stabilize radical intermediates as well. The reaction mechanisms of two PLP-dependent enzymes are discussed, kynureninase and tyrosine phenol-lyase (TPL). Kynureninase catalyzes a retro-Claisen reaction of kynurenine to give anthranilate and alanine. The key step, hydration of the γ-carbonyl, is assisted by acid-base catalysis with the phosphate of the PLP, mediated by a conserved tyrosine, and an oxyanion hole. TPL catalyzes the reversible elimination of phenol, a poor leaving group, from l-tyrosine. In TPL, the Cß-Cγ bond cleavage is accelerated by ground state strain from the bending of the substrate ring out of the plane with the Cß-Cγ bond. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications.
[Mh] Termos MeSH primário: Hidrolases/química
Fosfato de Piridoxal/fisiologia
Tirosina Fenol-Liase/química
[Mh] Termos MeSH secundário: Catálise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
5V5IOJ8338 (Pyridoxal Phosphate); EC 3.- (Hydrolases); EC 3.7.1.3 (kynureninase); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150124
[St] Status:MEDLINE


  3 / 103 MEDLINE  
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[PMID]:25432672
[Au] Autor:Min K; Park K; Park DH; Yoo YJ
[Ad] Endereço:Clean Energy Research Center, Korea Institute of Science and Technology, Seoul, 136-791, South Korea.
[Ti] Título:Overview on the biotechnological production of L-DOPA.
[So] Source:Appl Microbiol Biotechnol;99(2):575-84, 2015 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:L-DOPA (3,4-dihydroxyphenyl-L-alanine) has been widely used as a drug for Parkinson's disease caused by deficiency of the neurotransmitter dopamine. Since Monsanto developed the commercial process for L-DOPA synthesis for the first time, most of currently supplied L-DOPA has been produced by the asymmetric method, especially asymmetric hydrogenation. However, the asymmetric synthesis shows critical limitations such as a poor conversion rate and a low enantioselectivity. Accordingly, alternative biotechnological approaches have been researched for overcoming the shortcomings: microbial fermentation using microorganisms with tyrosinase, tyrosine phenol-lyase, or p-hydroxyphenylacetate 3-hydroxylase activity and enzymatic conversion by immobilized tyrosinase. Actually, Ajinomoto Co. Ltd commercialized Erwinia herbicola fermentation to produce L-DOPA from catechol. In addition, the electroenzymatic conversion system was recently introduced as a newly emerging scheme. In this review, we aim to not only overview the biotechnological L-DOPA production methods, but also to briefly compare and analyze their advantages and drawbacks. Furthermore, we suggest the future potential of biotechnological L-DOPA production as an industrial process.
[Mh] Termos MeSH primário: Biotecnologia/métodos
Erwinia/enzimologia
Levodopa/biossíntese
[Mh] Termos MeSH secundário: Enzimas Imobilizadas/metabolismo
Fermentação
Oxigenases de Função Mista/metabolismo
Monofenol Mono-Oxigenase/metabolismo
Tirosina Fenol-Liase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 46627O600J (Levodopa); EC 1.- (Mixed Function Oxygenases); EC 1.14.18.1 (Monophenol Monooxygenase); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150126
[Lr] Data última revisão:
150126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141130
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-014-6215-4


  4 / 103 MEDLINE  
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[PMID]:25035301
[Au] Autor:Phillips RS; Demidkina TV; Faleev NG
[Ad] Endereço:Department of Chemistry, University of Georgia, Athens, GA 30602, USA; Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA. Electronic address: plp@uga.edu.
[Ti] Título:The role of substrate strain in the mechanism of the carbon-carbon lyases.
[So] Source:Bioorg Chem;57:198-205, 2014 Dec.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The carbon-carbon lyases, tryptophan indole lyase (TIL) and tyrosine phenol-lyase (TPL) are bacterial enzymes which catalyze the reversible elimination of indole and phenol from l-tryptophan and l-tyrosine, respectively. These PLP-dependent enzymes show high sequence homology (∼40% identity) and both form homotetrameric structures. Steady state kinetic studies with both enzymes show that an active site base is essential for activity, and α-deuterated substrates exhibit modest primary isotope effects on kcat and kcat/Km, suggesting that substrate deprotonation is partially rate-limiting. Pre-steady state kinetics with TPL and TIL show rapid formation of external aldimine intermediates, followed by deprotonation to give quinonoid intermediates absorbing at about 500nm. In the presence of phenol and indole analogues, 4-hydroxypyridine and benzimidazole, the quinonoid intermediates of TPL and TIL decay to aminoacrylate intermediates, with λmax at about 340nm. Surprisingly, there are significant kinetic isotope effects on both formation and subsequent decay of the quinonoid intermediates when α-deuterated substrates are used. The crystal structure of TPL with a bound competitive inhibitor, 4-hydroxyphenylpropionate, identified several essential catalytic residues: Tyr-71, Thr-124, Arg-381, and Phe-448. The active sites of TIL and TPL are highly conserved with the exceptions of these residues: Arg-381(TPL)/Ile-396 (TIL); Thr-124 (TPL)/Asp-137 (TIL), and Phe-448 (TPL)/His-463 (TIL). Mutagenesis of these residues results in dramatic decreases in catalytic activity without changing substrate specificity. The conserved tyrosine, Tyr-71 (TPL)/Tyr-74 (TIL) is essential for elimination activity with both enzymes, and likely plays a role as a proton donor to the leaving group. Mutation of Arg-381 and Thr-124 of TPL to alanine results in very low but measurable catalytic activity. Crystallography of Y71F and F448H TPL with 3-fluoro-l-tyrosine bound demonstrated that there are two quinonoid structures, relaxed and tense. In the relaxed structure, the substrate aromatic ring is in plane with the Cß-Cγ bond, but in the tense structure, the substrate aromatic ring is about 20° out of plane with the Cß-Cγ bond. In the tense structure, hydrogen bonds are formed between the substrate OH and the guanidinium of Arg-381 and the OH of Thr-124, and the phenyl rings of Phe-448 and 449 provide steric strain. Based on the effects of mutagenesis, the substrate strain is estimated to contribute about 10(8) to TPL catalysis. Thus, the mechanisms of TPL and TIL require both substrate strain and acid/base catalysis, and substrate strain is probably responsible for the very high substrate specificity of TPL and TIL.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Triptofanase/metabolismo
Tirosina Fenol-Liase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bactérias/química
Bactérias/metabolismo
Cristalografia
Modelos Moleculares
Dados de Sequência Molecular
Alinhamento de Sequência
Especificidade por Substrato
Triptofanase/química
Tirosina Fenol-Liase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
EC 4.1.99.1 (Tryptophanase); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140719
[St] Status:MEDLINE


  5 / 103 MEDLINE  
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[PMID]:24022778
[Au] Autor:Chandel M; Azmi W
[Ti] Título:Purification and characterization of tyrosine phenol lyase from Citrobacter freundii.
[So] Source:Appl Biochem Biotechnol;171(8):2040-52, 2013 Dec.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified tyrosine phenol lyase showed maximum activity in borate buffer (0.05 M at pH 8.5) at 45 °C after 20 min of incubation. The Km and Vmax values of purified enzyme were found to be 0.446 mm and 0.342 mM/min/mg. This enzyme exhibits t1/2 of 10, 52 and 130 min at 55, 45 and 35 °C, respectively. The N-terminal amino acid sequence was determined as MET-ASN-TYR-PRO-ALA-GLU-PRO-PHE-ARG-ILETRP- TRP-VAL-GLY.
[Mh] Termos MeSH primário: Citrobacter freundii/enzimologia
Tirosina Fenol-Liase/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Dipeptídeos/química
Cinética
Peso Molecular
Tirosina Fenol-Liase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dipeptides); 1238-09-1 (phenylalanylarginine); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:140108
[Lr] Data última revisão:
140108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130912
[St] Status:MEDLINE


  6 / 103 MEDLINE  
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[PMID]:23827746
[Au] Autor:Azmi W; Kumar A; Dev V
[Ad] Endereço:Department of Biotechnology, Himachal Pradesh University, Summer-Hill, Shimla 171005, India. wamikazmi@rediffmail.com
[Ti] Título:Paraffin as oxygen vector modulates tyrosine phenol lyase production by Citrobacter freundii MTCC 2424.
[So] Source:Acta Microbiol Immunol Hung;60(2):145-54, 2013 Jun.
[Is] ISSN:1217-8950
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:The efficiency of three oxygen-vectors liquid paraffin, silicone oil and n-dodecane in the production of tyrosine phenol lyase (TPL) by Citrobacter freundii MTCC 2424 was evaluated at 4% (v/v) concentration. The liquid paraffin as oxygenvectors was found to exhibit a stimulatory effect on TPL synthesis. The liquid paraffin at 6% (v/v) resulted in 34% increase in the TPL synthesis accompanied by a 13% increase in the production of cell mass at a 10 L scale. This improvement in TPL and cell mass production in the presence of liquid paraffin can be related to the fact that liquid paraffin was capable of maintaining dissolved O2 concentration above 28% throughout the course of the fermentation. Maintenance of the dissolved O2 concentration above 28% could be viewed in terms of an adequate oxygen supply to the rapidly dividing cells of the bacterium, which in turn resulted in enhanced synthesis of TPL and cell mass.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Técnicas de Cultura Celular por Lotes/métodos
Citrobacter freundii/enzimologia
Oxigênio/metabolismo
Parafina/análise
Tirosina Fenol-Liase/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Técnicas de Cultura Celular por Lotes/instrumentação
Citrobacter freundii/genética
Fermentação
Tirosina Fenol-Liase/genética
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 8002-74-2 (Paraffin); EC 4.1.99.2 (Tyrosine Phenol-Lyase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130706
[St] Status:MEDLINE
[do] DOI:10.1556/AMicr.60.2013.2.5


  7 / 103 MEDLINE  
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[PMID]:23554162
[Au] Autor:Liu X; Li J; Hu C; Zhou Q; Zhang W; Hu M; Zhou J; Wang J
[Ad] Endereço:Laboratory of Non-coding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.
[Ti] Título:Significant expansion of the fluorescent protein chromophore through the genetic incorporation of a metal-chelating unnatural amino acid.
[So] Source:Angew Chem Int Ed Engl;52(18):4805-9, 2013 Apr 26.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Mh] Termos MeSH primário: Aminoácidos/química
Quelantes/química
Proteínas Luminescentes/química
[Mh] Termos MeSH secundário: Alanina/química
Alanina/metabolismo
Aminoácidos/metabolismo
Domínio Catalítico
Citrobacter freundii/enzimologia
Transferência Ressonante de Energia de Fluorescência
Hidroxiquinolinas/química
Proteínas Luminescentes/metabolismo
Metais/química
Mutação
Espectrofotometria Ultravioleta
Tirosina Fenol-Liase/química
Tirosina Fenol-Liase/genética
Tirosina Fenol-Liase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Chelating Agents); 0 (Hydroxyquinolines); 0 (Luminescent Proteins); 0 (Metals); EC 4.1.99.2 (Tyrosine Phenol-Lyase); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130405
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201301307


  8 / 103 MEDLINE  
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[PMID]:21899319
[Au] Autor:Milic D; Demidkina TV; Faleev NG; Phillips RS; Matkovic-Calogovic D; Antson AA
[Ad] Endereço:Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, HR-10000 Zagreb, Croatia. dmilic@chem.pmf.hr
[Ti] Título:Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage.
[So] Source:J Am Chem Soc;133(41):16468-76, 2011 Oct 19.
[Is] ISSN:1520-5126
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The key step in the enzymatic reaction catalyzed by tyrosine phenol-lyase (TPL) is reversible cleavage of the Cß-Cγ bond of L-tyrosine. Here, we present X-ray structures for two enzymatic states that form just before and after the cleavage of the carbon-carbon bond. As for most other pyridoxal 5'-phosphate-dependent enzymes, the first state, a quinonoid intermediate, is central for the catalysis. We captured this relatively unstable intermediate in the crystalline state by introducing substitutions Y71F or F448H in Citrobacter freundii TPL and briefly soaking crystals of the mutant enzymes with a substrate 3-fluoro-L-tyrosine followed by flash-cooling. The X-ray structures, determined at ~2.0 Å resolution, reveal two quinonoid geometries: "relaxed" in the open and "tense" in the closed state of the active site. The "tense" state is characterized by changes in enzyme contacts made with the substrate's phenolic moiety, which result in significantly strained conformation at Cß and Cγ positions. We also captured, at 2.25 Å resolution, the X-ray structure for the state just after the substrate's Cß-Cγ bond cleavage by preparing the ternary complex between TPL, alanine quinonoid and pyridine N-oxide, which mimics the α-aminoacrylate intermediate with bound phenol. In this state, the enzyme-ligand contacts remain almost exactly the same as in the "tense" quinonoid, indicating that the strain induced by the closure of the active site facilitates elimination of phenol. Taken together, structural observations demonstrate that the enzyme serves not only to stabilize the transition state but also to destabilize the ground state.
[Mh] Termos MeSH primário: Quinonas/metabolismo
Tirosina Fenol-Liase/química
Tirosina Fenol-Liase/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Domínio Catalítico
Citrobacter freundii/enzimologia
Cristalografia por Raios X
Modelos Moleculares
Conformação Molecular
Quinonas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Quinones); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110909
[St] Status:MEDLINE
[do] DOI:10.1021/ja203361g


  9 / 103 MEDLINE  
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[PMID]:21740012
[Au] Autor:Tanz N; Werner RA; Eisenreich W; Schmidt HL
[Ad] Endereço:isolab GmbH, Woelkestrasse 9/I, D-85301 Schweitenkirchen, Germany.
[Ti] Título:Assessment of enzymatic methods in the δ18O value determination of the L-tyrosine p-hydroxy group for proof of illegal meat and bone meal feeding to cattle.
[So] Source:J Agric Food Chem;59(17):9475-83, 2011 Sep 14.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The δ(18)O value of the p-hydroxy group of L-tyrosine depends on the biosynthesis by plants or animals, respectively. In animal proteins it reflects the diet and is therefore an absolute indicator for illegal feeding with meat and bone meal. The aim of this investigation was to perform the positional (18)O determination on L-tyrosine via a one-step enzymatic degradation. Proteins from plants, herbivores, omnivores, and carnivores were characterized by their δ(13)C, δ(15)N, and δ(18)O values, the latter for normalizing the positional δ(18)O values. Their L-tyrosine was degraded by tyrosine phenol lyase to phenol, analyzed as (2,4,6)-tribromophenol. Degradation by tyrosine decarboxylase yielded tyramine. The δ(18)O values of both analytes corresponded to the trophic levels of their sources but were not identical, probably due to an isotope effect on the tyrosine phenol lyase reaction. Availability of the enzyme, easy control of the reaction, and isolation of the analyte are in favor of tyrosine decarboxylase degradation as a routine method.
[Mh] Termos MeSH primário: Ração Animal/análise
Legislação sobre Alimentos
Carne
Minerais
Isótopos de Oxigênio
Tirosina/química
[Mh] Termos MeSH secundário: Animais
Produtos Biológicos
Bovinos
Proteínas na Dieta/análise
Encefalopatia Espongiforme Bovina/prevenção & controle
Encefalopatia Espongiforme Bovina/transmissão
Contaminação de Alimentos/análise
Isótopos de Oxigênio/análise
Isótopos de Oxigênio/química
Fenóis/química
Fenóis/metabolismo
Tirosina/metabolismo
Tirosina Descarboxilase/metabolismo
Tirosina Fenol-Liase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biological Products); 0 (Dietary Proteins); 0 (Minerals); 0 (Oxygen Isotopes); 0 (Phenols); 42HK56048U (Tyrosine); EC 4.1.1.25 (Tyrosine Decarboxylase); EC 4.1.99.2 (Tyrosine Phenol-Lyase); TRS31EO6ZN (bone meal)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110712
[St] Status:MEDLINE
[do] DOI:10.1021/jf201217r


  10 / 103 MEDLINE  
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[PMID]:21111764
[Au] Autor:Kim NJ; Choi JH; Kim YC; Lee J; Lee SY; Chang HN; Lee PC
[Ad] Endereço:Department of Chemical and Biomolecular Engineering (BK21 Program), Bioinformatics Research Center, BioProcess Engineering Research Center and Center for Ultramicrochemical Process Systems, KAIST, 335 Gwahangno, Yuseong-gu, Daejeon 305-701, Republic of Korea.
[Ti] Título:Development of anaerobically inducible nar promoter expression vectors for the expression of recombinant proteins in Escherichia coli.
[So] Source:J Biotechnol;151(1):102-7, 2011 Jan 10.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Dissolved oxygen (DO)-controlled nar promoter expression vectors were constructed, and their expression efficiency was compared with that of the T7 promoter pET22 expression vector by expressing human growth hormone (hGH), enhanced green fluorescence protein (EGFP), and ß-tyrosinase in Escherichia coli cells. The nar promoter expression vector pRBS, which was engineered with a 5'-untranslated region and ribosomal binding site for the T7 promoter, expressed hGH at a rate of up to 32% of the total cellular proteins (TCP) in E. coli W3110narL⁻. The expression level of hGH was further enhanced, up to ~42% of the TCP, by adding the N-terminal peptide tag of ß-galactosidase to hGH, which was comparable to the expression of ~43% of the TCP in pET-lac:hGH/BL21(DE3). A further engineered expression vector, pRBS(fnr), which coexpressed fumarate/nitrate reductase (fnr), expressed more EGFP than pET22 in BL21(DE3). In addition, recombinant ß-tyrosinase was successfully expressed at a rate of up to ~45% of the TCP in pRBS(fnr) in W3110narL⁻. From these results, the DO-controlled nar promoter system developed in this study can be considered a reliable and cost-effective expression system for protein production, especially in large-scale fermentation, as an alternative to the pET/BL(DE3) system.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Vetores Genéticos/genética
Regiões Promotoras Genéticas/genética
Proteínas Recombinantes/biossíntese
[Mh] Termos MeSH secundário: Anaerobiose
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Engenharia Genética/métodos
Proteínas de Fluorescência Verde/química
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Hormônio do Crescimento Humano/química
Hormônio do Crescimento Humano/genética
Hormônio do Crescimento Humano/metabolismo
Seres Humanos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Tirosina Fenol-Liase/química
Tirosina Fenol-Liase/genética
Tirosina Fenol-Liase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (enhanced green fluorescent protein); 12629-01-5 (Human Growth Hormone); 147336-22-9 (Green Fluorescent Proteins); EC 4.1.99.2 (Tyrosine Phenol-Lyase)
[Em] Mês de entrada:1104
[Cu] Atualização por classe:110103
[Lr] Data última revisão:
110103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101130
[St] Status:MEDLINE
[do] DOI:10.1016/j.jbiotec.2010.11.010



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