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  1 / 169 MEDLINE  
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[PMID]:28650068
[Au] Autor:Chen Z; Shen X; Wang J; Wang J; Yuan Q; Yan Y
[Ad] Endereço:State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, 15 Beisanhuan East Road, Chaoyang District, Beijing, 100029, China.
[Ti] Título:Rational engineering of p-hydroxybenzoate hydroxylase to enable efficient gallic acid synthesis via a novel artificial biosynthetic pathway.
[So] Source:Biotechnol Bioeng;114(11):2571-2580, 2017 Nov.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gallic acid (GA) is a naturally occurring phytochemical that has strong antioxidant and antibacterial activities. It is also used as a potential platform chemical for the synthesis of diverse high-value compounds. Hydrolytic degradation of tannins by acids, bases or microorganisms serves as a major way for GA production, which however, might cause environmental pollution and low yield and efficiency. Here, we report a novel approach for efficient microbial production of GA. First, structure-based rational engineering of PobA, a p-hydroxybenzoate hydroxylase from Pseudomonas aeruginosa, generated a new mutant, Y385F/T294A PobA, which displayed much higher activity toward 3,4-dihydroxybenzoic acid (3,4-DHBA) than the wild-type and any other reported mutants. Remarkably, expression of this mutant in Escherichia coli enabled generation of 1149.59 mg/L GA from 1000 mg/L 4-hydroxybenzoic acid (4-HBA), representing a 93% molar conversion ratio. Based on that, we designed and reconstituted a novel artificial biosynthetic pathway of GA and achieved 440.53 mg/L GA production from simple carbon sources in E. coli. Further enhancement of precursor supply through reinforcing shikimate pathway was able to improve GA de novo production to 1266.39 mg/L in shake flasks. Overall, this study not only led to the development of a highly active PobA variant for hydroxylating 3,4-DHBA into GA via structure-based protein engineering approach, but also demonstrated a promising pathway for bio-based manufacturing of GA and its derived compounds. Biotechnol. Bioeng. 2017;114: 2571-2580. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/genética
Vias Biossintéticas/genética
Escherichia coli/fisiologia
Ácido Gálico/metabolismo
Melhoramento Genético/métodos
Engenharia Metabólica/métodos
Engenharia de Proteínas/métodos
[Mh] Termos MeSH secundário: Ácido Gálico/isolamento & purificação
Pseudomonas aeruginosa/enzimologia
Pseudomonas aeruginosa/genética
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
632XD903SP (Gallic Acid); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26364


  2 / 169 MEDLINE  
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[PMID]:26995683
[Au] Autor:Dalvi S; Youssef NH; Fathepure BZ
[Ad] Endereço:Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, USA.
[Ti] Título:Microbial community structure analysis of a benzoate-degrading halophilic archaeal enrichment.
[So] Source:Extremophiles;20(3):311-21, 2016 May.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A benzoate-degrading archaeal enrichment was developed using sediment samples from Rozel Point at Great Salt Lake, UT. The enrichment degraded benzoate as the sole carbon source at salinity ranging from 2.0 to 5.0 M NaCl with highest rate of degradation observed at 4.0 M. The enrichment was also tested for its ability to grow on other aromatic compounds such as 4-hydroxybenzoic acid (4-HBA), gentisic acid, protocatechuic acid (PCA), catechol, benzene and toluene as the sole sources of carbon and energy. Of these, the culture only utilized 4-HBA as the carbon source. To determine the initial steps in benzoate degradation pathway, a survey of ring-oxidizing and ring-cleaving genes was performed using degenerate PCR primers. Results showed the presence of 4-hydroxybenzoate 3-monooxygenase (4-HBMO) and protocatechuate 3, 4-dioxygenase (3,4-PCA) genes suggesting that the archaeal enrichment might degrade benzoate to 4-HBA that is further converted to PCA by 4-HBMO and, thus, formed PCA would undergo ring-cleavage by 3,4-PCA to form intermediates that enter the Krebs cycle. Small subunit rRNA gene-based diversity survey revealed that the enrichment consisted entirely of class Halobacteria members belonging to the genera Halopenitus, Halosarcina, Natronomonas, Halosimplex, Halorubrum, Salinarchaeum and Haloterrigena. Of these, Halopenitus was the dominant group accounting for almost 91 % of the total sequences suggesting their potential role in degrading oxygenated aromatic compounds at extreme salinity.
[Mh] Termos MeSH primário: Archaea/metabolismo
Benzoatos/metabolismo
Microbiota
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/genética
4-Hidroxibenzoato-3-Mono-Oxigenase/metabolismo
Archaea/genética
Archaea/isolamento & purificação
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Lagos/química
Lagos/microbiologia
Parabenos/metabolismo
Protocatecoate-3,4-Dioxigenase/genética
Protocatecoate-3,4-Dioxigenase/metabolismo
RNA Ribossômico/genética
Salinidade
Tolerância a Sal
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Benzoates); 0 (Parabens); 0 (RNA, Ribosomal); EC 1.13.11.3 (Protocatechuate-3,4-Dioxygenase); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase); JG8Z55Y12H (4-hydroxybenzoic acid)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:160321
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-016-0823-0


  3 / 169 MEDLINE  
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[PMID]:26574388
[Au] Autor:Sokkar P; Boulanger E; Thiel W; Sanchez-Garcia E
[Ad] Endereço:Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.
[Ti] Título:Hybrid Quantum Mechanics/Molecular Mechanics/Coarse Grained Modeling: A Triple-Resolution Approach for Biomolecular Systems.
[So] Source:J Chem Theory Comput;11(4):1809-18, 2015 Apr 14.
[Is] ISSN:1549-9626
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We present a hybrid quantum mechanics/molecular mechanics/coarse-grained (QM/MM/CG) multiresolution approach for solvated biomolecular systems. The chemically important active-site region is treated at the QM level. The biomolecular environment is described by an atomistic MM force field, and the solvent is modeled with the CG Martini force field using standard or polarizable (pol-CG) water. Interactions within the QM, MM, and CG regions, and between the QM and MM regions, are treated in the usual manner, whereas the CG-MM and CG-QM interactions are evaluated using the virtual sites approach. The accuracy and efficiency of our implementation is tested for two enzymes, chorismate mutase (CM) and p-hydroxybenzoate hydroxylase (PHBH). In CM, the QM/MM/CG potential energy scans along the reaction coordinate yield reaction energies that are too large, both for the standard and polarizable Martini CG water models, which can be attributed to adverse effects of using large CG water beads. The inclusion of an atomistic MM water layer (10 Å for uncharged CG water and 5 Å for polarizable CG water) around the QM region improves the energy profiles compared to the reference QM/MM calculations. In analogous QM/MM/CG calculations on PHBH, the use of the pol-CG description for the outer water does not affect the stabilization of the highly charged FADHOOH-pOHB transition state compared to the fully atomistic QM/MM calculations. Detailed performance analysis in a glycine-water model system indicates that computation times for QM energy and gradient evaluations at the density functional level are typically reduced by 40-70% for QM/MM/CG relative to fully atomistic QM/MM calculations.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/química
Corismato Mutase/química
Simulação de Dinâmica Molecular
Teoria Quântica
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/metabolismo
Corismato Mutase/metabolismo
Glicina/química
Termodinâmica
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
059QF0KO0R (Water); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase); EC 5.4.99.5 (Chorismate Mutase); TE7660XO1C (Glycine)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151117
[Lr] Data última revisão:
151117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151118
[St] Status:MEDLINE
[do] DOI:10.1021/ct500956u


  4 / 169 MEDLINE  
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[PMID]:24220759
[Au] Autor:Labroo P; Cui Y
[Ad] Endereço:Department of Biological Engineering, Utah State University, Logan, UT, 84322, USA.
[Ti] Título:Amperometric bienzyme screen-printed biosensor for the determination of leucine.
[So] Source:Anal Bioanal Chem;406(1):367-72, 2014 Jan.
[Is] ISSN:1618-2650
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Leucine plays an important role in protein synthesis, brain functions, building muscle mass, and helping the body when it undergoes stress. Here, we report a new amperometric bienzyme screen-printed biosensor for the determination of leucine, by coimmobilizing p-hydroxybenzoate hydroxylase (HBH) and leucine dehydrogenase (LDH) on a screen-printed electrode with NADP(+) and p-hydroxybenzoate as the cofactors. The detection principle of the sensor is that LDH catalyzes the specific dehydrogenation of leucine by using NADP(+) as a cofactor. The product, NADPH, triggers the hydroxylation of p-hydroxybenzoate by HBH in the presence of oxygen to produce 3,4-dihydroxybenzoate, which results in a change in electron concentration at the working carbon electrode, which is detected by the potentiostat. The sensor shows a linear detection range between 10 and 600 µM with a detection limit of 2 µM. The response is reproducible and has a fast measuring time of 5-10 s after the addition of a given concentration of leucine.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/química
Técnicas Biossensoriais
Leucina Desidrogenase/química
Leucina/sangue
[Mh] Termos MeSH secundário: Carbono/química
Técnicas Eletroquímicas
Eletrodos
Enzimas Imobilizadas/química
Seres Humanos
Limite de Detecção
NADP/química
Oxirredução
Parabenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Parabens); 53-59-8 (NADP); 7440-44-0 (Carbon); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase); EC 1.4.1.9 (Leucine Dehydrogenase); GMW67QNF9C (Leucine); JG8Z55Y12H (4-hydroxybenzoic acid)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:160512
[Lr] Data última revisão:
160512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131114
[St] Status:MEDLINE
[do] DOI:10.1007/s00216-013-7443-7


  5 / 169 MEDLINE  
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[PMID]:23766373
[Au] Autor:Suemori A
[Ad] Endereço:Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology-AIST, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan. suemori.akio@aist.go.jp
[Ti] Título:Conserved and non-conserved residues and their role in the structure and function of p-hydroxybenzoate hydroxylase.
[So] Source:Protein Eng Des Sel;26(7):479-88, 2013 Jul.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In order to elucidate the molecular mechanism of the catalytic reaction and enzyme conformation, we substituted 53 conserved residues identified by aligning 92 p-hydroxybenzoate hydroxylase sequences and 19 non-conserved residues selected from crystallographic studies of Pseudomonas fluorescens NBRC14160 p-hydroxybenzoate hydroxylase with 19 other naturally occurring amino acids, yielding a database of 619 active single mutants. The database contained 365 and 254 active single mutants for 44/53 conserved residues and 19 non-conserved residues, respectively; the data included main activity, sub-activity for NADPH and NADPH reaction specificity. Active mutations were not observed for the G14, Q102, G160, E198, R220, R246, N300, F342 and G387 conserved residues, and only one active mutant was obtained at the G9, G11, G187, D286, Y201, R214 and G295 conserved residues and the S13, E32 and R42 non-conserved residues. Only seven active mutants with higher activity than the wild-type enzyme were observed at conserved residues, and only two were observed at non-conserved residues. The 365 mutants at conserved residues included 64 active mutants with higher NADPH reaction specificity than the wild-type enzyme, and some Y181X single mutants exhibited considerable changes in NADPH reaction specificity. A Y181X/L268G double-mutant database was constructed to computationally analyze the effects of these substitutions on structural conformation and function. These results indicated that some conserved or non-conserved residues are important for structural stability or enzyme function.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/química
4-Hidroxibenzoato-3-Mono-Oxigenase/metabolismo
Pseudomonas fluorescens/enzimologia
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/genética
Sequência de Aminoácidos
Sítios de Ligação
Sequência Conservada
Modelos Moleculares
Mutagênese Sítio-Dirigida
NADP/metabolismo
Estrutura Secundária de Proteína
Pseudomonas fluorescens/metabolismo
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
53-59-8 (NADP); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:130626
[Lr] Data última revisão:
130626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130615
[St] Status:MEDLINE
[do] DOI:10.1093/protein/gzt026


  6 / 169 MEDLINE  
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[PMID]:22779576
[Au] Autor:Kästner J
[Ad] Endereço:Computational Biochemistry Group, Institute of Theoretical Chemistry, University of Stuttgart, Pfaffenwaldring 55, D-70569 Stuttgart, Germany.
[Ti] Título:Umbrella integration with higher-order correction terms.
[So] Source:J Chem Phys;136(23):234102, 2012 Jun 21.
[Is] ISSN:1089-7690
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Umbrella integration is a method to analyze umbrella sampling simulations. It calculates free-energy changes from distributions obtained from molecular dynamics. While it can be formulated on the full sampled distributions, they are generally approximated by normal distributions. This is equivalent to the truncation of a power series of the free energy with respect to the reaction coordinate after the quadratic term or by a truncation of a cumulant expansion. Here, expressions for additional terms in the power series are derived. They can be calculated from the central moments of the distributions. This extension allows to test the approximations in applications.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/química
Dipeptídeos/química
Termodinâmica
[Mh] Termos MeSH secundário: Algoritmos
Simulação de Dinâmica Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dipeptides); 2867-20-1 (alanylalanine); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:120711
[Lr] Data última revisão:
120711
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120712
[St] Status:MEDLINE
[do] DOI:10.1063/1.4729373


  7 / 169 MEDLINE  
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[PMID]:21439475
[Au] Autor:Alt S; Burkard N; Kulik A; Grond S; Heide L
[Ad] Endereço:Pharmazeutische Biologie, Pharmazeutisches Institut, Eberhard-Karls-Universität Tübingen, Auf der Morgenstelle 8, 72076 Tübingen, Germany.
[Ti] Título:An artificial pathway to 3,4-dihydroxybenzoic acid allows generation of new aminocoumarin antibiotic recognized by catechol transporters of E. coli.
[So] Source:Chem Biol;18(3):304-13, 2011 Mar 25.
[Is] ISSN:1879-1301
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An artificial operon was synthesized, consisting of the genes for chorismate pyruvate-lyase of E. coli and for 4-hydroxybenzoate 3-hydroxylase of Corynebacterium cyclohexanicum. This operon, directing the biosynthesis of 3,4-dihdroxybenzoate, was expressed in the heterologous expression host Streptomyces coelicolor M512, together with a modified biosynthetic gene cluster for the aminocoumarin antibiotic clorobiocin. The resulting strain produced a clorobiocin derivative containing a 3,4-dihdroxybenzoyl moiety. Its structure was confirmed by MS and NMR analysis, and it was found to be a potent inhibitor of the gyrases from Escherichia coli and Staphylococcus aureus. Bioassays against different E. coli mutants suggested that this compound is actively imported by catechol siderophore transporters in the cell envelope. This study provides an example of the structure of a natural product that can be rationally modified by synthetic biology.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Proteínas da Membrana Bacteriana Externa/metabolismo
Hidroxibenzoatos/metabolismo
Novobiocina/análogos & derivados
Receptores de Superfície Celular/metabolismo
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/genética
Antibacterianos/química
Antibacterianos/farmacologia
Corynebacterium/genética
DNA Girase/metabolismo
Testes de Sensibilidade a Antimicrobianos por Disco-Difusão
Escherichia coli/enzimologia
Escherichia coli/genética
Hidroxibenzoatos/química
Família Multigênica
Novobiocina/biossíntese
Novobiocina/química
Novobiocina/farmacologia
Oxo-Ácido-Liases/genética
Streptomyces coelicolor/genética
Streptomyces coelicolor/metabolismo
Inibidores da Topoisomerase II
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Outer Membrane Proteins); 0 (Hydroxybenzoates); 0 (Receptors, Cell Surface); 0 (Topoisomerase II Inhibitors); 0 (novobiocin 401); 0 (siderophore receptors); 17EC19951N (Novobiocin); 36R5QJ8L4B (protocatechuic acid); 39868-96-7 (clorobiocin); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase); EC 4.1.3.- (Oxo-Acid-Lyases); EC 4.1.3.- (chorismate pyruvate lyase); EC 5.99.1.3 (DNA Gyrase)
[Em] Mês de entrada:1107
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110329
[St] Status:MEDLINE
[do] DOI:10.1016/j.chembiol.2010.12.016


  8 / 169 MEDLINE  
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[PMID]:20055497
[Au] Autor:Ukaegbu UE; Kantz A; Beaton M; Gassner GT; Rosenzweig AC
[Ad] Endereço:Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
[Ti] Título:Structure and ligand binding properties of the epoxidase component of styrene monooxygenase .
[So] Source:Biochemistry;49(8):1678-88, 2010 Mar 02.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Styrene monooxygenase (SMO) is a two-component flavoprotein monooxygenase that transforms styrene to styrene oxide in the first step of the styrene catabolic and detoxification pathway of Pseudomonas putida S12. The crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains. The overall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are some significant differences in secondary structure. Structural comparisons suggest that a large cavity open to the surface forms the FAD binding site. At the base of this pocket is another cavity that likely represents the styrene binding site. Flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA approximately 8000 times more tightly than the oxidized coenzyme. Equilibrium fluorescence and isothermal titration calorimetry data using benzene as a substrate analogue indicate that the oxidized flavin and substrate analogue binding equilibria of NSMOA are linked such that the binding affinity of each is increased by 60-fold when the enzyme is saturated with the other. A much weaker approximately 2-fold positive cooperative interaction is observed for the linked binding equilibria of benzene and reduced FAD. The low affinity of the substrate analogue for the reduced FAD complex of NSMOA is consistent with a preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene, identifying the apoenzyme structure as the key catalytic resting state of NSMOA poised to bind reduced FAD and initiate the oxygen reaction.
[Mh] Termos MeSH primário: Oxirredutases/química
Oxirredutases/metabolismo
Oxigenases/química
Oxigenases/metabolismo
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/química
4-Hidroxibenzoato-3-Mono-Oxigenase/metabolismo
Sítios de Ligação
Calorimetria
Cristalografia por Raios X
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/metabolismo
Flavinas/química
Flavinas/metabolismo
Ligantes
Oxirredução
Multimerização Proteica
Estrutura Secundária de Proteína
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Flavins); 0 (Ligands); 146-14-5 (Flavin-Adenine Dinucleotide); EC 1.- (Oxidoreductases); EC 1.- (epoxidase); EC 1.13.- (Oxygenases); EC 1.13.- (styrene monooxygenase); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase)
[Em] Mês de entrada:1003
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100109
[St] Status:MEDLINE
[do] DOI:10.1021/bi901693u


  9 / 169 MEDLINE  
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[PMID]:19201803
[Au] Autor:Zimmermann T; Sorg T; Siehler SY; Gerischer U
[Ad] Endereço:Institute of Microbiology and Biotechnology, University of Ulm, D-89069 Ulm, Germany. ulrike.gerischer@uni-ulm.de
[Ti] Título:Role of Acinetobacter baylyi Crc in catabolite repression of enzymes for aromatic compound catabolism.
[So] Source:J Bacteriol;191(8):2834-42, 2009 Apr.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here, we describe for the first time the Crc (catabolite repression control) protein from the soil bacterium Acinetobacter baylyi. Expression of A. baylyi crc varied according to the growth conditions. A strain with a disrupted crc gene showed the same growth as the wild type on a number of carbon sources. Carbon catabolite repression by acetate and succinate of protocatechuate 3,4-dioxygenase, the key enzyme of protocatechuate breakdown, was strongly reduced in the crc strain, whereas in the wild-type strain it underwent strong catabolite repression. This strong effect was not based on transcriptional regulation because the transcription pattern of the pca-qui operon (encoding protocatechuate 3,4-dioxygenase) did not reflect the derepression in the absence of Crc. pca-qui transcript abundance was slightly increased in the crc strain. Lack of Crc dramatically increased the mRNA stability of the pca-qui transcript (up to 14-fold), whereas two other transcripts (pobA and catA) remained unaffected. p-Hydroxybenzoate hydroxylase activity, encoded by pobA, was not significantly different in the absence of Crc, as protocatechuate 3,4-dioxygenase was. It is proposed that A. baylyi Crc is involved in the determination of the transcript stability of the pca-qui operon and thereby effects catabolite repression.
[Mh] Termos MeSH primário: Acinetobacter/fisiologia
Proteínas de Bactérias/fisiologia
Regulação Bacteriana da Expressão Gênica
Hidrocarbonetos Aromáticos/metabolismo
Estabilidade de RNA
Proteínas Repressoras/fisiologia
[Mh] Termos MeSH secundário: 4-Hidroxibenzoato-3-Mono-Oxigenase/biossíntese
Ácido Acético/metabolismo
Acinetobacter/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Carbono/metabolismo
Repressão Enzimática
Enzimas/biossíntese
Deleção de Genes
Perfilação da Expressão Gênica
Modelos Biológicos
Dados de Sequência Molecular
Protocatecoate-3,4-Dioxigenase/biossíntese
Proteínas Repressoras/genética
Alinhamento de Sequência
Ácido Succínico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Enzymes); 0 (Hydrocarbons, Aromatic); 0 (Repressor Proteins); 138186-82-0 (FruR protein, Bacteria); 7440-44-0 (Carbon); AB6MNQ6J6L (Succinic Acid); EC 1.13.11.3 (Protocatechuate-3,4-Dioxygenase); EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:0904
[Cu] Atualização por classe:141210
[Lr] Data última revisão:
141210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090210
[St] Status:MEDLINE
[do] DOI:10.1128/JB.00817-08


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[PMID]:18205479
[Au] Autor:Mata RA; Werner HJ; Thiel S; Thiel W
[Ad] Endereço:Institut für Theoretische Chemie, Universität Stuttgart, Pfaffenwaldring 55, D-70569 Stuttgart, Germany.
[Ti] Título:Toward accurate barriers for enzymatic reactions: QM/MM case study on p-hydroxybenzoate hydroxylase.
[So] Source:J Chem Phys;128(2):025104, 2008 Jan 14.
[Is] ISSN:0021-9606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The hydroxylation reaction catalyzed by p-hydroxybenzoate hydroxylase has been investigated by quantum mechanical/molecular mechanical (QM/MM) calculations at different levels of QM theory. The solvated enzyme was modeled (approximately 23,000 atoms in total, 49 QM atoms). The geometries of reactant and transition state were optimized for ten representative pathways using semiempirical (AM1) and density functional (B3LYP) methods as QM components. Single-point calculations at B3LYP/MM optimized geometries were performed with local correlation methods [LMP2, LCCSD(T0)] and augmented triple-zeta basis sets. A careful validation of the latter approach with regard to all computational parameters indicates convergence of the QM contribution to the computed barriers to within approximately 1 kcal mol(-1). Comparison with the available experimental data supports this assessment.
[Mh] Termos MeSH primário: 4-Hidroxibenzoato-3-Mono-Oxigenase/metabolismo
Simulação por Computador
Teoria Quântica
[Mh] Termos MeSH secundário: Catálise
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.14.13.2 (4-Hydroxybenzoate-3-Monooxygenase)
[Em] Mês de entrada:0804
[Cu] Atualização por classe:080121
[Lr] Data última revisão:
080121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080122
[St] Status:MEDLINE
[do] DOI:10.1063/1.2823055



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