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Pesquisa : D08.811.913.050.134.700 [Categoria DeCS]
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[PMID]:29381705
[Au] Autor:Nag A; St John PC; Crowley MF; Bomble YJ
[Ad] Endereço:Computational Science Center, National Renewable Energy Laboratory, Golden, Colorado, United States of America.
[Ti] Título:Prediction of reaction knockouts to maximize succinate production by Actinobacillus succinogenes.
[So] Source:PLoS One;13(1):e0189144, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Succinate is a precursor of multiple commodity chemicals and bio-based succinate production is an active area of industrial bioengineering research. One of the most important microbial strains for bio-based production of succinate is the capnophilic gram-negative bacterium Actinobacillus succinogenes, which naturally produces succinate by a mixed-acid fermentative pathway. To engineer A. succinogenes to improve succinate yields during mixed acid fermentation, it is important to have a detailed understanding of the metabolic flux distribution in A. succinogenes when grown in suitable media. To this end, we have developed a detailed stoichiometric model of the A. succinogenes central metabolism that includes the biosynthetic pathways for the main components of biomass-namely glycogen, amino acids, DNA, RNA, lipids and UDP-N-Acetyl-α-D-glucosamine. We have validated our model by comparing model predictions generated via flux balance analysis with experimental results on mixed acid fermentation. Moreover, we have used the model to predict single and double reaction knockouts to maximize succinate production while maintaining growth viability. According to our model, succinate production can be maximized by knocking out either of the reactions catalyzed by the PTA (phosphate acetyltransferase) and ACK (acetyl kinase) enzymes, whereas the double knockouts of PEPCK (phosphoenolpyruvate carboxykinase) and PTA or PEPCK and ACK enzymes are the most effective in increasing succinate production.
[Mh] Termos MeSH primário: Actinobacillus/metabolismo
Técnicas de Silenciamento de Genes
Ácido Succínico/metabolismo
[Mh] Termos MeSH secundário: Actinobacillus/enzimologia
Actinobacillus/genética
Biomassa
Meios de Cultura
Fermentação
Modelos Biológicos
Fosfato Acetiltransferase/genética
Fosfato Acetiltransferase/metabolismo
Fosfoenolpiruvato Carboxiquinase (ATP)/genética
Fosfoenolpiruvato Carboxiquinase (ATP)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); AB6MNQ6J6L (Succinic Acid); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 4.1.1.49 (Phosphoenolpyruvate Carboxykinase (ATP))
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189144


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[PMID]:28130304
[Au] Autor:Kim JN; Burne RA
[Ad] Endereço:Department of Microbiology, College of Natural Sciences, Pusan National University, Busan, Republic of Korea.
[Ti] Título:CcpA and CodY Coordinate Acetate Metabolism in Streptococcus mutans.
[So] Source:Appl Environ Microbiol;83(7), 2017 Apr 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the dental caries pathogen , phosphotransacetylase (Pta) and acetate kinase (Ack) convert pyruvate into acetate with the concomitant generation of ATP. The genes for this pathway are tightly regulated by multiple environmental and intracellular inputs, but the basis for differential expression of the genes for Pta and Ack in had not been investigated. Here, we show that inactivation in of or reduced the activity of the promoter, whereas a mutant displayed elevated promoter activity. The interactions of CcpA with the promoter regions of both genes were observed using electrophoretic mobility shift and DNase protection assays. CodY bound to the promoter region but only in the presence of branched-chain amino acids (BCAAs). DNase footprinting revealed that the upstream region of both genes contains two catabolite-responsive elements ( and ) that can be bound by CcpA. Notably, the site of overlaps with a CodY-binding site. The CcpA- and CodY-binding sites in the promoter region of both genes were further defined by site-directed mutagenesis. Some differences between the reported consensus CodY binding site and the region protected by CodY were noted. Transcription of the and genes in the mutant strain was markedly different at low pH relative to transcription at neutral pH. Thus, CcpA and CodY are direct regulators of transcription of and in that optimize acetate metabolism in response to carbohydrate, amino acid availability, and environmental pH. The human dental caries pathogen is remarkably adept at coping with extended periods of carbohydrate limitation during fasting periods. The phosphotransacetylase-acetate kinase (Pta-Ack) pathway in modulates carbohydrate flux and fine-tunes the ability of the organisms to cope with stressors that are commonly encountered in the oral cavity. Here, we show that CcpA controls transcription of the and genes via direct interaction with the promoter regions of both genes and that branched-chain amino acids (BCAAs), particularly isoleucine, enhance the ability of CodY to bind to the promoter region of the gene. A working model is proposed to explain how regulation of and genes by these allosterically controlled regulatory proteins facilitates proper carbon flow and energy production, which are essential functions during infection and pathogenesis as carbohydrate and amino acid availability continually fluctuate.
[Mh] Termos MeSH primário: Acetatos/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Regulação Bacteriana da Expressão Gênica
Streptococcus mutans/genética
Streptococcus mutans/metabolismo
[Mh] Termos MeSH secundário: Acetato Quinase/genética
Aminoácidos de Cadeia Ramificada/metabolismo
Sítios de Ligação
Metabolismo dos Carboidratos
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Cárie Dentária/microbiologia
Concentração de Íons de Hidrogênio
Mutagênese Sítio-Dirigida
Fosfato Acetiltransferase/genética
Fosfato Acetiltransferase/metabolismo
Regiões Promotoras Genéticas
Ácido Pirúvico/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Amino Acids, Branched-Chain); 0 (Bacterial Proteins); 0 (DNA-Binding Proteins); 8558G7RUTR (Pyruvic Acid); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.1 (Acetate Kinase)
[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:170129
[St] Status:MEDLINE


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[PMID]:27999972
[Au] Autor:Chen Y; Liu M; Chen S; Wei X
[Ad] Endereço:State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, 430070, China.
[Ti] Título:Decreased formation of branched-chain short fatty acids in Bacillus amyloliquefaciens by metabolic engineering.
[So] Source:Biotechnol Lett;39(4):529-533, 2017 Apr.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To reduce the unpleasant odor during 1-deoxynojirimycin (DNJ) production, the genes of leucine dehydrogenase (bcd) and phosphate butryltransferase (ptb) were deleted from Bacillus amyloliquefaciens HZ-12, and the concentrations of branched-chain short fatty acids (BCFAs) and DNJ were compared. RESULTS: By knockout of the ptb gene, 1.01 g BCFAs kg was produced from fermented soybean by HZ-12Δptb. This was a 56% decrease compared with that of HZ-12 (2.27 g BCFAs kg ). Moreover, no significant difference was found in the DNJ concentration (0.7 g kg ). After further deletion of the bcd gene from HZ-12Δptb, no BCFAs was detected in fermented soybeans with HZ-12ΔptbΔbcd, while the DNJ yield decreased by 26% compared with HZ-12. CONCLUSIONS: HZ-12Δptb had decreased BCFAs formation but also maintained the stable DNJ yield, which contributed to producing DNJ-rich products with decreased unpleasant smell.
[Mh] Termos MeSH primário: 1-Desoxinojirimicina/metabolismo
Bacillus amyloliquefaciens/metabolismo
Ácidos Graxos/biossíntese
Microbiologia de Alimentos
Engenharia Metabólica
[Mh] Termos MeSH secundário: Bacillus amyloliquefaciens/genética
Cromatografia Gasosa
Cromatografia Líquida de Alta Pressão
Regulação para Baixo
Fermentação
Expressão Gênica
Técnicas de Inativação de Genes
Genes Bacterianos
Leucina Desidrogenase/metabolismo
Odorantes/prevenção & controle
Fosfato Acetiltransferase/metabolismo
Feijão de Soja/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 19130-96-2 (1-Deoxynojirimycin); EC 1.4.1.9 (Leucine Dehydrogenase); EC 2.3.1.8 (Phosphate Acetyltransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170412
[Lr] Data última revisão:
170412
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2270-5


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[PMID]:27940001
[Au] Autor:Sirobhushanam S; Galva C; Saunders LP; Sen S; Jayaswal R; Wilkinson BJ; Gatto C
[Ad] Endereço:School of Biological Sciences, Illinois State University, Normal, IL 61790, United States.
[Ti] Título:Utilization of multiple substrates by butyrate kinase from Listeria monocytogenes.
[So] Source:Biochim Biophys Acta;1862(3):283-290, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Listeria monocytogenes, the causative agent of listeriosis, can build up to dangerous levels in refrigerated foods potentially leading to expensive product recalls. An important aspect of the bacterium's growth at low temperatures is its ability to increase the branched-chain fatty acid anteiso C15:0 content of its membrane at lower growth temperatures, which imparts greater membrane fluidity. Mutants in the branched-chain α-keto dehydrogenase (bkd) complex are deficient in branched-chain fatty acids (BCFAs,) but these can be restored by feeding C4 and C5 branched-chain carboxylic acids (BCCAs). This suggests the presence of an alternate pathway for production of acyl CoA precursors for fatty acid biosynthesis. We hypothesize that the alternate pathway is composed of butyrate kinase (buk) and phosphotransbutyrylase (ptb) encoded in the bkd complex which produce acyl CoA products by their sequential action through the metabolism of carboxylic acids. We determined the steady state kinetics of recombinant His-tagged Buk using 11 different straight-chain and BCCA substrates in the acyl phosphate forming direction. Buk demonstrated highest catalytic efficiency with pentanoate as the substrate. Low product formation observed with acetate (C2) and hexanoate (C6) as the substrates indicates that Buk is not involved in either acetate metabolism or long chain carboxylic acid activation. We were also able to show that Buk catalysis occurs through a ternary complex intermediate. Additionally, Buk demonstrates a strong preference for BCCAs at low temperatures. These results indicate that Buk may be involved in the activation and assimilation of exogenous carboxylic acids for membrane fatty acid biosynthesis.
[Mh] Termos MeSH primário: Listeria monocytogenes/metabolismo
Fosfotransferases (Aceptor do Grupo Carboxila)/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Ácidos Carboxílicos/metabolismo
Temperatura Baixa
Ácidos Graxos/metabolismo
Cinética
Lipogênese/fisiologia
Fluidez de Membrana/fisiologia
Fosfato Acetiltransferase/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Carboxylic Acids); 0 (Fatty Acids); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.7 (butyrate kinase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


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[PMID]:27613406
[Au] Autor:Hirokawa Y; Dempo Y; Fukusaki E; Hanai T
[Ad] Endereço:Laboratory for Bioinformatics, Graduate School of Systems Biosciences, Kyushu University, 804 Westwing, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
[Ti] Título:Metabolic engineering for isopropanol production by an engineered cyanobacterium, Synechococcus elongatus PCC 7942, under photosynthetic conditions.
[So] Source:J Biosci Bioeng;123(1):39-45, 2017 Jan.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Cyanobacteria engineered for production of biofuels and biochemicals from carbon dioxide represent a promising area of research in relation to a sustainable economy. Previously, we have succeeded in producing isopropanol from cellular acetyl-CoA by means of Synechococcus elongatus PCC 7942 into which a synthetic metabolic pathway was introduced. The isopropanol production by this synthetic metabolic pathway requires acetate; therefore, the cells grown under photosynthetic conditions have to be transferred to a dark and anaerobic conditions to produce acetate. In this study, we achieved acetate production under photosynthetic conditions by S. elongatus PCC 7942 into which we introduced the pta gene encoding phosphate acetyltransferase from Escherichia coli. The metabolic modification (via pta introduction) of the isopropanol-producing strain enabled production of isopropanol under photosynthetic conditions. During 14 days of production, the titer of isopropanol reached 0.55 mM (33.1 mg/l) with an intermediate product, acetone, at 0.21 mM (12.2 mg/l).
[Mh] Termos MeSH primário: 2-Propanol/metabolismo
Engenharia Metabólica
Fotossíntese
Synechococcus/genética
Synechococcus/metabolismo
[Mh] Termos MeSH secundário: Biocombustíveis
Escherichia coli/enzimologia
Escherichia coli/genética
Fosfato Acetiltransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biofuels); EC 2.3.1.8 (Phosphate Acetyltransferase); ND2M416302 (2-Propanol)
[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:160911
[St] Status:MEDLINE


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[PMID]:27348810
[Au] Autor:Liu L; Duan X; Wu J
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, China.
[Ti] Título:L-Tryptophan Production in Escherichia coli Improved by Weakening the Pta-AckA Pathway.
[So] Source:PLoS One;11(6):e0158200, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acetate accumulation during the fermentation process of Escherichia coli FB-04, an L-tryptophan production strain, is detrimental to L-tryptophan production. In an initial attempt to reduce acetate formation, the phosphate acetyltransferase gene (pta) from E. coli FB-04 was deleted, forming strain FB-04(Δpta). Unfortunately, FB-04(Δpta) exhibited a growth defect. Therefore, pta was replaced with a pta variant (pta1) from E. coli CCTCC M 2016009, forming strain FB-04(pta1). Pta1 exhibits lower catalytic capacity and substrate affinity than Pta because of a single amino acid substitution (Pro69Leu). FB-04(pta1) lacked the growth defect of FB-04(Δpta) and showed improved fermentation performance. Strain FB-04(pta1) showed a 91% increase in L-tryptophan yield in flask fermentation experiments, while acetate production decreased by 35%, compared with its parent FB-04. Throughout the fed-batch fermentation process, acetate accumulation by FB-04(pta1) was slower than that by FB-04. The final L-tryptophan titer of FB-04(pta1) reached 44.0 g/L, representing a 15% increase over that of FB-04. Metabolomics analysis showed that the pta1 genomic substitution slightly decreased carbon flux through glycolysis and significantly increased carbon fluxes through the pentose phosphate and common aromatic pathways. These results indicate that this strategy enhances L-tryptophan production and decreases acetate accumulation during the L-tryptophan fermentation process.
[Mh] Termos MeSH primário: Acetato Quinase/metabolismo
Escherichia coli/metabolismo
Redes e Vias Metabólicas
Fosfato Acetiltransferase/metabolismo
Triptofano/biossíntese
[Mh] Termos MeSH secundário: Acetato Quinase/genética
Acetatos/metabolismo
Carbono/metabolismo
Ativação Enzimática
Escherichia coli/genética
Fermentação
Deleção de Genes
Metaboloma
Metabolômica/métodos
Mutação
Fosfato Acetiltransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 7440-44-0 (Carbon); 8DUH1N11BX (Tryptophan); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.1 (Acetate Kinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160628
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0158200


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[PMID]:27338272
[Au] Autor:Breitkopf R; Uhlig R; Drenckhan T; Fischer RJ
[Ad] Endereço:BBSRC/EPSRC Synthetic Biology Research Centre, School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.
[Ti] Título:Two propanediol utilization-like proteins of Moorella thermoacetica with phosphotransacetylase activity.
[So] Source:Extremophiles;20(5):653-61, 2016 Sep.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Moorella thermoacetica is one of the model acetogenic bacteria for the resolution of the Wood-Ljungdahl (acetyl-CoA) pathway in which CO2 is autotrophically assimilated yielding acetyl-CoA as central intermediate. Its further conversion into acetate relies on subsequent phosphotransacetylase (PTA) and acetate kinase reactions. However, the genome of M. thermoacetica contains no pta homologous gene. It has been speculated that the moth_0864 and moth_1181 gene products sharing similarities with an evolutionarily distinct phosphotransacylase involved in 1,2-propanediol utilization (PDUL) of Salmonella enterica act as PTAs in M. thermoacetica. Here, we demonstrate specific PTA activities with acetyl-CoA as substrate of 9.05 and 2.03 U/mg for the recombinant enzymes PDUL1 (Moth_1181) and PDUL2 (Moth_0864), respectively. Both showed maximal activity at 65 °C and pH 7.6. Native proteins (90 kDa) are homotetramers composed of four subunits with apparent molecular masses of about 23 kDa. Thus, one or both PDULs of M. thermoacetica might act as PTAs in vivo catalyzing the penultimate step of the Wood-Ljungdahl pathway toward the formation of acetate. In silico analysis underlined that up to now beside of M. thermoacetica, only Sporomusa ovata contains only PDUL like class(III)-PTAs but no other phosphotransacetylases or phosphotransbutyrylases (PTBs).
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Genes Bacterianos
Moorella/enzimologia
Fosfato Acetiltransferase/metabolismo
Propilenoglicol/metabolismo
[Mh] Termos MeSH secundário: Acetatos/metabolismo
Acetilcoenzima A/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Estabilidade Enzimática
Temperatura Alta
Concentração de Íons de Hidrogênio
Moorella/genética
Fosfato Acetiltransferase/química
Fosfato Acetiltransferase/genética
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Bacterial Proteins); 6DC9Q167V3 (Propylene Glycol); 72-89-9 (Acetyl Coenzyme A); EC 2.3.1.8 (Phosphate Acetyltransferase)
[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:160625
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-016-0854-6


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[PMID]:27320015
[Au] Autor:Sirobhushanam S; Galva C; Sen S; Wilkinson BJ; Gatto C
[Ad] Endereço:School of Biological Sciences, Illinois State University, Normal, IL 61790, USA.
[Ti] Título:Broad substrate specificity of phosphotransbutyrylase from Listeria monocytogenes: A potential participant in an alternative pathway for provision of acyl CoA precursors for fatty acid biosynthesis.
[So] Source:Biochim Biophys Acta;1861(9 Pt A):1102-1110, 2016 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Listeria monocytogenes, the causative organism of the serious food-borne disease listeriosis, has a membrane abundant in branched-chain fatty acids (BCFAs). BCFAs are normally biosynthesized from branched-chain amino acids via the activity of branched chain α-keto acid dehydrogenase (Bkd), and disruption of this pathway results in reduced BCFA content in the membrane. Short branched-chain carboxylic acids (BCCAs) added as media supplements result in incorporation of BCFAs arising from the supplemented BCCAs in the membrane of L. monocytogenes bkd mutant MOR401. High concentrations of the supplements also effect similar changes in the membrane of the wild type organism with intact bkd. Such carboxylic acids clearly act as fatty acid precursors, and there must be an alternative pathway resulting in the formation of their CoA thioester derivatives. Candidates for this are the enzymes phosphotransbutyrylase (Ptb) and butyrate kinase (Buk), the products of the first two genes of the bkd operon. Ptb from L. monocytogenes exhibited broad substrate specificity, a strong preference for branched-chain substrates, a lack of activity with acetyl CoA and hexanoyl CoA, and strict chain length preference (C3-C5). Ptb catalysis involved ternary complex formation. Additionally, Ptb could utilize unnatural branched-chain substrates such as 2-ethylbutyryl CoA, albeit with lower efficiency, consistent with a potential involvement of this enzyme in the conversion of the carboxylic acid additives into CoA primers for BCFA biosynthesis.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
Aminoácidos de Cadeia Ramificada/biossíntese
Ácidos Graxos/biossíntese
Fosfato Acetiltransferase/metabolismo
Fosfotransferases (Aceptor do Grupo Carboxila)/genética
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Acil Coenzima A/metabolismo
Aminoácidos de Cadeia Ramificada/metabolismo
Ácidos Graxos/metabolismo
Seres Humanos
Lipogênese/genética
Listeria monocytogenes/genética
Listeria monocytogenes/patogenicidade
Listeriose/genética
Listeriose/microbiologia
Listeriose/patologia
Redes e Vias Metabólicas
Fosfato Acetiltransferase/genética
Fosfotransferases (Aceptor do Grupo Carboxila)/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Amino Acids, Branched-Chain); 0 (Fatty Acids); 5060-32-2 (hexanoyl-coenzyme A); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.7 (butyrate kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160621
[St] Status:MEDLINE


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[PMID]:27306110
[Au] Autor:Skagia A; Zografou C; Vezyri E; Venieraki A; Katinakis P; Dimou M
[Ad] Endereço:Laboratory of General and Agricultural Microbiology, Faculty of Crop Science, Agricultural University of Athens, Iera Odos 75, 11855, Athens, Greece.
[Ti] Título:Cyclophilin PpiB is involved in motility and biofilm formation via its functional association with certain proteins.
[So] Source:Genes Cells;21(8):833-51, 2016 Aug.
[Is] ISSN:1365-2443
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PpiB belongs to the superfamily of peptidyl-prolyl cis/trans isomerases (PPIases, EC: 5.2.1.8), which catalyze the rate-limiting protein folding step at peptidyl-prolyl bonds and control several biological processes. In this study, we show that PpiB acts as a negative effector of motility and biofilm formation ability of Escherichia coli. We identify multicopy suppressors of each ΔppiB phenotype among putative PpiB prey proteins which upon deletion are often characterized by analogous phenotypes. Many putative preys show similar gene expression in wild-type and ΔppiB genetic backgrounds implying possible post-translational modifications by PpiB. We further conducted in vivo and in vitro interaction screens to determine which of them represent true preys. For DnaK, acetyl-CoA carboxylase, biotin carboxylase subunit (AccC) and phosphate acetyltransferase (Pta) we also showed a direct role of PpiB in the functional control of these proteins because it increased the measured enzyme activity of each protein and further interfered with DnaK localization and the correct folding of AccC. Taken together, these results indicate that PpiB is involved in diverse regulatory mechanisms to negatively modulate motility and biofilm formation via its functional association with certain protein substrates.
[Mh] Termos MeSH primário: Acetil-CoA Carboxilase/química
Biofilmes/crescimento & desenvolvimento
Ciclofilinas/genética
Proteínas de Escherichia coli/genética
Proteínas de Choque Térmico HSP70/genética
[Mh] Termos MeSH secundário: Acetil-CoA Carboxilase/genética
Carbono-Nitrogênio Ligases/química
Carbono-Nitrogênio Ligases/genética
Ciclofilinas/química
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Proteínas de Escherichia coli/química
Proteínas de Choque Térmico HSP70/química
Fosfato Acetiltransferase/genética
Dobramento de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (HSP70 Heat-Shock Proteins); 137497-17-7 (cyclophilin B); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 3.6.1.- (dnaK protein, E coli); EC 5.2.1.- (Cyclophilins); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.14 (biotin carboxylase); EC 6.4.1.2 (Acetyl-CoA Carboxylase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1111/gtc.12383


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[PMID]:26975873
[Au] Autor:Marshall DD; Sadykov MR; Thomas VC; Bayles KW; Powers R
[Ad] Endereço:Department of Chemistry, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
[Ti] Título:Redox Imbalance Underlies the Fitness Defect Associated with Inactivation of the Pta-AckA Pathway in Staphylococcus aureus.
[So] Source:J Proteome Res;15(4):1205-12, 2016 Apr 01.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The phosphotransacetylase-acetate kinase (Pta-AckA) pathway is thought to be a vital ATP generating pathway for Staphylococcus aureus. Disruption of the Pta-AckA pathway during overflow metabolism causes significant reduction in growth rate and viability, albeit not due to intracellular ATP depletion. Here, we demonstrate that toxicity associated with inactivation of the Pta-AckA pathway resulted from an altered intracellular redox environment. Growth of the pta and ackA mutants under anaerobic conditions partially restored cell viability. NMR metabolomics analyses and (13)C6-glucose metabolism tracing experiments revealed the activity of multiple pathways that promote redox (NADH/NAD(+)) turnover to be enhanced in the pta and ackA mutants during anaerobic growth. Restoration of redox homeostasis in the pta mutant by overexpressing l- lactate dehydrogenase partially restored its viability under aerobic conditions. Together, our findings suggest that during overflow metabolism, the Pta-AckA pathway plays a critical role in preventing cell viability defects by promoting intracellular redox homeostasis.
[Mh] Termos MeSH primário: Acetato Quinase/genética
Proteínas de Bactérias/genética
Regulação Bacteriana da Expressão Gênica
Metabolômica
Fosfato Acetiltransferase/genética
Staphylococcus aureus/genética
[Mh] Termos MeSH secundário: Acetato Quinase/deficiência
Trifosfato de Adenosina/biossíntese
Aerobiose
Anaerobiose
Proteínas de Bactérias/metabolismo
Isótopos de Carbono
Glucose/metabolismo
Homeostase
L-Lactato Desidrogenase/metabolismo
Espectroscopia de Ressonância Magnética
Viabilidade Microbiana
Mutação
NAD/metabolismo
Oxirredução
Fosfato Acetiltransferase/deficiência
Staphylococcus aureus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carbon Isotopes); 0U46U6E8UK (NAD); 8L70Q75FXE (Adenosine Triphosphate); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.1 (Acetate Kinase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170403
[Lr] Data última revisão:
170403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160316
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.5b01089



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