Base de dados : MEDLINE
Pesquisa : D09.894.150 [Categoria DeCS]
Referências encontradas : 431 [refinar]
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[PMID]:28617934
[Au] Autor:Goldfine H
[Ad] Endereço:Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
[Ti] Título:The anaerobic biosynthesis of plasmalogens.
[So] Source:FEBS Lett;591(18):2714-2719, 2017 Sep.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The biosynthesis of plasmalogens in anaerobic bacteria differs fundamentally from that in animal cells. Firstly, the formation of the alk-1'-enyl ether bond in animal cells is oxygen dependent. Secondly, the first step in plasmalogen formation in animal cells is an acylation of dihydroxyacetone phosphate, which has been ruled out as a precursor in anaerobes. In bacteria the alk-1'-enyl ether bond is formed after the fully formed acyl glycerolipids are synthesized. Evidence will be presented for the conversion of the sn-1 acyl-linked chain to an O-alk-1'-enyl ether by an as yet unknown mechanism.
[Mh] Termos MeSH primário: Plasmalogênios/biossíntese
[Mh] Termos MeSH secundário: Acilação
Anaerobiose
Animais
Clostridium beijerinckii/metabolismo
Fosfato de Di-Hidroxiacetona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Plasmalogens); 57-04-5 (Dihydroxyacetone Phosphate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12714


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[PMID]:28280244
[Au] Autor:Mugabo Y; Zhao S; Lamontagne J; Al-Mass A; Peyot ML; Corkey BE; Joly E; Madiraju SRM; Prentki M
[Ad] Endereço:From the Montreal Diabetes Research Center and Centre de Recherche du Centre Hospitalier de l'Université de Montréal, Montréal, Québec H2X 0A9, Canada.
[Ti] Título:Metabolic fate of glucose and candidate signaling and excess-fuel detoxification pathways in pancreatic ß-cells.
[So] Source:J Biol Chem;292(18):7407-7422, 2017 May 05.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucose metabolism promotes insulin secretion in ß-cells via metabolic coupling factors that are incompletely defined. Moreover, chronically elevated glucose causes ß-cell dysfunction, but little is known about how cells handle excess fuels to avoid toxicity. Here we sought to determine which among the candidate pathways and coupling factors best correlates with glucose-stimulated insulin secretion (GSIS), define the fate of glucose in the ß-cell, and identify pathways possibly involved in excess-fuel detoxification. We exposed isolated rat islets for 1 h to increasing glucose concentrations and measured various pathways and metabolites. Glucose oxidation, oxygen consumption, and ATP production correlated well with GSIS and saturated at 16 mm glucose. However, glucose utilization, glycerol release, triglyceride and glycogen contents, free fatty acid (FFA) content and release, and cholesterol and cholesterol esters increased linearly up to 25 mm glucose. Besides being oxidized, glucose was mainly metabolized via glycerol production and release and lipid synthesis (particularly FFA, triglycerides, and cholesterol), whereas glycogen production was comparatively low. Using targeted metabolomics in INS-1(832/13) cells, we found that several metabolites correlated well with GSIS, in particular some Krebs cycle intermediates, malonyl-CoA, and lower ADP levels. Glucose dose-dependently increased the dihydroxyacetone phosphate/glycerol 3-phosphate ratio in INS-1(832/13) cells, indicating a more oxidized state of NAD in the cytosol upon glucose stimulation. Overall, the data support a role for accelerated oxidative mitochondrial metabolism, anaplerosis, and malonyl-CoA/lipid signaling in ß-cell metabolic signaling and suggest that a decrease in ADP levels is important in GSIS. The results also suggest that excess-fuel detoxification pathways in ß-cells possibly comprise glycerol and FFA formation and release extracellularly and the diversion of glucose carbons to triglycerides and cholesterol esters.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Ácidos Graxos/metabolismo
Glucose/farmacologia
Células Secretoras de Insulina/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Ésteres do Colesterol/metabolismo
Fosfato de Di-Hidroxiacetona/metabolismo
Relação Dose-Resposta a Droga
Glucose/metabolismo
Glicerofosfatos/metabolismo
Glicogênio/metabolismo
Masculino
Malonil Coenzima A/metabolismo
Ratos
Ratos Wistar
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cholesterol Esters); 0 (Fatty Acids); 0 (Glycerophosphates); 0 (Triglycerides); 524-14-1 (Malonyl Coenzyme A); 57-04-5 (Dihydroxyacetone Phosphate); 8L70Q75FXE (Adenosine Triphosphate); 9005-79-2 (Glycogen); 9NTI6P3O4X (alpha-glycerophosphoric acid); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.763060


  3 / 431 MEDLINE  
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[PMID]:27538376
[Au] Autor:Moreno-Sánchez R; Marín-Hernández Á; Del Mazo-Monsalvo I; Saavedra E; Rodríguez-Enríquez S
[Ad] Endereço:Instituto Nacional de Cardiología, Departamento de Bioquímica, Tlalpan D.F. 14080, Mexico. Electronic address: rafael.moreno@cardiologia.org.mx.
[Ti] Título:Assessment of the low inhibitory specificity of oxamate, aminooxyacetate and dichloroacetate on cancer energy metabolism.
[So] Source:Biochim Biophys Acta;1861(1 Pt A):3221-3236, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Exceedingly high therapeutic/experimental doses of metabolic drugs such as oxamate, aminooxyacetate (AOA) and dichloroacetate (DCA) are required to diminish growth, glycolysis and oxidative phosphorylation (OxPhos) of different cancer cells. To identify the mechanisms of action of these drugs on cancer energy metabolism, a systematic analysis of their specificities was undertaken. METHODS: Hepatocarcinoma AS-30D cells were treated with the inhibitors and glycolysis and OxPhos enzyme activities, metabolites and fluxes were analyzed. Kinetic modeling of glycolysis was used to identify the regulatory mechanisms. RESULTS: Oxamate (i) not only inhibited LDH, but also PYK and ENO activities inducing an increase in the cytosolic NAD(P)H, Fru1,6BP and DHAP levels in AS-30D cells; (ii) it slightly inhibited HPI, ALD and Glc6PDH; and (iii) it inhibited pyruvate-driven OxPhos in isolated heart mitochondria. AOA (i) strongly inhibited both AAT and AlaT, and 2-OGDH and glutamate-driven OxPhos; and (ii) moderately affected GAPDH and TPI. DCA slightly affected pyruvate-driven OxPhos and Glc6PDH. Kinetic modeling of cancer glycolysis revealed that oxamate inhibition of LDH, PYK and ENO was insufficient to achieve glycolysis flux inhibition. To do so, HK, HPI, TPI and GAPDH have to be also inhibited by the accumulated Fru1,6BP and DHAP induced by oxamate. CONCLUSION: Oxamate, AOA, and DCA are not specific drugs since they inhibit several enzymes/transporters of the glycolytic and OxPhos pathways through direct interaction or indirect mechanisms. GENERAL SIGNIFICANCE: These data explain why oxamate or AOA, through their multisite inhibitory actions on glycolysis or OxPhos, may be able to decrease the proliferation of cancer cells.
[Mh] Termos MeSH primário: Ácido Amino-Oxiacético/farmacologia
Ácido Dicloroacético/farmacologia
Metabolismo Energético/efeitos dos fármacos
Neoplasias/metabolismo
Ácido Oxâmico/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Simulação por Computador
Fosfato de Di-Hidroxiacetona/farmacologia
Inibidores Enzimáticos/farmacologia
Feminino
Glicólise/efeitos dos fármacos
Seres Humanos
Cinética
Camundongos
Mitocôndrias Cardíacas/efeitos dos fármacos
Mitocôndrias Cardíacas/metabolismo
Modelos Moleculares
NADP/metabolismo
Fosforilação Oxidativa/efeitos dos fármacos
Ratos Wistar
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Enzyme Inhibitors); 14I68GI3OQ (Aminooxyacetic Acid); 53-59-8 (NADP); 57-04-5 (Dihydroxyacetone Phosphate); 9LSH52S3LQ (Dichloroacetic Acid); QU60N5OPLG (Oxamic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


  4 / 431 MEDLINE  
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[PMID]:27404889
[Au] Autor:Fenwick MK; Ealick SE
[Ad] Endereço:Department of Chemistry and Chemical Biology, Cornell University , Ithaca, New York 14853, United States.
[Ti] Título:Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.
[So] Source:Biochemistry;55(30):4135-9, 2016 Aug 02.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The quinolinate synthase of prokaryotes and photosynthetic eukaryotes, NadA, contains a [4Fe-4S] cluster with unknown function. We report crystal structures of Pyrococcus horikoshii NadA in complex with dihydroxyacetone phosphate (DHAP), iminoaspartate analogues, and quinolinate. DHAP adopts a nearly planar conformation and chelates the [4Fe-4S] cluster via its keto and hydroxyl groups. The active site architecture suggests that the cluster acts as a Lewis acid in enediolate formation, like zinc in class II aldolases. The DHAP and putative iminoaspartate structures suggest a model for a condensed intermediate. The ensemble of structures suggests a two-state system, which may be exploited in early steps.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Complexos Multienzimáticos/química
[Mh] Termos MeSH secundário: Ácido Aspártico/análogos & derivados
Ácido Aspártico/química
Domínio Catalítico
Cristalografia por Raios X
Fosfato de Di-Hidroxiacetona/química
Proteínas com Ferro-Enxofre/química
Modelos Moleculares
Conformação Proteica
Pyrococcus horikoshii/enzimologia
Ácido Quinolínico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Iron-Sulfur Proteins); 0 (Multienzyme Complexes); 30KYC7MIAI (Aspartic Acid); 39434-08-7 (quinolinic acid synthetase); 57-04-5 (Dihydroxyacetone Phosphate); 79067-61-1 (iminoaspartic acid); F6F0HK1URN (Quinolinic Acid)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00626


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[PMID]:27149328
[Au] Autor:Richard JP; Amyes TL; Malabanan MM; Zhai X; Kim KJ; Reinhardt CJ; Wierenga RK; Drake EJ; Gulick AM
[Ad] Endereço:Department of Chemistry, University at Buffalo, State University of New York , Buffalo, New York 14260, United States.
[Ti] Título:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
[So] Source:Biochemistry;55(21):3036-47, 2016 May 31.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Kinetic parameters are reported for the reactions of whole substrates (kcat/Km, M(-1) s(-1)) (R)-glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP) and for the substrate pieces [(kcat/Km)E·HPi/Kd, M(-2) s(-1)] glycolaldehyde (GA) and phosphite dianion (HPi) catalyzed by the I172A/L232A mutant of triosephosphate isomerase from Trypanosoma brucei brucei (TbbTIM). A comparison with the corresponding parameters for wild-type, I172A, and L232A TbbTIM-catalyzed reactions shows that the effect of I172A and L232A mutations on ΔG(⧧) for the wild-type TbbTIM-catalyzed reactions of the substrate pieces is nearly the same as the effect of the same mutations on TbbTIM previously mutated at the second side chain. This provides strong evidence that mutation of the first hydrophobic side chain does not affect the functioning of the second side chain in catalysis of the reactions of the substrate pieces. By contrast, the effects of I172A and L232A mutations on ΔG(⧧) for wild-type TbbTIM-catalyzed reactions of the whole substrate are different from the effect of the same mutations on TbbTIM previously mutated at the second side chain. This is due to the change in the rate-determining step that determines the barrier to the isomerization reaction. X-ray crystal structures are reported for I172A, L232A, and I172A/L232A TIMs and for the complexes of these mutants to the intermediate analogue phosphoglycolate (PGA). The structures of the PGA complexes with wild-type and mutant enzymes are nearly superimposable, except that the space opened by replacement of the hydrophobic side chain is occupied by a water molecule that lies ∼3.5 Å from the basic side chain of Glu167. The new water at I172A mutant TbbTIM provides a simple rationalization for the increase in the activation barrier ΔG(⧧) observed for mutant enzyme-catalyzed reactions of the whole substrate and substrate pieces. By contrast, the new water at the L232A mutant does not predict the decrease in ΔG(⧧) observed for the mutant enzyme-catalyzed reactions of the substrate piece GA.
[Mh] Termos MeSH primário: Fosfato de Di-Hidroxiacetona/metabolismo
Ácido Glutâmico/química
Gliceraldeído 3-Fosfato/metabolismo
Triose-Fosfato Isomerase/química
Triose-Fosfato Isomerase/metabolismo
Trypanosoma brucei brucei/enzimologia
[Mh] Termos MeSH secundário: Catálise
Cristalografia por Raios X
Interações Hidrofóbicas e Hidrofílicas
Cinética
Modelos Moleculares
Mutação/genética
Relação Estrutura-Atividade
Triose-Fosfato Isomerase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
142-10-9 (Glyceraldehyde 3-Phosphate); 3KX376GY7L (Glutamic Acid); 57-04-5 (Dihydroxyacetone Phosphate); EC 5.3.1.1 (Triose-Phosphate Isomerase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160506
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00311


  6 / 431 MEDLINE  
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[PMID]:26992791
[Au] Autor:Jain VK; Tear CJ; Lim CY
[Ad] Endereço:Industrial Biotechnology Division, Institute of Chemical & Engineering Sciences, Agency for Science, Technology and Research (A-STAR), 1, Pesek Road, Jurong Island 627833, Singapore. Electronic address: jainvk@ices.a-star.edu.sg.
[Ti] Título:Dihydroxyacetone production in an engineered Escherichia coli through expression of Corynebacterium glutamicum dihydroxyacetone phosphate dephosphorylase.
[So] Source:Enzyme Microb Technol;86:39-44, 2016 May.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dihydroxyacetone (DHA) has several industrial applications such as a tanning agent in tanning lotions in the cosmetic industry; its production via microbial fermentation would present a more sustainable option for the future. Here we genetically engineered Escherichia coli (E. coli) for DHA production from glucose. Deletion of E. coli triose phosphate isomerase (tpiA) gene was carried out to accumulate dihydroxyacetone phosphate (DHAP), for use as the main intermediate or precursor for DHA production. The accumulated DHAP was then converted to DHA through the heterologous expression of Corynebacterium glutamicum DHAP dephosphorylase (cghdpA) gene. To conserve DHAP exclusively for DHA production we removed methylglyoxal synthase (mgsA) gene in the ΔtpiA strain. This drastically improved DHA production from 0.83g/l (0.06g DHA/g glucose) in the ΔtpiA strain bearing cghdpA to 5.84g/l (0.41g DHA/g glucose) in the ΔtpiAΔmgsA double mutant containing the same gene. To limit the conversion of intracellular DHA to glycerol, glycerol dehydrogenase (gldA) gene was further knocked out resulting in a ΔtpiAΔmgsAΔgldA triple mutant. This triple mutant expressing the cghdpA gene produced 6.60g/l of DHA at 87% of the maximum theoretical yield. In summary, we demonstrated an efficient system for DHA production in genetically engineered E. coli strain.
[Mh] Termos MeSH primário: Fosfato de Di-Hidroxiacetona/metabolismo
Di-Hidroxiacetona/biossíntese
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Corynebacterium glutamicum/enzimologia
Corynebacterium glutamicum/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Fermentação
Deleção de Genes
Cinética
Engenharia Metabólica
Redes e Vias Metabólicas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 57-04-5 (Dihydroxyacetone Phosphate); O10DDW6JOO (Dihydroxyacetone)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170117
[Lr] Data última revisão:
170117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160320
[St] Status:MEDLINE


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[PMID]:26602120
[Au] Autor:Deng S; Scott D; Myers D; Garg U
[Ad] Endereço:Department of Pathology and Laboratory Medicine, Children's Mercy Hospitals and Clinics, 2401 Gillham Road, Kansas City, MO, 64108, USA.
[Ti] Título:Quantification of Dihydroxyacetone Phosphate (DHAP) in Human Red Blood Cells by HPLC-TripleTOF 5600™ Mass Spectrometer.
[So] Source:Methods Mol Biol;1378:81-6, 2016.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Triosephosphate isomerase (TPI) is a glycolytic enzyme which catalyzes the interconversion between glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). TPI deficiency results in accumulation of DHAP in human red blood cells and other tissues. The disease is characterized by congenital hemolytic anemia, and progressive neuromuscular dysfunction. The laboratory diagnosis is generally made by measurement of TPI activity in RBCs. Measurement of DHAP can be useful in further confirmation and follow-up of the disease. We developed HPLC/TOF-MS method for quantitation of DHAP in RBCs. The method involves simple protein precipitation, reverse phase C8 column chromatography, ion pairing with tributylamine, and long run time of 50 min to separate the two isomers (G3P and DHAP).
[Mh] Termos MeSH primário: Análise Química do Sangue/métodos
Cromatografia Líquida de Alta Pressão/métodos
Fosfato de Di-Hidroxiacetona/sangue
Eritrócitos/química
Espectrometria de Massas/métodos
[Mh] Termos MeSH secundário: Análise Química do Sangue/instrumentação
Cromatografia Líquida de Alta Pressão/instrumentação
Seres Humanos
Espectrometria de Massas/instrumentação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
57-04-5 (Dihydroxyacetone Phosphate)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151125
[Lr] Data última revisão:
151125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151126
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-3182-8_10


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[PMID]:26186096
[Au] Autor:Cam Y; Alkim C; Trichez D; Trebosc V; Vax A; Bartolo F; Besse P; François JM; Walther T
[Ad] Endereço:INSA, UPS, INP, LISBP, Université de Toulouse , 135 Avenue de Rangueil, 31077 Toulouse, France.
[Ti] Título:Engineering of a Synthetic Metabolic Pathway for the Assimilation of (d)-Xylose into Value-Added Chemicals.
[So] Source:ACS Synth Biol;5(7):607-18, 2016 07 15.
[Is] ISSN:2161-5063
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A synthetic pathway for (d)-xylose assimilation was stoichiometrically evaluated and implemented in Escherichia coli strains. The pathway proceeds via isomerization of (d)-xylose to (d)-xylulose, phosphorylation of (d)-xylulose to obtain (d)-xylulose-1-phosphate (X1P), and aldolytic cleavage of the latter to yield glycolaldehyde and DHAP. Stoichiometric analyses showed that this pathway provides access to ethylene glycol with a theoretical molar yield of 1. Alternatively, both glycolaldehyde and DHAP can be converted to glycolic acid with a theoretical yield that is 20% higher than for the exclusive production of this acid via the glyoxylate shunt. Simultaneous expression of xylulose-1 kinase and X1P aldolase activities, provided by human ketohexokinase-C and human aldolase-B, respectively, restored growth of a (d)-xylulose-5-kinase mutant on xylose. This strain produced ethylene glycol as the major metabolic endproduct. Metabolic engineering provided strains that assimilated the entire C2 fraction into the central metabolism or that produced 4.3 g/L glycolic acid at a molar yield of 0.9 in shake flasks.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Engenharia Metabólica/métodos
Xilose/metabolismo
[Mh] Termos MeSH secundário: Acetaldeído/análogos & derivados
Acetaldeído/metabolismo
Aldeído Liases/genética
Aldeído Liases/metabolismo
Fosfato de Di-Hidroxiacetona/genética
Fosfato de Di-Hidroxiacetona/metabolismo
Enzimas/genética
Enzimas/metabolismo
Escherichia coli/genética
Glicolatos/metabolismo
Mutação
Pentosefosfatos/genética
Pentosefosfatos/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Xilose/genética
Xilulose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes); 0 (Glycolates); 0 (Pentosephosphates); 0WT12SX38S (glycolic acid); 2547-08-2 (xylulose-1-phosphate); 57-04-5 (Dihydroxyacetone Phosphate); 5962-29-8 (Xylulose); A1TA934AKO (Xylose); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 4.1.2.- (Aldehyde-Lyases); GO1N1ZPR3B (Acetaldehyde); W0A0XPU08U (glycolaldehyde)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170314
[Lr] Data última revisão:
170314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150718
[St] Status:MEDLINE
[do] DOI:10.1021/acssynbio.5b00103


  9 / 431 MEDLINE  
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[PMID]:26709515
[Au] Autor:Park SH; Kim HS; Park MS; Moon S; Song MK; Park HS; Hahn H; Kim SJ; Bae E; Kim HJ; Han BW
[Ad] Endereço:Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
[Ti] Título:Structure and Stability of the Dimeric Triosephosphate Isomerase from the Thermophilic Archaeon Thermoplasma acidophilum.
[So] Source:PLoS One;10(12):e0145331, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thermoplasma acidophilum is a thermophilic archaeon that uses both non-phosphorylative Entner-Doudoroff (ED) pathway and Embden-Meyerhof-Parnas (EMP) pathway for glucose degradation. While triosephosphate isomerase (TPI), a well-known glycolytic enzyme, is not involved in the ED pathway in T. acidophilum, it has been considered to play an important role in the EMP pathway. Here, we report crystal structures of apo- and glycerol-3-phosphate-bound TPI from T. acidophilum (TaTPI). TaTPI adopts the canonical TIM-barrel fold with eight α-helices and parallel eight ß-strands. Although TaTPI shares ~30% sequence identity to other TPIs from thermophilic species that adopt tetrameric conformation for enzymatic activity in their harsh physiological environments, TaTPI exists as a dimer in solution. We confirmed the dimeric conformation of TaTPI by analytical ultracentrifugation and size-exclusion chromatography. Helix 5 as well as helix 4 of thermostable tetrameric TPIs have been known to play crucial roles in oligomerization, forming a hydrophobic interface. However, TaTPI contains unique charged-amino acid residues in the helix 5 and adopts dimer conformation. TaTPI exhibits the apparent Td value of 74.6°C and maintains its overall structure with some changes in the secondary structure contents at extremely acidic conditions (pH 1-2). Based on our structural and biophysical analyses of TaTPI, more compact structure of the protomer with reduced length of loops and certain patches on the surface could account for the robust nature of Thermoplasma acidophilum TPI.
[Mh] Termos MeSH primário: Gliceraldeído 3-Fosfato/metabolismo
Thermoplasma/enzimologia
Triose-Fosfato Isomerase/metabolismo
Triose-Fosfato Isomerase/ultraestrutura
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Dicroísmo Circular
Cristalografia por Raios X
Fosfato de Di-Hidroxiacetona/química
Dimerização
Gliceraldeído 3-Fosfato/química
Glicólise/fisiologia
Modelos Moleculares
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
142-10-9 (Glyceraldehyde 3-Phosphate); 57-04-5 (Dihydroxyacetone Phosphate); EC 5.3.1.1 (Triose-Phosphate Isomerase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151229
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0145331


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[PMID]:26455817
[Au] Autor:Reichmann D; Couté Y; Ollagnier de Choudens S
[Ad] Endereço:Université Grenoble Alpes , iRTSV-LCBM, F-38000 Grenoble, France.
[Ti] Título:Dual activity of quinolinate synthase: triose phosphate isomerase and dehydration activities play together to form quinolinate.
[So] Source:Biochemistry;54(42):6443-6, 2015 Oct 27.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Quinolinate synthase (NadA) is an Fe4S4 cluster-containing dehydrating enzyme involved in the synthesis of quinolinic acid (QA), the universal precursor of the essential coenzyme nicotinamide adenine dinucleotide. The reaction catalyzed by NadA is not well understood, and two mechanisms have been proposed in the literature that differ in the nature of the molecule (DHAP or G-3P) that condenses with iminoaspartate (IA) to form QA. In this article, using biochemical approaches, we demonstrate that DHAP is the triose that condenses with IA to form QA. The capacity of NadA to use G-3P is due to its previously unknown triose phosphate isomerase activity.
[Mh] Termos MeSH primário: Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
Triose-Fosfato Isomerase/química
Triose-Fosfato Isomerase/metabolismo
[Mh] Termos MeSH secundário: Ácido Aspártico/análogos & derivados
Ácido Aspártico/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Fosfato de Di-Hidroxiacetona/metabolismo
Redes e Vias Metabólicas
Modelos Químicos
NAD/biossíntese
Ácido Quinolínico/metabolismo
Thermotoga maritima/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Multienzyme Complexes); 0U46U6E8UK (NAD); 30KYC7MIAI (Aspartic Acid); 39434-08-7 (quinolinic acid synthetase); 57-04-5 (Dihydroxyacetone Phosphate); 79067-61-1 (iminoaspartic acid); EC 5.3.1.1 (Triose-Phosphate Isomerase); F6F0HK1URN (Quinolinic Acid)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:151027
[Lr] Data última revisão:
151027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151013
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.5b00991



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