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[PMID]:28712849
[Au] Autor:Liu LK; Becker DF; Tanner JJ
[Ad] Endereço:Department of Biochemistry, University of Missouri, Columbia, MO, 65211, United States.
[Ti] Título:Structure, function, and mechanism of proline utilization A (PutA).
[So] Source:Arch Biochem Biophys;632:142-157, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline has important roles in multiple biological processes such as cellular bioenergetics, cell growth, oxidative and osmotic stress response, protein folding and stability, and redox signaling. The proline catabolic pathway, which forms glutamate, enables organisms to utilize proline as a carbon, nitrogen, and energy source. FAD-dependent proline dehydrogenase (PRODH) and NAD -dependent glutamate semialdehyde dehydrogenase (GSALDH) convert proline to glutamate in two sequential oxidative steps. Depletion of PRODH and GSALDH in humans leads to hyperprolinemia, which is associated with mental disorders such as schizophrenia. Also, some pathogens require proline catabolism for virulence. A unique aspect of proline catabolism is the multifunctional proline utilization A (PutA) enzyme found in Gram-negative bacteria. PutA is a large (>1000 residues) bifunctional enzyme that combines PRODH and GSALDH activities into one polypeptide chain. In addition, some PutAs function as a DNA-binding transcriptional repressor of proline utilization genes. This review describes several attributes of PutA that make it a remarkable flavoenzyme: (1) diversity of oligomeric state and quaternary structure; (2) substrate channeling and enzyme hysteresis; (3) DNA-binding activity and transcriptional repressor function; and (4) flavin redox dependent changes in subcellular location and function in response to proline (functional switching).
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/química
Proteínas de Bactérias/química
Flavoproteínas/química
Bactérias Gram-Negativas/enzimologia
Proteínas de Membrana/química
Prolina Oxidase/química
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/deficiência
1-Pirrolina-5-Carboxilato Desidrogenase/genética
1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Erros Inatos do Metabolismo dos Aminoácidos
Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/genética
Flavina-Adenina Dinucleotídeo/metabolismo
Flavoproteínas/genética
Flavoproteínas/metabolismo
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Prolina/química
Prolina/genética
Prolina/metabolismo
Prolina Oxidase/genética
Prolina Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavoproteins); 0 (Membrane Proteins); 0 (PutA protein, Bacteria); 146-14-5 (Flavin-Adenine Dinucleotide); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.5.3.- (Proline Oxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


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[PMID]:28213180
[Au] Autor:Balestro GC; Higashi B; Lopes SM; Gonçalves JE; Vieira LG; de Oliveira AJ; Gonçalves RA
[Ad] Endereço:Department of Pharmacy, Graduate Program in Pharmaceutical Sciences, State University of Maringá, Avenida Colombo 5790, 87.020-900 Maringá, PR, Brazil.
[Ti] Título:Biochemical composition of symplastic sap from sugarcane genetically modified to overproduce proline.
[So] Source:Plant Physiol Biochem;113:133-140, 2017 Apr.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Global interest in sugarcane has increased significantly in recent years because of its economic impact on sustainable energy production. The purpose of the present study was to evaluate changes in the concentrations of total sugars, amino acids, free proline, and total proteins by colorimetric analyses and nuclear magnetic resonance (NMR) to perform a metabolic profiling of a water-soluble fraction of symplastic sap in response to the constitutive expression of a mutant Δ -pyrroline-5-carboxylate synthetase (P5CS) gene from Vigna aconitifolia. However, there was not a significant increase in the free proline content in the sap of transgenic plants compared to the non-transformed control plants. The most noticeable difference between the two genotypes was an almost two-fold increase in the accumulation of sucrose in the stem internodes of P5CS transgenic sugarcane plants. The results presented in this work showed that transgenic sugarcane plants with increased levels of free proline accumulates high soluble sugar content and, therefore, may represent a novel genotype for improving sugarcane cultivars.
[Mh] Termos MeSH primário: Prolina/biossíntese
Saccharum/genética
Saccharum/metabolismo
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/genética
1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Biomassa
Etanol/metabolismo
Genótipo
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Proteínas de Plantas/biossíntese
Proteínas de Plantas/metabolismo
Caules de Planta/metabolismo
Plantas Geneticamente Modificadas
Prolina/metabolismo
Saccharum/enzimologia
Sacarose/metabolismo
Vigna/enzimologia
Vigna/genética
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (Plant Proteins); 059QF0KO0R (Water); 3K9958V90M (Ethanol); 57-50-1 (Sucrose); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE


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[PMID]:25623067
[Au] Autor:Mantilla BS; Paes LS; Pral EM; Martil DE; Thiemann OH; Fernández-Silva P; Bastos EL; Silber AM
[Ad] Endereço:From the Instituto de Ciências Biomédicas, Departamento de Parasitologia, Universidade de São Paulo, 05508-000 São Paulo, Brazil.
[Ti] Título:Role of Δ1-pyrroline-5-carboxylate dehydrogenase supports mitochondrial metabolism and host-cell invasion of Trypanosoma cruzi.
[So] Source:J Biol Chem;290(12):7767-90, 2015 Mar 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline is crucial for energizing critical events throughout the life cycle of Trypanosoma cruzi, the etiological agent of Chagas disease. The proline breakdown pathway consists of two oxidation steps, both of which produce reducing equivalents as follows: the conversion of proline to Δ(1)-pyrroline-5-carboxylate (P5C), and the subsequent conversion of P5C to glutamate. We have identified and characterized the Δ(1)-pyrroline-5-carboxylate dehydrogenase from T. cruzi (TcP5CDH) and report here on how this enzyme contributes to a central metabolic pathway in this parasite. Size-exclusion chromatography, two-dimensional gel electrophoresis, and small angle x-ray scattering analysis of TcP5CDH revealed an oligomeric state composed of two subunits of six protomers. TcP5CDH was found to complement a yeast strain deficient in PUT2 activity, confirming the enzyme's functional role; and the biochemical parameters (Km, kcat, and kcat/Km) of the recombinant TcP5CDH were determined, exhibiting values comparable with those from T. cruzi lysates. In addition, TcP5CDH exhibited mitochondrial staining during the main stages of the T. cruzi life cycle. mRNA and enzymatic activity levels indicated the up-regulation (6-fold change) of TcP5CDH during the infective stages of the parasite. The participation of P5C as an energy source was also demonstrated. Overall, we propose that this enzymatic step is crucial for the viability of both replicative and infective forms of T. cruzi.
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Mitocôndrias/metabolismo
Trypanosoma/patogenicidade
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/química
Sequência de Aminoácidos
Animais
Sequência de Bases
Células CHO
Cricetinae
Cricetulus
Primers do DNA
Dados de Sequência Molecular
Reação em Cadeia da Polimerase em Tempo Real
Homologia de Sequência de Aminoácidos
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150128
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.574525


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[PMID]:25557497
[Au] Autor:Lagautriere T; Bashiri G; Baker EN
[Ad] Endereço:Structural Biology Laboratory, School of Biological Sciences and Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, Auckland 1010, New Zealand.
[Ti] Título:Use of a "silver bullet" to resolve crystal lattice dislocation disorder: a cobalamin complex of Δ1-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis.
[So] Source:J Struct Biol;189(2):153-7, 2015 Feb.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The use of small molecules as "silver bullets" that can bind to generate crosslinks between protein molecules has been advanced as a powerful means of enhancing success in protein crystallization (McPherson and Cudney, 2006). We have explored this approach in attempts to overcome an order-disorder phenomenon that complicated the structural analysis of the enzyme Δ(1)-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis (P5CDH, Mtb-PruA). Using the Silver Bullets Bio screen, we obtained new crystal packing using cobalamin as a co-crystallization agent. This crystal form did not display the order-disorder phenomenon previously encountered. Solution of the crystal structure showed that cobalamin molecules are present in the crystal contacts. Although the cobalamin binding probably does not have physiological relevance, it reflects similarities in the nucleotide-binding region of Mtb-PruA, with the nucleotide loop of cobalamin sharing the binding site for the adenine moiety of NAD(+).
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/química
Proteínas de Bactérias/química
Reagentes para Ligações Cruzadas/química
Mycobacterium tuberculosis/enzimologia
Vitamina B 12/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalização
Cristalografia por Raios X
Ligações de Hidrogênio
Cinética
Modelos Moleculares
NAD/química
Estrutura Quaternária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cross-Linking Reagents); 0U46U6E8UK (NAD); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150106
[St] Status:MEDLINE


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[PMID]:25492892
[Au] Autor:Sanyal N; Arentson BW; Luo M; Tanner JJ; Becker DF
[Ad] Endereço:From the Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588 and.
[Ti] Título:First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.
[So] Source:J Biol Chem;290(4):2225-34, 2015 Jan 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH) catalyze the four-electron oxidation of proline to glutamate via the intermediates P5C and l-glutamate-γ-semialdehyde (GSA). In Gram-negative bacteria, PRODH and P5CDH are fused together in the bifunctional enzyme proline utilization A (PutA) whereas in other organisms PRODH and P5CDH are expressed as separate monofunctional enzymes. Substrate channeling has previously been shown for bifunctional PutAs, but whether the monofunctional enzymes utilize an analogous channeling mechanism has not been examined. Here, we report the first evidence of substrate channeling in a PRODH-P5CDH two-enzyme pair. Kinetic data for the coupled reaction of PRODH and P5CDH from Thermus thermophilus are consistent with a substrate channeling mechanism, as the approach to steady-state formation of NADH does not fit a non-channeling two-enzyme model. Furthermore, inactive P5CDH and PRODH mutants inhibit NADH production and increase trapping of the P5C intermediate in coupled assays of wild-type PRODH-P5CDH enzyme pairs, indicating that the mutants disrupt PRODH-P5CDH channeling interactions. A dissociation constant of 3 µm was estimated for a putative PRODH-P5CDH complex by surface plasmon resonance (SPR). Interestingly, P5CDH binding to PRODH was only observed when PRODH was immobilized with the top face of its (ßα)8 barrel exposed. Using the known x-ray crystal structures of PRODH and P5CDH from T. thermophilus, a model was built for a proposed PRODH-P5CDH enzyme channeling complex. The structural model predicts that the core channeling pathway of bifunctional PutA enzymes is conserved in monofunctional PRODH-P5CDH enzyme pairs.
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
NAD/química
Prolina Oxidase/metabolismo
Prolina/química
Mapeamento de Interação de Proteínas
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: Catálise
Flavoproteínas/metabolismo
Modelos Moleculares
Mutação
Oxigênio/química
Ligação Proteica
Estrutura Terciária de Proteína
Especificidade por Substrato
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Flavoproteins); 0U46U6E8UK (NAD); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.5.3.- (Proline Oxidase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141211
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.625483


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[PMID]:25400271
[Au] Autor:Wan PJ; Fu KY; Lü FG; Wang XX; Guo WC; Li GQ
[Ad] Endereço:Education Ministry Key Laboratory of Integrated Management of Crop Diseases and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing, China.
[Ti] Título:Knocking down a putative Δ(1) -pyrroline-5-carboxylate dehydrogenase gene by RNA interference inhibits flight and causes adult lethality in the Colorado potato beetle Leptinotarsa decemlineata (Say).
[So] Source:Pest Manag Sci;71(10):1387-96, 2015 Oct.
[Is] ISSN:1526-4998
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Leptinotarsa decemlineata is an able disperser by flight. Novel control strategies must be explored to control the damage and inhibit the dispersal efficiently. Proline is a major energy substrate during flight. Δ-Pyrroline-5-carboxylate dehydrogenase (P5CDh) catalyses the second step of proline degradation for the production of ATP. RESULTS: A full-length Ldp5cdh cDNA was cloned. Ldp5cdh was ubiquitously expressed in the eggs, the first through fourth larval instars, wandering larvae, pupae and adults. In the adults, Ldp5cdh mRNA was widely distributed in thorax muscles, midgut, foregut, hindgut, Malpighian tubules, ventral ganglion, fat body and epidermis, with the expression levels from the highest to the lowest. Two double-stranded RNAs (dsRNAs) (dsLdp5cdh1 and dsLdp5cdh2) targeting Ldp5cdh were constructed and bacterially expressed. Ingestion of dsLdp5cdh1 and dsLdp5cdh2 successfully silenced Ldp5cdh, significantly increased the contents of proline, arginine and alanine, but strongly decreased the contents of asparate, asparagine, glutamate and glutamine in the haemolymph. Moreover, knocking down Ldp5cdh significantly reduced ATP content, decreased flight speed, shortened flight distance and increased adult mortality. CONCLUSIONS: It seems that identified Ldp5cdh encodes a functional P5CDh enzyme, and Ldp5cdh may serve as a potential target for dsRNA-based pesticide for controlling the damage and dispersal of L. decemlineata adults. © 2014 Society of Chemical Industry.
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/genética
Coleópteros/enzimologia
Coleópteros/fisiologia
Proteínas de Insetos/genética
Interferência de RNA
Solanum tuberosum/parasitologia
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/química
1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Sequência de Aminoácidos
Animais
Coleópteros/classificação
Coleópteros/genética
Feminino
Técnicas de Silenciamento de Genes
Controle de Insetos
Proteínas de Insetos/química
Proteínas de Insetos/metabolismo
Masculino
Dados de Sequência Molecular
Filogenia
Doenças das Plantas/parasitologia
RNA de Cadeia Dupla/genética
RNA de Cadeia Dupla/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Insect Proteins); 0 (RNA, Double-Stranded); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141118
[St] Status:MEDLINE
[do] DOI:10.1002/ps.3941


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[PMID]:25391710
[Au] Autor:Lachman A
[Ad] Endereço:a Department of Psychiatry , Stellenbosch University , Tygerberg Campus, Parow , South Africa . Author's email: anusha@sun.ac.za.
[Ti] Título:New developments in diagnosis and treatment update: Schizophrenia/first episode psychosis in children and adolescents.
[So] Source:J Child Adolesc Ment Health;26(2):109-24, 2014.
[Is] ISSN:1728-0591
[Cp] País de publicação:South Africa
[La] Idioma:eng
[Ab] Resumo:Childhood onset schizophrenia (COS) is diagnosed before the age of 13 years, and early onset schizophrenia (EOS) is diagnosed before the age of 18 years. EOS is considered extremely rare and its prevalence in comparison to the worldwide prevalence of schizophrenia (1%) has not adequately been studied. Patients who experience the first episode of psychosis need to be treated early and optimally to lessen the morbidity and improve the outcome of the illness. Treatment needs to be a combination of both pharmacological and non-pharmacological modalities. Pharmacological intervention is necessary for remission, improvement of positive symptoms and to aid with the efficacy of psychosocial interventions. There is a lack of efficacy and safety data of the use of antipsychotic medication in children, with most of the information available being extrapolations of adult data. An increased use of atypical antipsychotic drugs in the treatment of EOS has been accompanied by growing concern about the appropriate use and associated side effects in children and adolescents. This update highlights new developments, concepts and treatment trends in EOS.
[Mh] Termos MeSH primário: Esquizofrenia/terapia
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/deficiência
Administração Oral
Adolescente
Algoritmos
Erros Inatos do Metabolismo dos Aminoácidos/induzido quimicamente
Antipsicóticos/uso terapêutico
Doenças dos Gânglios da Base/induzido quimicamente
Doenças Cardiovasculares/induzido quimicamente
Criança
Transtornos Cognitivos/psicologia
Terapia Cognitiva/métodos
Preparações de Ação Retardada
Seres Humanos
Abuso de Maconha/complicações
Síndrome Metabólica/induzido quimicamente
Neuroimagem/métodos
Síndrome Maligna Neuroléptica/etiologia
Prolina Oxidase/deficiência
Puberdade/fisiologia
Fatores de Risco
Esquizofrenia/diagnóstico
Esquizofrenia/etiologia
Convulsões/induzido quimicamente
Resultado do Tratamento
Ganho de Peso/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antipsychotic Agents); 0 (Delayed-Action Preparations); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.5.3.- (Proline Oxidase)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141114
[St] Status:MEDLINE
[do] DOI:10.2989/17280583.2014.924416


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[PMID]:25345824
[Au] Autor:Gong M; Tang C; Zhu C
[Ad] Endereço:a Key Laboratory of Microbial Resources, Ministry of Agriculture / Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, Beijing 100081, People's Republic of China.
[Ti] Título:Cloning and expression of delta-1-pyrroline-5-carboxylate dehydrogenase in Escherichia coli DH5α improves phosphate solubilization.
[So] Source:Can J Microbiol;60(11):761-5, 2014 Nov.
[Is] ISSN:1480-3275
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:A primary cDNA library of Penicillium oxalicum I1 was constructed using the switching mechanism at the 5' end of the RNA transcript (SMART) technique. A total of 106 clones showed halos in tricalcium phosphate (TCP) medium, and clone I-40 showed clear halos. The full-length cDNA of clone I-40 was 1355 bp with a complete open reading frame (ORF) of 1032 bp, encoding a protein of 343 amino acids. Multiple alignment analysis revealed a high degree of homology between the ORF of clone I-40 and delta-1-pyrroline-5-carboxylate dehydrogenase (P5CDH) of other fungi. The ORF expression vector was constructed and transformed into Escherichia coli DH5α. The transformant (ORF-1) with the P5CDH gene secreted organic acid in medium with TCP as the sole source of phosphate. Acetic acid and α-ketoglutarate were secreted in 4 and 24 h, respectively. ORF-1 decreased the pH of the medium from 6.62 to 3.45 and released soluble phosphate at 0.172 mg·mL(-1) in 28 h. Expression of the P. oxalicum I1 p5cdh gene in E. coli could enhance organic acid secretion and phosphate-solubilizing ability.
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/genética
1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Fosfatos de Cálcio/metabolismo
Clonagem Molecular
Escherichia coli/genética
Penicillium/enzimologia
[Mh] Termos MeSH secundário: Ácido Acético/metabolismo
Escherichia coli/metabolismo
Biblioteca Gênica
Vetores Genéticos
Ácidos Cetoglutáricos/metabolismo
Penicillium/genética
Proteínas Recombinantes/metabolismo
Solubilidade
Transformação Bacteriana
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Phosphates); 0 (Ketoglutaric Acids); 0 (Recombinant Proteins); 8ID597Z82X (alpha-ketoglutaric acid); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); K4C08XP666 (tricalcium phosphate); Q40Q9N063P (Acetic Acid)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141028
[St] Status:MEDLINE
[do] DOI:10.1139/cjm-2014-0412


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[PMID]:25284427
[Au] Autor:Pang S; Lynn DA; Lo JY; Paek J; Curran SP
[Ad] Endereço:Davis School of Gerontology, University of Southern California, 3715 McClintock Avenue, Los Angeles, California 90089, USA.
[Ti] Título:SKN-1 and Nrf2 couples proline catabolism with lipid metabolism during nutrient deprivation.
[So] Source:Nat Commun;5:5048, 2014 Oct 06.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mechanisms that coordinate different metabolic pathways, such as glucose and lipid, have been recognized. However, a potential interaction between amino acid and lipid metabolism remains largely elusive. Here we show that during starvation of Caenorhabditis elegans, proline catabolism is coupled with lipid metabolism by SKN-1. Mutation of alh-6, a conserved proline catabolic enzyme, accelerates fat mobilization, enhances the expression of genes involved in fatty acid oxidation and reduces survival in response to fasting. This metabolic coordination is mediated by the activation of the transcription factor SKN-1/Nrf2, possibly due to the accumulation of the alh-6 substrate P5C, and also requires the transcriptional co-regulator MDT-15. Constitutive activation of SKN-1 induces a similar transcriptional response, which protects animals from fat accumulation when fed a high carbohydrate diet. In human cells, an orthologous alh-6 enzyme, ALDH4A1, is also linked to the activity of Nrf2, the human orthologue of SKN-1, and regulates the expression of lipid metabolic genes. Our findings identify a link between proline catabolism and lipid metabolism, and uncover a physiological role for SKN-1 in metabolism.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Ligação a DNA/metabolismo
Metabolismo dos Lipídeos
Fator 2 Relacionado a NF-E2/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Animais
Caenorhabditis elegans
Ácidos Graxos/química
Alimentos
Células HEK293
Seres Humanos
Metabolismo
Estresse Oxidativo
Oxigênio/química
Prolina/genética
Prolina/metabolismo
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (DNA-Binding Proteins); 0 (Fatty Acids); 0 (NF-E2-Related Factor 2); 0 (NFE2L2 protein, human); 0 (Transcription Factors); 148733-36-2 (skn-1 protein, C elegans); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.2.1.88 (ALDH4A1 protein, human); S88TT14065 (Oxygen)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141007
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms6048


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[PMID]:24980685
[Au] Autor:Ferreira AG; Scherer EB; da Cunha AA; Manfredini V; Biancini GB; Vanzin CS; Vargas CR; Wyse AT
[Ad] Endereço:Programa de Pós-Graduação em Ciências Biológicas: Bioquímica, ICBS, UFRGS, Rua Ramiro Barcelos, 2600-Anexo, CEP 90035-003, Porto Alegre, RS, Brazil. Electronic address: deiakf@gmail.com.
[Ti] Título:Hyperprolinemia induces DNA, protein and lipid damage in blood of rats: antioxidant protection.
[So] Source:Int J Biochem Cell Biol;54:20-5, 2014 Sep.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The present study investigated the effects of hyperprolinemia on oxidative damage to biomolecules (protein, lipids and DNA) and the antioxidant status in blood of rats. The influence of the antioxidants on the effects elicited by proline was also examined. Wistar rats received two daily injections of proline and/or vitamin E plus C (6th-28th day of life) and were killed 12h after the last injection. Results showed that hyperprolinemia induced a significant oxidative damage to proteins, lipids and DNA demonstrated by increased carbonyl content, malondialdehyde levels and a greater damage index in comet assay, respectively. The concomitant antioxidants administration to proline treatment completely prevented oxidative damage to proteins, but partially prevented lipids and DNA damage. We also observed that the non-enzymatic antioxidant potential was decreased by proline treatment and partially prevented by antioxidant supplementation. The plasma levels of vitamins E and C significantly increased in rats treated exogenously with these vitamins but, interestingly, when proline was administered concomitantly with vitamin E plus C, the levels of these vitamins were similar to those found in plasma of control and proline rats. Our findings suggest that hyperprolinemia promotes oxidative damage to the three major classes of macromolecules in blood of rats. These effects were accomplished by decrease in non-enzymatic antioxidant potential and decrease in vitamins administered exogenously, which significantly decreased oxidative damage to biomolecules studied. These data suggest that antioxidants may be an effective adjuvant therapeutic to limit oxidative damage caused by proline.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Aminoácidos/fisiopatologia
Antioxidantes/farmacologia
Dano ao DNA/efeitos dos fármacos
DNA/química
Lipídeos/química
Estresse Oxidativo/efeitos dos fármacos
Prolina Oxidase/deficiência
Proteínas/química
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/deficiência
Animais
Ácido Ascórbico/farmacologia
Suplementos Nutricionais
Masculino
Malondialdeído/metabolismo
Oxirredução
Prolina/química
Ratos
Ratos Wistar
Vitamina E/farmacologia
Vitaminas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Lipids); 0 (Proteins); 0 (Vitamins); 1406-18-4 (Vitamin E); 4Y8F71G49Q (Malondialdehyde); 9007-49-2 (DNA); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.5.3.- (Proline Oxidase); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140702
[St] Status:MEDLINE



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