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[PMID]:28414287
[Au] Autor:Tapbergenov SO; Sovetov BS; Tapbergenov AT; Hahn E
[Ad] Endereço:Department of Biochemistry and Chemical Disciplines, Semey State Medical University, Semey, Kazakhstan.
[Ti] Título:[Metabolic effects of combined introduction of adrenalin and blocker of methanoprolol beta-adrenophyleters].
[Ti] Título:Metabolicheskie éffekty sochetannogo vvedeniia adrenalina i blokatora beta-adrenoretseptorov metoprolola..
[So] Source:Biomed Khim;63(2):154-158, 2017 Mar.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The effect of combined administration of adrenaline (0.4 mg/kg, i.p.) and b1-blocker metoprolol (25 mg/kg) on the activity of glutathione peroxidase (GPO), glutathione reductase (GR), catalase, adenosine deaminase (AD), AMP deaminase (AMPD), 5¢-nucleotidase (5¢N), on the level ofmalonic dialdehyde (MDA) and conjugated dienes (CD) was investigated. In blood adrenaline administration to animals caused an increase in the activity of AMPD, AD, 5¢N and GPO, and the increase the level of CD in the blood increases. Metoprolol caused a more pronounced increase in the activity of blood AMPD, AD, 5'N and the amount of CD. In contrast to adrenaline, metoprolol decreased the MDA level of, and decreased the activity of GPO and catalase. Combined administration of metoprolol and adrenaline to animals was accompanied by an increase in the activity of AD, AMPD, 5¢N, a decrease in the activity of GR, GPO, catalase, and a decrease in MDA in the blood. In the heart, adrenaline injection was accompanied by an increase in the MDA level, a decrease in 5¢N activity and an increase in the ratio of the activities of the enzymes AD+AMPD/5¢N. Metoprolol injection reduced MDA and CD levels and the activity of GR and GPO. The combined administration of metoprolol and adrenaline in the heart was accompanied by activation of AD, AMPD and 5¢N, and a decrease in the amount of MDA and CD, and a decrease in the activity of GR, GPO, and catalase. In the liver adrenaline caused an increase in MDA and DC levels, activation of catalase, AD, AMPD, and 5¢N. Metoprolol caused a decrease in MDA and CD levels and activity of catalase and GPO, an increase in the activity of AD and AMPD in the liver. Combined administration of adrenaline and metoprolol reduced manifestations of the heart and liver oxidative stress response as compared with administration of adrenaline alone.
[Mh] Termos MeSH primário: Antagonistas de Receptores Adrenérgicos beta 1/farmacologia
Epinefrina/farmacologia
Coração/efeitos dos fármacos
Fígado/efeitos dos fármacos
Metoprolol/farmacologia
Simpatomiméticos/farmacologia
[Mh] Termos MeSH secundário: 5'-Nucleotidase/metabolismo
AMP Desaminase/metabolismo
Adenosina Desaminase/metabolismo
Animais
Animais não Endogâmicos
Antioxidantes/metabolismo
Catalase/metabolismo
Combinação de Medicamentos
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Injeções Intraperitoneais
Fígado/metabolismo
Malondialdeído/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adrenergic beta-1 Receptor Antagonists); 0 (Antioxidants); 0 (Drug Combinations); 0 (Sympathomimetics); 4Y8F71G49Q (Malondialdehyde); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.8.1.7 (Glutathione Reductase); EC 3.1.3.5 (5'-Nucleotidase); EC 3.5.4.4 (Adenosine Deaminase); EC 3.5.4.6 (AMP Deaminase); GEB06NHM23 (Metoprolol); YKH834O4BH (Epinephrine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.18097/PBMC20176302154


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[PMID]:28159278
[Au] Autor:Li D; Zhang L; Song S; Wang Z; Kong C; Luo Y
[Ad] Endereço:Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, PR China.
[Ti] Título:The role of microorganisms in the degradation of adenosine triphosphate (ATP) in chill-stored common carp (Cyprinus carpio) fillets.
[So] Source:Food Chem;224:347-352, 2017 Jun 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Biochemical and microbial changes after harvest strongly affect the final quality and shelf life of fish and fish products. In this study, the role of microbes in the degradation of adenosine triphosphate (ATP), and the origin of adenosine monophosphate deaminase (AMPD) and acid phosphatase (ACP) in common carp fillets during different stages of chilled storage (at 4°C) were investigated. The content of ATP, ADP, AMP, IMP, HxR, and Hx, the activity of AMPD and ACP, and the total count of viable, Aeromonas, Pseudomonas, H S-producing bacteria, and lactic acid bacteria were examined. Results indicated that the population of microbial communities in control samples increased with storage time, and Pseudomonas peaked on the 10th day of storage. Changes in AMPD activity were less related to the abundance of microbes during the entire storage period. However, ACP was derived from both fish muscle and microbial secretion during the middle and late stages of storage. Degradation of ATP to IMP was not affected by spoilage bacteria, but the hydrolysis of IMP, and the transformation of HxR to Hx was affected considerably by the spoilage bacteria.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Carpas/microbiologia
Armazenamento de Alimentos
Alimentos Marinhos/microbiologia
[Mh] Termos MeSH secundário: AMP Desaminase/metabolismo
Fosfatase Ácida/metabolismo
Aeromonas/isolamento & purificação
Aeromonas/metabolismo
Animais
Temperatura Baixa
Contagem de Colônia Microbiana
Análise de Alimentos
Contaminação de Alimentos
Microbiologia de Alimentos
Lactobacillus/isolamento & purificação
Lactobacillus/metabolismo
Pseudomonas/isolamento & purificação
Pseudomonas/metabolismo
Alimentos Marinhos/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 3.1.3.2 (Acid Phosphatase); EC 3.5.4.6 (AMP Deaminase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170205
[St] Status:MEDLINE


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[PMID]:27991918
[Au] Autor:Hong S; Zhou W; Fang B; Lu W; Loro E; Damle M; Ding G; Jager J; Zhang S; Zhang Y; Feng D; Chu Q; Dill BD; Molina H; Khurana TS; Rabinowitz JD; Lazar MA; Sun Z
[Ad] Endereço:Division of Diabetes, Endocrinology and Metabolism, Department of Medicine, Baylor College of Medicine, Houston, Texas, USA.
[Ti] Título:Dissociation of muscle insulin sensitivity from exercise endurance in mice by HDAC3 depletion.
[So] Source:Nat Med;23(2):223-234, 2017 Feb.
[Is] ISSN:1546-170X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type 2 diabetes and insulin resistance are associated with reduced glucose utilization in the muscle and poor exercise performance. Here we find that depletion of the epigenome modifier histone deacetylase 3 (HDAC3) specifically in skeletal muscle causes severe systemic insulin resistance in mice but markedly enhances endurance and resistance to muscle fatigue, despite reducing muscle force. This seemingly paradoxical phenotype is due to lower glucose utilization and greater lipid oxidation in HDAC3-depleted muscles, a fuel switch caused by the activation of anaplerotic reactions driven by AMP deaminase 3 (Ampd3) and catabolism of branched-chain amino acids. These findings highlight the pivotal role of amino acid catabolism in muscle fatigue and type 2 diabetes pathogenesis. Further, as genome occupancy of HDAC3 in skeletal muscle is controlled by the circadian clock, these results delineate an epigenomic regulatory mechanism through which the circadian clock governs skeletal muscle bioenergetics. These findings suggest that physical exercise at certain times of the day or pharmacological targeting of HDAC3 could potentially be harnessed to alter systemic fuel metabolism and exercise performance.
[Mh] Termos MeSH primário: Histona Desacetilases/genética
Resistência à Insulina/genética
Metabolismo dos Lipídeos/genética
Fadiga Muscular/genética
Força Muscular/genética
Músculo Esquelético/metabolismo
Condicionamento Físico Animal
Resistência Física/genética
[Mh] Termos MeSH secundário: AMP Desaminase/metabolismo
Aminoácidos de Cadeia Ramificada/metabolismo
Animais
Western Blotting
Composição Corporal
Ritmo Circadiano/genética
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/metabolismo
Metabolismo Energético
Epigênese Genética
Técnicas de Silenciamento de Genes
Técnica Clamp de Glucose
Código das Histonas/genética
Camundongos
Proteômica
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (histone deacetylase 3); EC 3.5.4.6 (AMP Deaminase); EC 3.5.4.6 (AMPD3 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161220
[St] Status:MEDLINE
[do] DOI:10.1038/nm.4245


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[PMID]:27662835
[Au] Autor:Chew BL; Fisk ID; Fray R; Tucker GA; Bodi Z; Ferguson A; Xia W; Seymour GB
[Ad] Endereço:School of Biological Sciences, Universiti Sains Malaysia, 11800, Penang, Malaysia.
[Ti] Título:The effect of adenosine monophosphate deaminase overexpression on the accumulation of umami-related metabolites in tomatoes.
[So] Source:Plant Cell Rep;36(1):81-87, 2017 Jan.
[Is] ISSN:1432-203X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: This study highlights the changes in umami-related nucleotide and glutamate levels when the AMP deaminase gene was elevated in transgenic tomato. Taste is perceived as one of a combination of five sensations, sweet, sour, bitter, salty, and umami. The umami taste is best known as a savoury sensation and plays a central role in food flavour, palatability, and eating satisfaction. Umami flavour can be imparted by the presence of glutamate and is greatly enhanced by the addition of ribonucleotides, such as inosine monophosphate (IMP) and guanosine monophosphate (GMP). The production of IMP is regulated by the enzyme adenosine monophosphate (AMP) deaminase which functions to convert AMP into IMP. We have generated transgenic tomato (Solanum lycopersicum) lines over expressing AMP deaminase under the control of a fruit-specific promoter. The transgenic lines showed substantially enhanced levels of AMP deaminase expression in comparison to the wild-type control. Elevated AMP deaminase levels resulted in the reduced accumulation of glutamate and increased levels of the umami nucleotide GMP. AMP concentrations were unchanged. The effects on the levels of glutamate and GMP were unexpected and are discussed in relation to the metabolite flux within this pathway.
[Mh] Termos MeSH primário: AMP Desaminase/metabolismo
Lycopersicon esculentum/enzimologia
Metaboloma
Paladar
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/metabolismo
Frutas/genética
Frutas/metabolismo
Regulação da Expressão Gênica de Plantas
Genes de Plantas
Ácido Glutâmico/metabolismo
Guanosina Monofosfato/metabolismo
Lycopersicon esculentum/genética
Lycopersicon esculentum/metabolismo
Metaboloma/genética
Proteínas de Plantas
Plantas Geneticamente Modificadas
Reação em Cadeia da Polimerase em Tempo Real
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 3KX376GY7L (Glutamic Acid); 415SHH325A (Adenosine Monophosphate); 85-32-5 (Guanosine Monophosphate); EC 3.5.4.6 (AMP Deaminase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE
[do] DOI:10.1007/s00299-016-2058-z


  5 / 1013 MEDLINE  
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[PMID]:27596420
[Au] Autor:Li S; Chen L; Hu Y; Fang G; Zhao M; Guo Y; Pang Z
[Ad] Endereço:College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China.
[Ti] Título:Enzymatic production of 5'-inosinic acid by AMP deaminase from a newly isolated Aspergillus oryzae.
[So] Source:Food Chem;216:275-81, 2017 Feb 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:5'-adenylic acid deaminase (AMP deaminase), an important enzyme for the food industry, can catalyze the irreversible hydrolysis of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia. In this study, a new strain was screened that efficiently produces 3191.6U/g of AMP deaminase at 32°C. After purification, the optimal temperature and pH of the AMP deaminase were found to be 40°C and 6.0, respectively, but it was partially inhibited by Fe(3+), Cu(2+), Al(3+), and Zn(2+). With amplification of the AMP deaminase production system, 6mL of crude enzyme could produce 2.00mg/g of IMP from 2.04mg/g of dried yeast with an 84.8% molar yield after 40min. These results provide a new insight into AMP deaminase production and offer a potential platform for producing 5'-IMP.
[Mh] Termos MeSH primário: AMP Desaminase/análise
AMP Desaminase/biossíntese
Aspergillus oryzae/isolamento & purificação
Inosina Monofosfato/análise
Inosina Monofosfato/biossíntese
[Mh] Termos MeSH secundário: Ativação Enzimática/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
131-99-7 (Inosine Monophosphate); EC 3.5.4.6 (AMP Deaminase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170104
[Lr] Data última revisão:
170104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160907
[St] Status:MEDLINE


  6 / 1013 MEDLINE  
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[PMID]:28026807
[Au] Autor:Tapbergenov SO; Sovetov BS; Tapbergenov AT
[Ad] Endereço:Department of Biochemistry and Chemical disciplines, Semey State Medical University, Semey, Kazakhstan.
[Ti] Título:[Features of influence adenosine, AMP and hyperadrenalinemiya on the immune status, metabolic enzymes of purine nucleotides and the antioxidant defense system].
[Ti] Título:Osobennosti vozdeistviia adenozina, AMP i giperadrenalinemii na immunnyi status, fermenty metabolizma purinovykh nukleotidov i sistemu antioksidantnoi zashchity..
[So] Source:Biomed Khim;62(6):645-649, 2016 Nov.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Administration of a large dose of adrenaline (4 mg/kg 60 min before analysis) increased blood levels of total leukocytes, lymphocytes, decreased T-cell suppressors, leukocyte migration inhibition reaction (LMIR) and NBT test, but increased the level of conjugated dienes (CD). Administration of AMPand adenosine increased levels of total leukocytes, lymphocytes, T- lymphocytes, T-helpers, decreased the level of malondialdehyde (MDA), LMIR, and T-cell suppressors. Sympathetic hyperactivation induced by administration of a large dose of adrenaline (4 mg/kg 60 min before analysis) was accompanied by an increase in heart and liver activities of glutathione peroxidase (GPx), catalase, AMP deaminase (AMPD), and adenosine deaminase (AD). Administration of AMP or adenosine caused a decrease in activities of glutathione reductase (GR), GPx, catalase, a decrease in the MDA level and an increase in activities of AMPD and AD in the heart. In the liver AMP and adenosine also caused a decrease in activities of glutathione reductase (GR), GPx, a decrease in the MDA level and an increase in activities of AMPD and AD. The data obtained suggest that administration of adrenaline, AMP, and adenosine influences activity of enzymes involved in purine nucleotide metabolism. However, in contrast to adrenaline, administration of AMP or adenosine does not provoke stress reaction.
[Mh] Termos MeSH primário: AMP Desaminase/sangue
Adenosina Desaminase/sangue
Monofosfato de Adenosina/farmacologia
Adenosina/farmacologia
Hiperfunção Adrenocortical
Oxirredutases/sangue
[Mh] Termos MeSH secundário: Hiperfunção Adrenocortical/sangue
Hiperfunção Adrenocortical/imunologia
Animais
Antioxidantes/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 415SHH325A (Adenosine Monophosphate); EC 1.- (Oxidoreductases); EC 3.5.4.4 (Adenosine Deaminase); EC 3.5.4.6 (AMP Deaminase); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE
[do] DOI:10.18097/PBMC20166206645


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[PMID]:27906632
[Au] Autor:Toczek M; Kutryb-Zajac B; Zukowska P; Slominska EM; Isalan M; Mielcarek M; Smolenski RT
[Ad] Endereço:a Department of Biochemistry , Medical University of Gdansk , Gdansk , Poland.
[Ti] Título:Changes in cardiac nucleotide metabolism in Huntington's disease.
[So] Source:Nucleosides Nucleotides Nucleic Acids;35(10-12):707-712, 2016 Dec.
[Is] ISSN:1532-2335
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Huntington's disease (HD) is a monogenic neurodegenerative disorder with a significant peripheral component to the disease pathology. This includes an HD-related cardiomyopathy, with an unknown pathological mechanism. In this study, we aimed to define changes in the metabolism of cardiac nucleotides using the well-established R6/2 mouse model. In particular, we focused on measuring the activity of enzymes that control ATP and other adenine nucleotides in the cardiac pool, including eNTPD, AMPD, e5'NT, ADA, and PNP. We employed HPLC to assay the activities of these enzymes by measuring the concentrations of adenine nucleotide catabolites in the hearts of symptomatic R6/2 mice. We found a reduced activity of AMPD (12.9 ± 1.9 nmol/min/mg protein in control; 7.5 ± 0.5 nmol/min/mg protein in R6/2) and e5'NT (11.9 ± 1.7 nmol/min/mg protein in control; 6.7 ± 0.7 nmol/min/mg protein in R6/2). Moreover, we detected an increased activity of ADA (1.3 ± 0.2 nmol/min/mg protein in control; 5.2 ± 0.5 nmol/min/mg protein in R6/2), while no changes in eNTPD and PNP activities were observed. Analysis of cardiac adenine nucleotide catabolite levels revealed an increased inosine level (0.7 ± 0.01 nmol/mg dry tissue in control; 2.7 ±0.8 nmol/mg dry tissue in R6/2) and a reduced concentration of cardiac adenosine (0.9 ± 0.2 nmol/mg dry tissue in control; 0.2 ± 0.08 nmol/mg dry tissue in R6/2). This study highlights a decreased rate of degradation of cardiac nucleotides in HD mouse model hearts, and an increased capacity for adenosine deamination, that may alter adenosine signaling.
[Mh] Termos MeSH primário: Adenosina/metabolismo
Doença de Huntington/metabolismo
Inosina/metabolismo
Miocárdio/metabolismo
[Mh] Termos MeSH secundário: AMP Desaminase/metabolismo
Adenosina Desaminase/metabolismo
Animais
Modelos Animais de Doenças
Seres Humanos
Camundongos
Purina-Núcleosídeo Fosforilase/metabolismo
Pirofosfatases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
5A614L51CT (Inosine); EC 2.4.2.1 (Purine-Nucleoside Phosphorylase); EC 3.5.4.4 (Adenosine Deaminase); EC 3.5.4.6 (AMP Deaminase); EC 3.6.1.- (Pyrophosphatases); EC 3.6.1.- (nucleoside-triphosphate diphosphohydrolase 3); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


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[PMID]:27760513
[Au] Autor:Joshi PR; Apitz T; Zierz S
[Ad] Endereço:a Department of Neurology , Martin-Luther-University Halle-Wittenberg , Halle (Saale) , Germany.
[Ti] Título:Normal activities of AMP-deaminase and adenylate kinase in patients with McArdle disease.
[So] Source:Neurol Res;38(12):1052-1055, 2016 Dec.
[Is] ISSN:1743-1328
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:During physical activity in McArdle patients, little or no lactate is released in the skeletal muscle. However, excessive ammonia production has frequently been reported in these patients. Production of ammonia is catalysed by AMP deaminase (AMPD) and adenylate kinase (AK). The activities of AMPD and AK along with housekeeping enzyme phosphoglucoisomerase (PGI) were measured in 11 genetically confirmed McArdle patients and compared with 27 healthy controls. The AMPD and AK activities were not significantly different in patients and controls. The activity of PGI was significantly higher in patients than in controls suggesting compensation of the impaired glycogenolysis in McArdle. The ratios of activities of AMPD and AK over PGI were significantly lower in patients than in controls. High ammonia production in McArdle patients is not based on enzyme induction of AMPD and AK but possibly due to kinetic activation of the enzyme AMPD by increased concentration of the substrate AMP.
[Mh] Termos MeSH primário: AMP Desaminase/metabolismo
Adenilato Quinase/metabolismo
Doença de Depósito de Glicogênio Tipo V/enzimologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Feminino
Antebraço/fisiologia
Seres Humanos
Ácido Láctico/metabolismo
Masculino
Meia-Idade
Fosfoglucomutase/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
33X04XA5AT (Lactic Acid); EC 2.7.4.3 (Adenylate Kinase); EC 3.5.4.6 (AMP Deaminase); EC 5.4.2.2 (Phosphoglucomutase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170124
[Lr] Data última revisão:
170124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE


  9 / 1013 MEDLINE  
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[PMID]:27539573
[Au] Autor:Li S; Qian Y; Liang Y; Chen X; Zhao M; Guo Y; Pang Z
[Ad] Endereço:College of Light Industry and Food Engineering, Guangxi University, Nanning, 530004, China.
[Ti] Título:Overproduction, Purification and Characterization of Adenylate Deaminase from Aspergillus oryzae.
[So] Source:Appl Biochem Biotechnol;180(8):1635-1643, 2016 Dec.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Adenylate deaminase (AMPD, EC 3.5.4.6) is an aminohydrolase that widely used in the food and medicine industries. In this study, the gene encoding Aspergillus oryzae AMPD was cloned and expressed in Escherichia coli. Induction with 0.75 mM isopropyl ß-D-l-thiogalactopyranoside resulted in an enzyme activity of 1773.9 U/mL. Recombinant AMPD was purified to electrophoretic homogeneity using nickel affinity chromatography, and its molecular weight was calculated as 78.6 kDa. Purified AMPD exhibited maximal activity at 35 °C, pH 6.0 and 30 mM K , with apparent K and V values of 2.7 × 10 M and 77.5 µmol/mg/min under these conditions. HPLC revealed that recombinant AMPD could effectively catalyse the synthesis of inosine-5'-monophosphate (IMP) with minimal by-products, indicating high specificity and suggesting that it could prove useful for IMP production.
[Mh] Termos MeSH primário: AMP Desaminase/isolamento & purificação
AMP Desaminase/metabolismo
Aspergillus oryzae/enzimologia
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/química
Monofosfato de Adenosina/metabolismo
Aspergillus oryzae/efeitos dos fármacos
Biocatálise/efeitos dos fármacos
Clonagem Molecular
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática/efeitos dos fármacos
Concentração de Íons de Hidrogênio
Inosina Monofosfato/química
Inosina Monofosfato/metabolismo
Íons
Cinética
Metais/farmacologia
Peso Molecular
Proteínas Recombinantes/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ions); 0 (Metals); 0 (Recombinant Proteins); 131-99-7 (Inosine Monophosphate); 415SHH325A (Adenosine Monophosphate); EC 3.5.4.6 (AMP Deaminase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


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[PMID]:27525900
[Au] Autor:Maltese PE; Venturini L; Poplavskaya E; Bertelli M; Cecchin S; Granato M; Nikulina SY; Salmina A; Aksyutina N; Capelli E; Ricevuti G; Lorusso L
[Ad] Endereço:MAGI Non-Profit Human Medical Genetics Institute, Rovereto, TN, Italy paolo.maltese@assomagi.org.
[Ti] Título:Genetic evaluation of AMPD1, CPT2, and PGYM metabolic enzymes in patients with chronic fatigue syndrome.
[So] Source:Genet Mol Res;15(3), 2016 Jul 29.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:Chronic fatigue syndrome (CFS) is a disease that can seriously impair one's quality of life; patients complain of excessive fatigue and myalgia following physical exertion. This disease may be associated with abnormalities in genes affecting exercise tolerance and physical performance. Adenosine monophosphate deaminase (AMPD1), carnitine palmitoyltransferase II (CPT2), and the muscle isoform of glycogen phosphorylase (PYGM) genes provide instructions for producing enzymes that play major roles in energy production during work. The aim of this study was to look for evidence of genotype-associated excessive muscle fatigue. Three metabolic genes (AMPD1, CPT2, and PYGM) were therefore fully sequenced in 17 Italian patients with CFS. We examined polymorphisms known to alter the function of these metabolic genes, and compared their genotypic distributions in CFS patients and 50 healthy controls using chi-square tests and odds ratios. One-way analysis of variance with F-ratio was carried out to determine the associations between genotypes and disease severity using CF scores. No major genetic variations between patients and controls were found in the three genes studied, and we did not find any association between these genes and CFS. In conclusion, variations in AMPD1, CPT2, and PGYM genes are not associated with the onset, susceptibility, or severity of CFS.
[Mh] Termos MeSH primário: AMP Desaminase/genética
Carnitina O-Palmitoiltransferase/genética
Síndrome de Fadiga Crônica/genética
Glicogênio Fosforilase Muscular/genética
[Mh] Termos MeSH secundário: AMP Desaminase/metabolismo
Adolescente
Adulto
Carnitina O-Palmitoiltransferase/metabolismo
Estudos de Casos e Controles
Síndrome de Fadiga Crônica/enzimologia
Feminino
Expressão Gênica
Estudos de Associação Genética
Predisposição Genética para Doença
Glicogênio Fosforilase Muscular/metabolismo
Seres Humanos
Masculino
Meia-Idade
Polimorfismo Genético
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.4.1.- (Glycogen Phosphorylase, Muscle Form); EC 3.5.4.6 (AMP Deaminase); EC 3.5.4.6 (AMPD1 protein, human)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170303
[Lr] Data última revisão:
170303
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE
[do] DOI:10.4238/gmr.15038717



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