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[PMID]:29309428
[Au] Autor:Sarika K; Hossain F; Muthusamy V; Zunjare RU; Baveja A; Goswami R; Thirunavukkarasu N; Jha SK; Gupta HS
[Ad] Endereço:Division of Genetics, ICAR-Indian Agricultural Research Institute, New Delhi, India.
[Ti] Título:Opaque16, a high lysine and tryptophan mutant, does not influence the key physico-biochemical characteristics in maize kernel.
[So] Source:PLoS One;13(1):e0190945, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The enhancement of lysine and tryptophan in maize is so far basedon opaque2(o2) mutant, that along with the endosperm-modifiersled to development of Quality Protein Maize[QPM]. Though many mutants improving the endospermic protein quality were discovered, they could not be successfully deployed. Recently discovered opaque16 (o16)mutant enhances the lysine and tryptophan content in maize endosperm. In the present study, the influence of o16 on the endosperm modification was analyzed in four F2 populations, two each segregating for o16 allele alone and in combination with o2. The recessive o16o16 seed endosperm was found to be vitreousphenotypically similar to wild-O16O16. The mutant did not influence the degree of kernel opaqueness in o2o2 genetic background as opaqueness in o2o2/O16O16 and o2o2/o16o16 was similar. Grain hardness of o16o16 was comparable with the normal and QPM maize. The pattern of microscopic organization of proteinaceous matrix and starch granules, and zein profiling of the storage protein in o16o16 were found to be similar with normal maize endosperm, but distinct from the o2o2-soft genotype. The pattern in o2o2/o16o16 was unique and different from o2o2 and o16o16 as well. Here we demonstrated the effects of o16 on physico-biochemical characteristics of endosperm and report of o16 possessing negligible influence on kernel modification and hardness, which holds a great significance in maize quality breeding programme.
[Mh] Termos MeSH primário: Lisina/metabolismo
Mutação
Proteínas de Plantas/metabolismo
Triptofano/metabolismo
Zea mays/metabolismo
[Mh] Termos MeSH secundário: Genes de Plantas
Marcadores Genéticos
Proteínas de Plantas/química
Proteínas de Plantas/genética
Zea mays/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Genetic Markers); 0 (Plant Proteins); 8DUH1N11BX (Tryptophan); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190945


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[PMID]:29231001
[Au] Autor:Wu JY; Wang D; Kong J; Wang XX; Yu XJ
[Ad] Endereço:Department of Forensic Pathology, Medical College, Shantou University, Shantou 515041, China.
[Ti] Título:[Metabolic Characteristics of Lethal Bradycardia Induced by Myocardial Ischemia].
[So] Source:Fa Yi Xue Za Zhi;33(1):11-16, 2017 Feb.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVES: To explore the metabolic characteristics of lethal bradycardia induced by myocardial ischemia in rat's serum. METHODS: A rat myocardial ischemia-bradycardia-sudden cardiac death (MI-B-SCD) model was established, which was compared with the sham-operation group. The metabolic profile of postmortem serum was analyzed by gas chromatography-mass spectrometry (GC-MS), coupled with the analysis of serum metabolic characteristics using metabolomics strategies. RESULTS: The serum metabolic profiles were significantly different between the MI-B-SCD rats and the control rats. Compared to the control rats, the MI-B-SCD rats had significantly higher levels of lysine, ornithine, purine, serine, alanine, urea and lactic acid; and significantly lower levels of succinate, hexadecanoic acid, 2-ketoadipic acid, glyceraldehyde, hexendioic acid and octanedioic acid in the serum. There were some correlations among different metabolites. CONCLUSIONS: There is obvious metabolic alterations in the serum of MI-B-SCD rat. Both lysine and purine have a high value in diagnosing MI-B-SCD. The results are expected to provide references for forensic and clinical applications of prevention and control of sudden cardiac death.
[Mh] Termos MeSH primário: Bradicardia/metabolismo
Morte Súbita Cardíaca
Cromatografia Gasosa-Espectrometria de Massas/métodos
Metabolômica/métodos
Isquemia Miocárdica/metabolismo
[Mh] Termos MeSH secundário: Animais
Bradicardia/patologia
Doença da Artéria Coronariana
Modelos Animais de Doenças
Lisina/sangue
Lisina/metabolismo
Isquemia Miocárdica/diagnóstico
Purinas/sangue
Purinas/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Purines); K3Z4F929H6 (Lysine); W60KTZ3IZY (purine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2017.01.003


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[PMID]:28461104
[Au] Autor:Prokop S; Perry NA; Vishnivetskiy SA; Toth AD; Inoue A; Milligan G; Iverson TM; Hunyady L; Gurevich VV
[Ad] Endereço:Department of Physiology, Faculty of Medicine, Semmelweis University, Budapest, Hungary.
[Ti] Título:Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.
[So] Source:Cell Signal;36:98-107, 2017 Aug.
[Is] ISSN:1873-3913
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Non-visual arrestins interact with hundreds of different G protein-coupled receptors (GPCRs). Here we show that by introducing mutations into elements that directly bind receptors, the specificity of arrestin-3 can be altered. Several mutations in the two parts of the central "crest" of the arrestin molecule, middle-loop and C-loop, enhanced or reduced arrestin-3 interactions with several GPCRs in receptor subtype and functional state-specific manner. For example, the Lys139Ile substitution in the middle-loop dramatically enhanced the binding to inactive M muscarinic receptor, so that agonist activation of the M did not further increase arrestin-3 binding. Thus, the Lys139Ile mutation made arrestin-3 essentially an activation-independent binding partner of M , whereas its interactions with other receptors, including the ß -adrenergic receptor and the D and D dopamine receptors, retained normal activation dependence. In contrast, the Ala248Val mutation enhanced agonist-induced arrestin-3 binding to the ß -adrenergic and D dopamine receptors, while reducing its interaction with the D dopamine receptor. These mutations represent the first example of altering arrestin specificity via enhancement of the arrestin-receptor interactions rather than selective reduction of the binding to certain subtypes.
[Mh] Termos MeSH primário: Arrestinas/metabolismo
Receptores Acoplados a Proteínas-G/agonistas
Receptores Acoplados a Proteínas-G/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Arrestinas/química
Células COS
Bovinos
Cercopithecus aethiops
Sequência Conservada
Células HEK293
Seres Humanos
Lisina/metabolismo
Proteínas Mutantes/metabolismo
Mutação/genética
Ligação Proteica
Estrutura Secundária de Proteína
Rodopsina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arrestins); 0 (Mutant Proteins); 0 (Receptors, G-Protein-Coupled); 0 (arrestin3); 9009-81-8 (Rhodopsin); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:28460646
[Au] Autor:Markusic DM; Nichols TC; Merricks EP; Palaschak B; Zolotukhin I; Marsic D; Zolotukhin S; Srivastava A; Herzog RW
[Ad] Endereço:Department of Pediatrics, University of Florida, Gainesville, FL, 32610, USA. dmarkusic@ufl.edu.
[Ti] Título:Evaluation of engineered AAV capsids for hepatic factor IX gene transfer in murine and canine models.
[So] Source:J Transl Med;15(1):94, 2017 May 01.
[Is] ISSN:1479-5876
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Adeno-associated virus (AAV) gene therapy vectors have shown the best outcomes in human clinical studies for the treatment of genetic diseases such as hemophilia. However, these pivotal investigations have also identified several challenges. For example, high vector doses are often used for hepatic gene transfer, and cytotoxic T lymphocyte responses against viral capsid may occur. Therefore, achieving therapy at reduced vector doses and other strategies to reduce capsid antigen presentation are desirable. METHODS: We tested several engineered AAV capsids for factor IX (FIX) expression for the treatment of hemophilia B by hepatic gene transfer. These capsids lack potential phosphorylation or ubiquitination sites, or had been generated through molecular evolution. RESULTS: AAV2 capsids lacking either a single lysine residue or 3 tyrosine residues directed substantially higher coagulation FIX expression in mice compared to wild-type sequence or other mutations. In hemophilia B dogs, however, expression from the tyrosine-mutant vector was merely comparable to historical data on AAV2. Evolved AAV2-LiC capsid was highly efficient in hemophilia B mice but lacked efficacy in a hemophilia B dog. CONCLUSIONS: Several alternative strategies for capsid modification improve the in vivo performance of AAV vectors in hepatic gene transfer for correction of hemophilia. However, capsid optimization solely in mouse liver may not predict efficacy in other species and thus is of limited translational utility.
[Mh] Termos MeSH primário: Capsídeo/metabolismo
Dependovirus/genética
Fator IX/genética
Técnicas de Transferência de Genes
Engenharia Genética
[Mh] Termos MeSH secundário: Animais
Cães
Vetores Genéticos/metabolismo
Hemofilia B/genética
Hepatócitos/metabolismo
Fígado/metabolismo
Lisina/genética
Masculino
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Modelos Animais
Mutação/genética
Transdução Genética
Tirosina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
42HK56048U (Tyrosine); 9001-28-9 (Factor IX); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1186/s12967-017-1200-1


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[PMID]:29339748
[Au] Autor:Lee S; Oh S; Jeong K; Jo H; Choi Y; Seo HD; Kim M; Choe J; Kwon CS; Lee D
[Ad] Endereço:Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
[Ti] Título:Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.
[So] Source:Nat Commun;9(1):240, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2-Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.
[Mh] Termos MeSH primário: Chaperonas de Histonas/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Proteínas Nucleares/metabolismo
Nucleossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cromatina/genética
Cromatina/metabolismo
Regulação Fúngica da Expressão Gênica
Chaperonas de Histonas/genética
Histona-Lisina N-Metiltransferase/genética
Histonas/metabolismo
Lisina/metabolismo
Mutação
Proteínas Nucleares/genética
Nucleossomos/genética
Ligação Proteica
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Histone Chaperones); 0 (Histones); 0 (Nuclear Proteins); 0 (Nucleosomes); 0 (Saccharomyces cerevisiae Proteins); EC 2.1.1.43 (Dot1 protein, S cerevisiae); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02759-8


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[PMID]:29037697
[Au] Autor:Hu Y; Shao Y; Wu C; Yuan C; Ishimura G; Liu W; Chen S
[Ad] Endereço:National Engineering Laboratory of Intelligent Food Technology and Equipment, Key Laboratory for Agro-Products Postharvest Handling of Ministry of Agriculture, Key Laboratory for Agro-Products Nutritional Evaluation of Ministry of Agriculture, Zhejiang Key Laboratory for Agro-Food Processing, Fuli I
[Ti] Título:γ-PGA and MTGase improve the formation of ε-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein.
[So] Source:Food Chem;242:330-337, 2018 Mar 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The present study investigated the mechanism of ε-(γ-glutamyl) lysine cross-links within hairtail (Trichiurus haumela) surimi protein via γ-polyglutamic acid (γ-PGA) and MTGase. The results indicated that the addition of MTGase and γ-PGA markedly improved the gelation properties of hairtail surimi protein, including its maximum breaking force and deformation, water holding capacity and gel strength. The maximum improvements were achieved by adding 0.5units MTGase/g meat paste in combination with 0.06% γ-PGA. SDS-PAGE showed that the band intensity of cross-linked proteins increased, whereas that of myosin heavy chain decreased after treatments. Further scanning electron microscopy (SEM) analysis showed the formation of a denser gel matrix, which was caused by much stronger and more inter- and intra-molecular cross-linking of proteins, via MTGase catalysing ε-(γ-glutamyl) lysine cross-links formed between lysine residues in the gel protein and glutamic residues in the hydrolytic γ-PGA. The results provide reliable guidance for the improvement of hairtail surimi protein gelation properties.
[Mh] Termos MeSH primário: Produtos Pesqueiros
Manipulação de Alimentos/métodos
Géis/química
Lisina/química
Perciformes
Ácido Poliglutâmico/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Eletroforese em Gel de Poliacrilamida
Lisina/metabolismo
Ácido Poliglutâmico/química
Ácido Poliglutâmico/metabolismo
Transglutaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gels); 0 (poly(gamma-glutamic acid)); 25513-46-6 (Polyglutamic Acid); EC 2.3.2.13 (Transglutaminases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE


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[PMID]:29288669
[Au] Autor:Kobayashi F; Nishiuchi T; Takaki K; Konno H
[Ad] Endereço:Graduate School of Natural Science & Technology, Kanazawa University, Kanazawa 920-1192, Japan.
[Ti] Título:Ubiquitin chain specificities of E6AP E3 ligase and its HECT domain.
[So] Source:Biochem Biophys Res Commun;496(2):686-692, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ubiquitination of target proteins is accomplished by isopeptide bond formation between the carboxy group of the C-terminal glycine (Gly) residue of ubiquitin (Ub) and the É›-amino group of lysine (Lys) on the target proteins. The formation of an isopeptide bond between Ubs that gives rise to a poly-Ub chain on the target proteins and the types of poly-Ub chains formed depend on which of the seven Lys residues or N-terminal methionine (Met) residue on Ub is used for chain elongation. To understand the linkage specificity mechanism of Ub chains on E3, the previous study established an assay to monitor the formation of a free diubiquitin chain (Ub chain synthesis assay) by HECT type E3 ligase. In this study, we investigated Ub chain specificity using E6AP HECT domain. We here demonstrate the importance of the N-terminal domain of full length E6AP for Ub chain specificity.
[Mh] Termos MeSH primário: Ubiquitina-Proteína Ligases/metabolismo
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Células HEK293
Seres Humanos
Lisina/análise
Lisina/metabolismo
Metionina/análise
Metionina/metabolismo
Poliubiquitina/química
Poliubiquitina/metabolismo
Domínios Proteicos
Ubiquitina/química
Ubiquitina-Proteína Ligases/química
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ubiquitin); 120904-94-1 (Polyubiquitin); AE28F7PNPL (Methionine); EC 2.3.2.26 (UBE3A protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


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[PMID]:29198865
[Au] Autor:Kakizawa T; Ota Y; Itoh Y; Suzuki T
[Ad] Endereço:Department of Chemistry and Biochemistry, School of Advanced Science and Engineering, Waseda University, Shinjuku, Tokyo 169-8555, Japan.
[Ti] Título:Histone H3 peptides incorporating modified lysine residues as lysine-specific demethylase 1 inhibitors.
[So] Source:Bioorg Med Chem Lett;28(2):167-169, 2018 01 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lysine-specific demethylase 1 (LSD1) is a flavin-dependent enzyme that removes methyl groups from mono- or dimethylated lysine residues at the fourth position of histone H3. We have previously reported several histone H3 peptides containing an LSD1 inactivator motif at Lys-4. In this study, histone H3 peptides having a trans-2-phenylcyclopropylamine (PCPA), a 2,5-dihydro-1H-pyrrole, and a 1,2,3,6-tetrahydropyridine moiety at Lys-4 were prepared along with related compounds possessing a shorter side chain at the fourth position. Enzymatic assays showed that PCPA peptides containing a longer side chain, which can react with FAD in the active site, are potent LSD1-selective inhibitors.
[Mh] Termos MeSH primário: Inibidores Enzimáticos/farmacologia
Histona Desmetilases/antagonistas & inibidores
Histonas/farmacologia
Lisina/antagonistas & inibidores
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Histona Desmetilases/metabolismo
Histonas/química
Seres Humanos
Lisina/metabolismo
Estrutura Molecular
Peptídeos/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Histones); 0 (Peptides); EC 1.14.11.- (Histone Demethylases); EC 1.5.- (KDM1A protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


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[PMID]:29274335
[Au] Autor:Khan S; Kowluru A
[Ad] Endereço:ß-Cell Biochemistry Laboratory, John D. Dingell VA Medical Center, and Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI, 48201, USA.
[Ti] Título:CD36 mediates lipid accumulation in pancreatic beta cells under the duress of glucolipotoxic conditions: Novel roles of lysine deacetylases.
[So] Source:Biochem Biophys Res Commun;495(3):2221-2226, 2018 01 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cluster of differentiation 36 (CD36) is implicated in the intake of long-chain fatty acids and fat storage in various cell types including the pancreatic beta cell, thus contributing to the pathogenesis of metabolic stress and diabetes. Recent evidence indicates that CD36 undergoes post-translational modifications such as acetylation-deacetylation. However, putative roles of such modifications in its functional activation and onset of beta cell dysregulation under the duress of glucolipotoxicity (GLT) remain largely unknown. Using pharmacological approaches, we validated, herein, the hypothesis that acetylation-deacetylation signaling steps are involved in CD36-mediated lipid accumulation and downstream apoptotic signaling in pancreatic beta (INS-1832/13) cells under GLT. Exposure of these cells to GLT resulted in significant lipid accumulation without affecting the CD36 expression. Sulfo-n-succinimidyl oleate (SSO), an irreversible inhibitor of CD36, significantly attenuated lipid accumulation under GLT conditions, thus implicating CD36 in this metabolic step. Furthermore, trichostatin A (TSA) or valproic acid (VPA), known inhibitors of lysine deacetylases, markedly suppressed GLT-associated lipid accumulation with no discernible effects on CD36 expression. Lastly, SSO or TSA prevented caspase 3 activation in INS-1832/13 cells exposed to GLT conditions. Based on these findings, we conclude that an acetylation-deacetylation signaling step might regulate CD36 functional activity and subsequent lipid accumulation and caspase 3 activation in pancreatic beta cells exposed to GLT conditions. Identification of specific lysine deacetylases that control CD36 function should provide novel clues for the prevention of beta-cell dysfunction under GLT.
[Mh] Termos MeSH primário: Diabetes Mellitus/metabolismo
Glucose/metabolismo
Histona Desacetilases/metabolismo
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/patologia
Lisina/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Linhagem Celular
Células Cultivadas
Seres Humanos
Metabolismo dos Lipídeos
Estresse Oxidativo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
EC 3.5.1.98 (Histone Deacetylases); IY9XDZ35W2 (Glucose); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


  10 / 30494 MEDLINE  
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[PMID]:29233695
[Au] Autor:Son HF; Kim KJ
[Ad] Endereço:School of Life Sciences, KNU Creative BioResearch Group, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea; KNU Institute for Microorganisms, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu, 41566, Republic of Korea.
[Ti] Título:Structural basis for substrate specificity of meso-diaminopimelic acid decarboxylase from Corynebacterium glutamicum.
[So] Source:Biochem Biophys Res Commun;495(2):1815-1821, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:l-lysine is an essential amino acid that is widely used as a food supplement for humans and animals. meso-Diaminopimelic acid decarboxylase (DAPDC) catalyzes the final step in the de novol-lysine biosynthetic pathway by converting meso-diaminopimelic acid (meso-DAP) into l-lysine by decarboxylation reaction. To elucidate its molecular mechanisms, we determined the crystal structure of DAPDC from Corynebacterium glutamicum (CgDAPDC). The PLP cofactor is bound at the center of the barrel domain and forms a Schiff base with the catalytic Lys75 residue. We also determined the CgDAPDC structure in complex with both pyridoxal 5'-phosphate (PLP) and the l-lysine product and revealed that the protein has an optimal substrate binding pocket to accommodate meso-DAP as a substrate. Structural comparison of CgDAPDC with other amino acid decarboxylases with different substrate specificities revealed that the position of the α15 helix in CgDAPDC and the residues located on the helix are crucial for determining the substrate specificities of the amino acid decarboxylases.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Carboxiliases/química
Carboxiliases/metabolismo
Corynebacterium glutamicum/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Carboxiliases/genética
Domínio Catalítico
Corynebacterium glutamicum/genética
Cristalografia por Raios X
Lisina/biossíntese
Modelos Moleculares
Mutagênese Sítio-Dirigida
Estrutura Quaternária de Proteína
Fosfato de Piridoxal/metabolismo
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 5V5IOJ8338 (Pyridoxal Phosphate); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.20 (diaminopimelic acid decarboxylase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE



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