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Pesquisa : D08.811.913.050.134.105 [Categoria DeCS]
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[PMID]:27771289
[Au] Autor:Dercksen M; Duran M; IJlst L; Kulik W; Ruiter JP; van Cruchten A; Tuchman M; Wanders RJ
[Ad] Endereço:Laboratory Genetic Metabolic Diseases, Departments of Pediatrics and Clinical Chemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands; Human Metabonomics, North-West University, Potchefstroom Campus, South Africa. Electronic address: marli.dercksen@nwu.ac.za.
[Ti] Título:A novel UPLC-MS/MS based method to determine the activity of N-acetylglutamate synthase in liver tissue.
[So] Source:Mol Genet Metab;119(4):307-310, 2016 12.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: N-acetylglutamate synthase (NAGS) plays a key role in the removal of ammonia via the urea cycle by catalyzing the synthesis of N-acetylglutamate (NAG), the obligatory cofactor in the carbamyl phosphate synthetase 1 reaction. Enzymatic analysis of NAGS in liver homogenates has remained insensitive and inaccurate, which prompted the development of a novel method. METHODS: UPLC-MS/MS was used in conjunction with stable isotope (N-acetylglutamic-2,3,3,4,4-d acid) dilution for the quantitative detection of NAG produced by the NAGS enzyme. The assay conditions were optimized using purified human NAGS and the optimized enzyme conditions were used to measure the activity in mouse liver homogenates. RESULTS: A low signal-to-noise ratio in liver tissue samples was observed due to non-enzymatic formation of N-acetylglutamate and low specific activity, which interfered with quantitative analysis. Quenching of acetyl-CoA immediately after the incubation circumvented this analytical difficulty and allowed accurate and sensitive determination of mammalian NAGS activity. The specificity of the assay was validated by demonstrating a complete deficiency of NAGS in liver homogenates from Nags -/- mice. CONCLUSION: The novel NAGS enzyme assay reported herein can be used for the diagnosis of inherited NAGS deficiency and may also be of value in the study of secondary hyperammonemia present in various inborn errors of metabolism as well as drug treatment.
[Mh] Termos MeSH primário: Aminoácido N-Acetiltransferase/genética
Carbamoil-Fosfato Sintase (Amônia)/genética
Hiperamonemia/diagnóstico
Distúrbios Congênitos do Ciclo da Ureia/diagnóstico
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Aminoácido N-Acetiltransferase/metabolismo
Animais
Carbamoil-Fosfato Sintase (Amônia)/deficiência
Seres Humanos
Hiperamonemia/genética
Hiperamonemia/metabolismo
Hiperamonemia/fisiopatologia
Fígado/enzimologia
Camundongos
Camundongos Knockout
Espectrometria de Massas em Tandem
Distúrbios Congênitos do Ciclo da Ureia/genética
Distúrbios Congênitos do Ciclo da Ureia/metabolismo
Distúrbios Congênitos do Ciclo da Ureia/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
72-89-9 (Acetyl Coenzyme A); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); EC 2.3.1.1 (NAGS protein, human); EC 6.3.4.16 (Carbamoyl-Phosphate Synthase (Ammonia))
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28369041
[Au] Autor:Jurenas D; Chatterjee S; Konijnenberg A; Sobott F; Droogmans L; Garcia-Pino A; Van Melderen L
[Ad] Endereço:Laboratoire de Génétique et Physiologie Bactérienne, Université Libre de Bruxelles, Gosselies, Belgium.
[Ti] Título:AtaT blocks translation initiation by N-acetylation of the initiator tRNA .
[So] Source:Nat Chem Biol;13(6):640-646, 2017 Jun.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Toxin-antitoxin (TA) loci are prevalent in bacterial genomes. They are suggested to play a central role in dormancy and persister states. Under normal growth conditions, TA toxins are neutralized by their cognate antitoxins, and under stress conditions, toxins are freed and inhibit essential cellular processes using a variety of mechanisms. Here we characterize ataR-ataT, a novel TA system, from enterohemorrhagic Escherichia coli. We show that the toxin AtaT is a GNAT family enzyme that transfers an acetyl group from acetyl coenzyme A to the amine group of the methionyl aminoacyl moiety of initiator tRNA. AtaT specifically modifies Met-tRNA , but no other aminoacyl-tRNAs, including the elongator Met-tRNA . We demonstrate that once acetylated, AcMet-tRNA fails to interact with initiation factor-2 (IF2), resulting in disruption of the translation initiation complex. This work reveals a new mechanism of translation inhibition and confirms Met-tRNA as a prime target to efficiently block cell growth.
[Mh] Termos MeSH primário: Aminoácido N-Acetiltransferase/metabolismo
Escherichia coli
Regulação da Expressão Gênica/genética
RNA de Transferência de Metionina/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Eletroforese em Gel Bidimensional
Modelos Biológicos
Biossíntese de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Transfer, Met); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2346


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[PMID]:28152637
[Au] Autor:Schrettl V; Felgenhauer N; Rabe C; Fernando M; Eyer F
[Ad] Endereço:a Department of Clinical Toxicology , Klinikum Rechts der Isar, Technical University of Munich (TUM) , Munich , Germany.
[Ti] Título:L-Arginine in the treatment of valproate overdose - five clinical cases.
[So] Source:Clin Toxicol (Phila);55(4):260-266, 2017 04.
[Is] ISSN:1556-9519
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Valproic acid and its metabolites - particularly valproyl-CoA - are inhibitors of the enzyme N-acetylglutamate synthetase. The amino acid l-arginine can stimulate N-acetylglutamate synthetase activity and could be potentially used therapeutically to correct hyperammonemia caused by valproate therapy or overdose. Severely valproic-acid-poisoned patients are usually treated with l-carnitine or hemodialysis in order to decrease hyperammonemia. We herein report of five cases, in which l-arginine was administered. METHODS: Observational study on five cases. Patients with hyperammonemia (i.e., ammonia 80 > µg/dL) and symptoms consistent with valproate overdose (i.e., drowsiness, coma) were selected for treatment with l-arginine. Data was collected retrospectively. RESULTS: l-Arginine decreased ammonia levels in a close temporal relation (case I ammonia in EDTA-plasma [µg/dL] decreased from 381 to 39; case II from 281 to 50; case III from 669 to 74; case IV from 447 to 56; case V from 202 to 60). In cases I and II, hemodialysis was performed and l-carnitine was given before the administration of l-arginine. In case III, hemodialysis was performed after the administration of l-arginine was already started. In cases IV and V, treatment with l-arginine was the sole measure to decrease ammonia levels in plasma. CONCLUSION: The results suggest that l-arginine may be beneficial in selected cases of valproate overdose complicated by hyperammonemia. l-Arginine could extend our conventional treatment options for valproic acid overdose.
[Mh] Termos MeSH primário: Arginina/uso terapêutico
Overdose de Drogas/tratamento farmacológico
Ácido Valproico/envenenamento
[Mh] Termos MeSH secundário: Acil Coenzima A/sangue
Acil Coenzima A/envenenamento
Adulto
Aminoácido N-Acetiltransferase/antagonistas & inibidores
Aminoácido N-Acetiltransferase/sangue
Amônia/sangue
Carnitina/uso terapêutico
Coma/induzido quimicamente
Coma/tratamento farmacológico
Overdose de Drogas/sangue
Feminino
Seres Humanos
Hiperamonemia/sangue
Hiperamonemia/tratamento farmacológico
Masculino
Diálise Renal
Ácido Valproico/sangue
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (valproyl-coenzyme A); 614OI1Z5WI (Valproic Acid); 7664-41-7 (Ammonia); 94ZLA3W45F (Arginine); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1080/15563650.2017.1284333


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[PMID]:28135072
[Au] Autor:Mori S; Nepal KK; Kelly GT; Sharma V; Simkhada D; Gowda V; Delgado D; Watanabe CM
[Ad] Endereço:Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
[Ti] Título:Priming of Azabicycle Biosynthesis in the Azinomycin Class of Antitumor Agents.
[So] Source:Biochemistry;56(6):805-808, 2017 Feb 14.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The biosynthesis of the azabicyclic ring system of the azinomycin family of antitumor agents represents the "crown jewel" of the pathway and is a complex process involving at least 14 enzymatic steps. This study reports on the first biosynthetic step, the inroads, in the construction of the novel aziridino [1,2-a]pyrrolidine, azabicyclic core, allowing us to support a new mechanism for azabicycle formation.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Aminoácido N-Acetiltransferase/metabolismo
Antineoplásicos Alquilantes/metabolismo
Compostos Azabicíclicos/metabolismo
Proteínas de Bactérias/metabolismo
Desenho de Drogas
Fosfotransferases (Aceptor do Grupo Carboxila)/metabolismo
Pirrolidinas/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Acetilação
Aldeído Oxirredutases/genética
Aminoácido N-Acetiltransferase/genética
Antibióticos Antineoplásicos/química
Antibióticos Antineoplásicos/metabolismo
Antibióticos Antineoplásicos/farmacologia
Antineoplásicos Alquilantes/química
Antineoplásicos Alquilantes/farmacologia
Compostos Azabicíclicos/química
Compostos Azabicíclicos/farmacologia
Proteínas de Bactérias/genética
Biocatálise
Dipeptídeos/química
Dipeptídeos/metabolismo
Dipeptídeos/farmacologia
Técnicas de Inativação de Genes
Ácido Glutâmico/metabolismo
Estrutura Molecular
Mutação
Naftalenos/química
Naftalenos/metabolismo
Naftalenos/farmacologia
Peptídeos/química
Peptídeos/metabolismo
Peptídeos/farmacologia
Fosfotransferases (Aceptor do Grupo Carboxila)/genética
Pirrolidinas/química
Pirrolidinas/farmacologia
Proteínas Recombinantes/metabolismo
Streptomyces/enzimologia
Streptomyces/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibiotics, Antineoplastic); 0 (Antineoplastic Agents, Alkylating); 0 (Azabicyclo Compounds); 0 (Bacterial Proteins); 0 (Dipeptides); 0 (Naphthalenes); 0 (Peptides); 0 (Pyrrolidines); 0 (Recombinant Proteins); 106486-76-4 (azinomycin B); 106486-77-5 (azinomycin A); 3KX376GY7L (Glutamic Acid); 72-89-9 (Acetyl Coenzyme A); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.38 (N-acetyl-gamma-glutamyl-phosphate reductase); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.8 (acetylglutamate kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01108


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[PMID]:26986217
[Au] Autor:Sang W; Yu L; He L; Ma WH; Zhu ZH; Zhu F; Wang XP; Lei CL
[Ad] Endereço:Hubei Insect Resources Utilization and Sustainable Pest Management Key Laboratory, Huazhong Agricultural University, Wuhan, China.
[Ti] Título:UVB Radiation Delays Tribolium castaneum Metamorphosis by Influencing Ecdysteroid Metabolism.
[So] Source:PLoS One;11(3):e0151831, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ultraviolet B (UVB) radiation is an important environmental factor. It is generally known that UVB exhibits high genotoxicity due to causing DNA damage, potentially leading to skin carcinogenesis and aging in mammals. However, little is known about the effects of UVB on the development and metamorphosis of insects, which are the most abundant terrestrial animals. In the present study, we performed dose-response analyses of the effects UVB irradiation on Tribolium castaneum metamorphosis, assessed the function of the T. castaneum prothoracicotropic hormone gene (Trcptth), and analyzed ecdysteroid pathway gene expression profile and ecdysterone titers post-UVB irradiation. The results showed that UVB not only caused death of T. castaneum larvae, but also delayed larval-pupal metamorphosis and reduced the size and emergence rate of pupae. In addition, we verified the function of Trcptth, which is responsible for regulating metamorphosis. It was also found that the expression profiles of Trcptth as well as ecdysteroidogenesis and response genes were influenced by UVB radiation. Therefore, a disturbance pulse of ecdysteroid may be involved in delaying development under exposure to irradiation. To our knowledge, this is the first report indicating that UVB can influence the metamorphosis of insects. This study will contribute to a better understanding of the impact of UVB on signaling mechanisms in insect metamorphosis.
[Mh] Termos MeSH primário: Ecdisteroides/fisiologia
Metamorfose Biológica/efeitos da radiação
Tribolium/efeitos da radiação
Raios Ultravioleta/efeitos adversos
[Mh] Termos MeSH secundário: Aminoácido N-Acetiltransferase
Animais
Sequência de Bases
Relação Dose-Resposta à Radiação
Ecdisteroides/metabolismo
Ecdisterona/análise
Ecdisterona/fisiologia
Regulação da Expressão Gênica/fisiologia
Regulação da Expressão Gênica/efeitos da radiação
Genes de Insetos/fisiologia
Genes de Insetos/efeitos da radiação
Larva/fisiologia
Larva/efeitos da radiação
Metamorfose Biológica/fisiologia
Filogenia
Pupa/fisiologia
Pupa/efeitos da radiação
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transcriptoma
Tribolium/genética
Tribolium/crescimento & desenvolvimento
Tribolium/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ecdysteroids); 5289-74-7 (Ecdysterone); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160318
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0151831


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[PMID]:26571592
[Au] Autor:Okanishi H; Kim K
[Ti] Título:[Functional discovery of functionally unknown proteins by mass spectrometry].
[So] Source:Seikagaku;87(3):286-91, 2015 Jun.
[Is] ISSN:0037-1017
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Aminoácido N-Acetiltransferase/análise
Espectrometria de Massas
Processamento de Proteína Pós-Traducional/fisiologia
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Espectrometria de Massas/métodos
Peso Molecular
Proteínas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Proteins); 317-66-8 (propionyl-coenzyme A); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151118
[St] Status:MEDLINE


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[PMID]:26461067
[Au] Autor:Gustafsson Sheppard N; Jarl L; Mahadessian D; Strittmatter L; Schmidt A; Madhusudan N; Tegnér J; Lundberg EK; Asplund A; Jain M; Nilsson R
[Ad] Endereço:Unit of Computational Medicine, Department of Medicine, Karolinska Institutet, Stockholm, Sweden.
[Ti] Título:The folate-coupled enzyme MTHFD2 is a nuclear protein and promotes cell proliferation.
[So] Source:Sci Rep;5:15029, 2015 Oct 13.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Folate metabolism is central to cell proliferation and a target of commonly used cancer chemotherapeutics. In particular, the mitochondrial folate-coupled metabolism is thought to be important for proliferating cancer cells. The enzyme MTHFD2 in this pathway is highly expressed in human tumors and broadly required for survival of cancer cells. Although the enzymatic activity of the MTHFD2 protein is well understood, little is known about its larger role in cancer cell biology. We here report that MTHFD2 is co-expressed with two distinct gene sets, representing amino acid metabolism and cell proliferation, respectively. Consistent with a role for MTHFD2 in cell proliferation, MTHFD2 expression was repressed in cells rendered quiescent by deprivation of growth signals (serum) and rapidly re-induced by serum stimulation. Overexpression of MTHFD2 alone was sufficient to promote cell proliferation independent of its dehydrogenase activity, even during growth restriction. In addition to its known mitochondrial localization, we found MTHFD2 to have a nuclear localization and co-localize with DNA replication sites. These findings suggest a previously unknown role for MTHFD2 in cancer cell proliferation, adding to its known function in mitochondrial folate metabolism.
[Mh] Termos MeSH primário: Aminoácido N-Acetiltransferase/metabolismo
Núcleo Celular/enzimologia
Ácido Fólico/metabolismo
Metilenotetra-Hidrofolato Desidrogenase (NADP)/metabolismo
Neoplasias Experimentais/enzimologia
Neoplasias Experimentais/patologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Proliferação Celular
Células HeLa
Seres Humanos
Camundongos
Mitocôndrias/metabolismo
Proteínas Nucleares/metabolismo
Ratos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Proteins); 935E97BOY8 (Folic Acid); EC 1.5.1.5 (Methylenetetrahydrofolate Dehydrogenase (NADP)); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151014
[St] Status:MEDLINE
[do] DOI:10.1038/srep15029


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[PMID]:26210075
[Au] Autor:Liu X; Liu S; Bode L; Liu C; Zhang L; Wang X; Li D; Lei Y; Peng X; Cheng Z; Xie P
[Ad] Endereço:Shanghai Key Laboratory of Forensic Medicine, Institute of Forensic Science, Ministry of Justice, Shanghai 200063, China.
[Ti] Título:Persistent human Borna disease virus infection modifies the acetylome of human oligodendroglia cells towards higher energy and transporter levels.
[So] Source:Virology;485:58-78, 2015 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Borna disease virus (BDV) is a neurotropic RNA virus persistently infecting mammalian hosts including humans. Lysine acetylation (Kac) is a key protein post-translational modification (PTM). The unexpectedly broad regulatory scope of Kac let us to profile the entire acetylome upon BDV infection. METHODS: The acetylome was profiled through stable isotope labeling for cell culture (SILAC)-based quantitative proteomics. The quantifiable proteome was annotated using bioinformatics. RESULTS: We identified and quantified 791 Kac sites in 473 Kac proteins in human BDV Hu-H1-infected and non-infected oligodendroglial (OL) cells. Bioinformatic analysis revealed that BDV infection alters the acetylation of metabolic proteins, membrane-associated proteins and transmembrane transporter activity, and affects the acetylation of several lysine acetyltransferases (KAT). CONCLUSIONS: Upon BDV persistence the OL acetylome is manipulated towards higher energy and transporter levels necessary for shuttling BDV proteins to and from nuclear replication sites.
[Mh] Termos MeSH primário: Aminoácido N-Acetiltransferase/metabolismo
Vírus da Doença de Borna/fisiologia
Proteínas de Transporte/metabolismo
Proteínas de Membrana/metabolismo
Oligodendroglia/metabolismo
Processamento de Proteína Pós-Traducional
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Sequência de Aminoácidos
Aminoácido N-Acetiltransferase/genética
Proteínas de Transporte/genética
Linhagem Celular
Biologia Computacional
Metabolismo Energético
Feto
Interações Hospedeiro-Patógeno
Seres Humanos
Marcação por Isótopo
Lisina/metabolismo
Proteínas de Membrana/genética
Anotação de Sequência Molecular
Dados de Sequência Molecular
Oligodendroglia/virologia
Mapeamento de Interação de Proteínas
Proteoma/genética
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Membrane Proteins); 0 (Proteome); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:151023
[Lr] Data última revisão:
151023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150727
[St] Status:MEDLINE


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[PMID]:26190825
[Au] Autor:Montgomery DC; Sorum AW; Guasch L; Nicklaus MC; Meier JL
[Ad] Endereço:Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick MD, 21702, USA.
[Ti] Título:Metabolic Regulation of Histone Acetyltransferases by Endogenous Acyl-CoA Cofactors.
[So] Source:Chem Biol;22(8):1030-1039, 2015 Aug 20.
[Is] ISSN:1879-1301
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The finding that chromatin modifications are sensitive to changes in cellular cofactor levels potentially links altered tumor cell metabolism and gene expression. However, the specific enzymes and metabolites that connect these two processes remain obscure. Characterizing these metabolic-epigenetic axes is critical to understanding how metabolism supports signaling in cancer, and developing therapeutic strategies to disrupt this process. Here, we describe a chemical approach to define the metabolic regulation of lysine acetyltransferase (KAT) enzymes. Using a novel chemoproteomic probe, we identify a previously unreported interaction between palmitoyl coenzyme A (palmitoyl-CoA) and KAT enzymes. Further analysis reveals that palmitoyl-CoA is a potent inhibitor of KAT activity and that fatty acyl-CoA precursors reduce cellular histone acetylation levels. These studies implicate fatty acyl-CoAs as endogenous regulators of histone acetylation, and suggest novel strategies for the investigation and metabolic modulation of epigenetic signaling.
[Mh] Termos MeSH primário: Acil Coenzima A/metabolismo
Aminoácido N-Acetiltransferase/metabolismo
Histona Acetiltransferases/metabolismo
Lisina/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Acil Coenzima A/biossíntese
Acil Coenzima A/química
Aminoácido N-Acetiltransferase/química
Células HEK293
Histona Acetiltransferases/química
Seres Humanos
Cinética
Lisina/química
Modelos Químicos
Palmitoil Coenzima A/química
Palmitoil Coenzima A/metabolismo
Proteômica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 1763-10-6 (Palmitoyl Coenzyme A); EC 2.3.1.1 (Amino-Acid N-Acetyltransferase); EC 2.3.1.48 (Histone Acetyltransferases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150721
[St] Status:MEDLINE
[do] DOI:10.1016/j.chembiol.2015.06.015


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[PMID]:26068232
[Au] Autor:Shi D; Allewell NM; Tuchman M
[Ad] Endereço:Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, the George Washington University, Washington, DC 20010, USA. dshi@childrensnational.org.
[Ti] Título:The N-Acetylglutamate Synthase Family: Structures, Function and Mechanisms.
[So] Source:Int J Mol Sci;16(6):13004-22, 2015 Jun 09.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:N-acetylglutamate synthase (NAGS) catalyzes the production of N-acetylglutamate (NAG) from acetyl-CoA and L-glutamate. In microorganisms and plants, the enzyme functions in the arginine biosynthetic pathway, while in mammals, its major role is to produce the essential co-factor of carbamoyl phosphate synthetase 1 (CPS1) in the urea cycle. Recent work has shown that several different genes encode enzymes that can catalyze NAG formation. A bifunctional enzyme was identified in certain bacteria, which catalyzes both NAGS and N-acetylglutamate kinase (NAGK) activities, the first two steps of the arginine biosynthetic pathway. Interestingly, these bifunctional enzymes have higher sequence similarity to vertebrate NAGS than those of the classical (mono-functional) bacterial NAGS. Solving the structures for both classical bacterial NAGS and bifunctional vertebrate-like NAGS/K has advanced our insight into the regulation and catalytic mechanisms of NAGS, and the evolutionary relationship between the two NAGS groups.
[Mh] Termos MeSH primário: Aminoácido N-Acetiltransferase/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoácido N-Acetiltransferase/metabolismo
Animais
Bactérias/enzimologia
Domínio Catalítico
Seres Humanos
Dados de Sequência Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
EC 2.3.1.1 (Amino-Acid N-Acetyltransferase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150613
[St] Status:MEDLINE
[do] DOI:10.3390/ijms160613004



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