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Pesquisa : D08.811.913.050.134.029 [Categoria DeCS]
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  1 / 19 MEDLINE  
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[PMID]:26535573
[Au] Autor:Mamidi AS; Arora P; Surolia A
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka, India.
[Ti] Título:Multivariate PLS Modeling of Apicomplexan FabD-Ligand Interaction Space for Mapping Target-Specific Chemical Space and Pharmacophore Fingerprints.
[So] Source:PLoS One;10(11):e0141674, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biomolecular recognition underlying drug-target interactions is determined by both binding affinity and specificity. Whilst, quantification of binding efficacy is possible, determining specificity remains a challenge, as it requires affinity data for multiple targets with the same ligand dataset. Thus, understanding the interaction space by mapping the target space to model its complementary chemical space through computational techniques are desirable. In this study, active site architecture of FabD drug target in two apicomplexan parasites viz. Plasmodium falciparum (PfFabD) and Toxoplasma gondii (TgFabD) is explored, followed by consensus docking calculations and identification of fifteen best hit compounds, most of which are found to be derivatives of natural products. Subsequently, machine learning techniques were applied on molecular descriptors of six FabD homologs and sixty ligands to induce distinct multivariate partial-least square models. The biological space of FabD mapped by the various chemical entities explain their interaction space in general. It also highlights the selective variations in FabD of apicomplexan parasites with that of the host. Furthermore, chemometric models revealed the principal chemical scaffolds in PfFabD and TgFabD as pyrrolidines and imidazoles, respectively, which render target specificity and improve binding affinity in combination with other functional descriptors conducive for the design and optimization of the leads.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Acetiltransferase
Antimaláricos/química
Inibidores Enzimáticos/química
Modelos Químicos
Plasmodium falciparum/enzimologia
Proteínas de Protozoários
Toxoplasma/enzimologia
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Acetiltransferase/antagonistas & inibidores
Proteína de Transporte de Acila S-Acetiltransferase/química
Sistemas de Liberação de Medicamentos
Proteínas de Protozoários/antagonistas & inibidores
Proteínas de Protozoários/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimalarials); 0 (Enzyme Inhibitors); 0 (Protozoan Proteins); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0141674


  2 / 19 MEDLINE  
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[PMID]:20954296
[Au] Autor:Kresge N; Simoni RD; Hill RL
[Ti] Título:Mercury detoxification and natural product synthesis: the work of Christopher T. Walsh.
[So] Source:J Biol Chem;285(42):e14-5, 2010 Oct 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Produtos Biológicos/biossíntese
Mercúrio/metabolismo
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Acetiltransferase/metabolismo
História do Século XX
História do Século XXI
Seres Humanos
Oxirredutases/isolamento & purificação
Pseudomonas aeruginosa/metabolismo
[Pt] Tipo de publicação:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE; PORTRAITS
[Ps] Nome de pessoa como assunto:Walsh CT
[Nm] Nome de substância:
0 (Biological Products); EC 1.- (Oxidoreductases); EC 1.16.- (mercuric reductase); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); FXS1BY2PGL (Mercury)
[Em] Mês de entrada:1012
[Cu] Atualização por classe:141202
[Lr] Data última revisão:
141202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101019
[St] Status:MEDLINE


  3 / 19 MEDLINE  
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[PMID]:17071746
[Au] Autor:Crawford JM; Dancy BC; Hill EA; Udwary DW; Townsend CA
[Ad] Endereço:Department of Chemistry, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
[Ti] Título:Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase.
[So] Source:Proc Natl Acad Sci U S A;103(45):16728-33, 2006 Nov 07.
[Is] ISSN:0027-8424
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Polyketides are a class of natural products that exhibit a wide range of functional and structural diversity. They include antibiotics, immunosuppressants, antifungals, antihypercholesterolemics, and cytotoxins. Polyketide synthases (PKSs) use chemistry similar to fatty acid synthases (FASs), although building block variation and differing extents of reduction of the growing polyketide chain underlie their biosynthetic versatility. In contrast to the well studied sequential modular type I PKSs, less is known about how the iterative type I PKSs carry out and control chain initiation, elongation, folding, and cyclization during polyketide processing. Domain structure analysis of a group of related fungal, nonreducing PKSs has revealed well defined N-terminal domains longer than commonly seen for FASs and modular PKSs. Predicted structure of this domain disclosed a region similar to malonyl-CoA:acyl-carrier protein (ACP) transacylases (MATs). MATs play a key role transferring precursor CoA thioesters from solution onto FASs and PKSs for chain elongation. On the basis of site-directed mutagenesis, radiolabeling, and kinetics experiments carried out with individual domains of the norsolorinic acid PKS, we propose that the N-terminal domain is a starter unit:ACP transacylase (SAT domain) that selects a C(6) fatty acid from a dedicated yeast-like FAS and transfers this unit onto the PKS ACP, leading to the production of the aflatoxin precursor, norsolorinic acid. These findings could indicate a much broader role for SAT domains in starter unit selection among nonreducing iterative, fungal PKSs, and they provide a biochemical rationale for the classical acetyl "starter unit effect."
[Mh] Termos MeSH primário: Proteína de Transporte de Acila S-Acetiltransferase/química
Policetídeo Sintases/química
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Acetiltransferase/genética
Proteína de Transporte de Acila S-Acetiltransferase/metabolismo
Aflatoxinas/biossíntese
Aflatoxinas/química
Sequência de Aminoácidos
Aspergillus/enzimologia
Aspergillus/genética
Sequência de Bases
Clonagem Molecular
DNA Fúngico/genética
Genes Fúngicos
Dados de Sequência Molecular
Estrutura Molecular
Mutagênese Sítio-Dirigida
Policetídeo Sintases/genética
Policetídeo Sintases/metabolismo
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Aflatoxins); 0 (DNA, Fungal); 0 (Recombinant Proteins); 79956-01-7 (Polyketide Synthases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase)
[Em] Mês de entrada:0612
[Cu] Atualização por classe:170219
[Lr] Data última revisão:
170219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061031
[St] Status:MEDLINE


  4 / 19 MEDLINE  
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[PMID]:11779582
[Au] Autor:Ichinowatari G; Yamada M; Yaginuma H; Tsuyuki K; Tanimoto A; Ohuchi K
[Ad] Endereço:Laboratory of Pathophysiological Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
[Ti] Título:Participation of prostaglandin E2 and platelet-activating factor in thapsigargin-induced production of interleukin-6.
[So] Source:Eur J Pharmacol;434(3):187-96, 2002 Jan 11.
[Is] ISSN:0014-2999
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Incubation of rat peritoneal macrophages in the presence of thapsigargin increased production of prostaglandin E2, intracellular platelet-activating factor (PAF) and interleukin-6. However, no PAF was detected in the conditioned medium. In the presence of SK&F 98625 (diethyl 7-(3,4,5-triphenyl-2-oxo-2,3-dihydroimidazol-1-yl)heptane phosphonate), a CoA-independent transacylase inhibitor, the thapsigargin-induced increases in the interleukin-6 mRNA level and interleukin-6 production were suppressed in a concentration-dependent manner. This inhibitor also suppressed the production of prostaglandin E2 and intracellular PAF. The PAF receptor antagonists such as E6123 ((S)-(+)-6-(2-chlorophenyl)-3-cyclopropanecarbonyl-8,11-dimethyl-2,3,4,5-tetrahydro-8H-pyrido[4',3':4,5]thieno[3,2-f][1,2,4]triazolo [4,3-a][1,4]diazepine) and L-652,731 (2,5-bis(3,4,5-trimethylphenyl)tetrahydrofuran) partially inhibited the thapsigargin-induced increase in the levels of interleukin-6 mRNA and interleukin-6 protein. The SK&F 98625-induced suppression of interleukin-6 mRNA accumulation and interleukin-6 production was partially restored by addition of exogenous prostaglandin E2. However, exogenous PAF failed to reverse the suppression suggesting that the intracellular PAF does not act in an autocrine mechanism. These findings suggested that the concurrently produced prostaglandin E2 and intracellular PAF participate in the thapsigargin-induced increase in the interleukin-6 mRNA level and interleukin-6 production by rat peritoneal macrophages.
[Mh] Termos MeSH primário: Dinoprostona/fisiologia
Interleucina-6/biossíntese
Fator de Ativação de Plaquetas/fisiologia
Receptores de Superfície Celular
Receptores Acoplados a Proteínas-G
Tapsigargina/farmacologia
[Mh] Termos MeSH secundário: Acetiltransferases/antagonistas & inibidores
Proteína de Transporte de Acila S-Acetiltransferase
Animais
Azepinas/farmacologia
Células Cultivadas
Dinoprostona/antagonistas & inibidores
Relação Dose-Resposta a Droga
Sinergismo Farmacológico
Inibidores Enzimáticos/farmacologia
Furanos/farmacologia
Imidazóis/farmacologia
Indometacina/farmacologia
Interleucina-6/antagonistas & inibidores
Interleucina-6/genética
Macrófagos Peritoneais/efeitos dos fármacos
Macrófagos Peritoneais/metabolismo
Masculino
Compostos Organofosforados/farmacologia
Fator de Ativação de Plaquetas/antagonistas & inibidores
Fator de Ativação de Plaquetas/biossíntese
Fator de Ativação de Plaquetas/farmacologia
Glicoproteínas da Membrana de Plaquetas/antagonistas & inibidores
Glicoproteínas da Membrana de Plaquetas/fisiologia
RNA Mensageiro/antagonistas & inibidores
RNA Mensageiro/biossíntese
Ratos
Ratos Sprague-Dawley
Tapsigargina/antagonistas & inibidores
Triazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Azepines); 0 (Enzyme Inhibitors); 0 (Furans); 0 (Imidazoles); 0 (Interleukin-6); 0 (Organophosphorus Compounds); 0 (Platelet Activating Factor); 0 (Platelet Membrane Glycoproteins); 0 (RNA, Messenger); 0 (Receptors, Cell Surface); 0 (Receptors, G-Protein-Coupled); 0 (SK&F 98625); 0 (Triazoles); 0 (platelet activating factor receptor); 131614-02-3 (E 6123); 67526-95-8 (Thapsigargin); 99103-35-2 (2,5-bis(3,4,5-trimethoxyphenyl)tetrahydrofuran); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); K7Q1JQR04M (Dinoprostone); XXE1CET956 (Indomethacin)
[Em] Mês de entrada:0204
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020110
[St] Status:MEDLINE


  5 / 19 MEDLINE  
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[PMID]:11570897
[Au] Autor:Lobo S; Florova G; Reynolds KA
[Ad] Endereço:Department of Medicinal Chemistry and Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, Virginia 23219, USA.
[Ti] Título:A Streptomyces collinus thiolase with novel acetyl-CoA:acyl carrier protein transacylase activity.
[So] Source:Biochemistry;40(39):11955-64, 2001 Oct 02.
[Is] ISSN:0006-2960
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acetyl-CoA:acyl carrier protein (ACP) transacylase (ACT) activity has been demonstrated for the 3-ketoacyl-ACP synthase III (KASIII) which initiates fatty acid biosynthesis in the type II dissociable fatty acid synthases of plants and bacteria. Several lines of evidence have indicated the possibility of ACT activity being associated with proteins other than KASIII. Using a crude extract of Streptomyces collinus, we have resolved from KASIII an additional protein with ACT activity and subsequently purified it 85-fold in five chromatographic steps. The 45 kDa protein was shown by gel filtration to have a molecular mass of 185 +/- 35 kDa, consistent with a homotetrameric structure for the native enzyme. The corresponding gene (fadA) was cloned and sequenced and shown to encode a protein with amino acid sequence homology to type II thiolases. The fadA was expressed in Escherichia coli, and the resulting recombinant FadA enzyme purified by metal chelate chromatography was shown to have both ACT and thiolase activities. Kinetic studies revealed that in an ACT assay FadA had a substrate specificity for a two-carbon acetyl-CoA substrate (K(m) 8.7 +/- 1.4 microM) but was able to use ACPs from both type II fatty acid and polyketide synthases (Streptomyces glaucescens FabC ACP, K(m) 10.7 +/- 1.4 microM; E. coli FabC ACP, K(m) 8.8 +/- 2 microM; FrenN ACP, K(m) 44 +/- 12 microM). In the thiolase assay kinetic analyses revealed similar K(m) values for binding of substrates acetoacetyl-CoA (K(m) 9.8 +/- 0.8 microM) and CoA (K(m) 10.9 +/- 1.8 microM). A Cys92Ser mutant of FadA possessed virtually unchanged K(m) values for acetoacetyl-CoA and CoA but had a greater than 99% decrease in k(cat) for the thiolase activity. No detectable ACT activity was observed for the Cys92Ser mutant, demonstrating that both activities are associated with FadA and likely involve formation of the same covalent acetyl-S-Cys enzyme intermediate. An ACT activity with ACP has not previously been observed for thiolases and in the case of the S. collinus FadA is significantly lower (k(cat) 3 min(-1)) than the thiolase activity of FadA (k(cat) 2170 min(-1)). The ACT activity of FadA is comparable to the KAS activity and significantly higher than the ACT activity, reported for a streptomycete KASIII.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/metabolismo
Acetiltransferases/metabolismo
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Acetiltransferases/química
Acetiltransferases/genética
Acetiltransferases/isolamento & purificação
Proteína de Transporte de Acila S-Acetiltransferase
Sequência de Aminoácidos
Sequência de Bases
Cromatografia em Gel
Clonagem Molecular
Primers do DNA
Eletroforese em Gel de Poliacrilamida
Inibidores Enzimáticos/farmacologia
Escherichia coli/genética
Seres Humanos
Cinética
Dados de Sequência Molecular
Peso Molecular
Fases de Leitura Aberta
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Tiofenos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (DNA Primers); 0 (Enzyme Inhibitors); 0 (Recombinant Proteins); 0 (Thiophenes); 82079-32-1 (thiolactomycin); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:0110
[Cu] Atualização por classe:071114
[Lr] Data última revisão:
071114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:010926
[St] Status:MEDLINE


  6 / 19 MEDLINE  
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[PMID]:9463491
[Au] Autor:Winkler JD; Sung CM; Chabot-Flecher M; Griswold DE; Marshall LA; Chilton FH; Bondinell W; Mayer RJ
[Ad] Endereço:Department of Immunopharmacology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406, USA. james_d_winkler@sbphrd.com
[Ti] Título:Beta-lactams SB 212047 and SB 216754 are irreversible, time-dependent inhibitors of coenzyme A-independent transacylase.
[So] Source:Mol Pharmacol;53(2):322-9, 1998 Feb.
[Is] ISSN:0026-895X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The enzyme coenzyme A-independent transacylase (CoA-IT) has been demonstrated to be the key mediator of arachidonate remodeling, a process that moves arachidonate into 1-ether-containing phospholipids. Blockade of CoA-IT by reversible inhibitors has been shown to block the release of arachidonate in stimulated neutrophils and inhibit the production of eicosanoids and platelet-activating factor. We describe novel inhibitors of CoA-IT activity that contain a beta-lactam nucleus. beta-Lactams were investigated as potential mechanism-based inhibitors of CoA-IT on the basis of the expected formation of an acyl-enzyme intermediate complex. Two beta-lactams, SB 212047 and SB 216754, were shown to be specific, time-dependent inhibitors of CoA-IT activity (IC50 = 6 and 20 microM, respectively, with a 10-min pretreatment time). Extensive washing and dilution could not remove the inhibition, suggesting it was irreversible. In stimulated human monocytes, SB 216754 decreased the production of eicosanoids in a time-dependent manner. In an in vivo model of phorbol ester-induced ear inflammation, SB 216754 was able to inhibit indices of both edema and cell infiltration. Taken together, the results support two hypotheses: 1) CoA-IT activity is important for the production of inflammatory lipid mediators in stimulated cells and in vivo and 2) the mechanism by which CoA-IT acts to transfer arachidonate is through an acyl-enzyme intermediate.
[Mh] Termos MeSH primário: Acetiltransferases/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Lactamas
beta-Lactamas/farmacologia
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila S-Acetiltransferase
Animais
Anti-Inflamatórios/farmacologia
Linhagem Celular
Eicosanoides/metabolismo
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Microssomos/enzimologia
Neutrófilos/enzimologia
Fator de Ativação de Plaquetas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Eicosanoids); 0 (Enzyme Inhibitors); 0 (Lactams); 0 (Platelet Activating Factor); 0 (SB-212047); 0 (SB-216754); 0 (beta-Lactams); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase)
[Em] Mês de entrada:9803
[Cu] Atualização por classe:071114
[Lr] Data última revisão:
071114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:980314
[St] Status:MEDLINE


  7 / 19 MEDLINE  
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[PMID]:9422335
[Au] Autor:Shamsuddin M; Chen E; Anderson J; Smith LJ
[Ad] Endereço:Pulmonary Division, Northwestern University Medical School, Veterans Affairs Lakeside Medical Center, Chicago, IL 60611-3053, USA.
[Ti] Título:Regulation of leukotriene and platelet-activating factor synthesis in human alveolar macrophages.
[So] Source:J Lab Clin Med;130(6):615-26, 1997 Dec.
[Is] ISSN:0022-2143
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been suggested that phospholipase A2 (PLA2) contributes to the regulation of leukotriene (LT) and platelet-activating factor (PAF) synthesis by controlling the release of their precursors, arachidonic acid (AA) and lysophosphatidylcholine (lysoPC), from membrane phospholipids. In rat alveolar macrophages (AMs), PLA2 appears to have a major role in LT synthesis but a more limited role in PAF synthesis. The present study was designed to define the role of PLA2 in LT and PAF synthesis in human AMs and determine whether differences exist between AMs obtained from normal subjects and those from patients with asthma. In the normal subjects, the calcium ionophore A23187 (Cal) increased AM PAF synthesis (percent incorporation of tritiated acetate) by 135% (p < 0.01) and LTB4 synthesis 88-fold (p < 0.001). Phorbol myristate acetate (PMA) had little effect alone, but it had a synergistic effect with Cal, increasing PAF synthesis by 466% and LTB4 synthesis to 229-fold above the control values (p < 0.001 for both). Ro 25-4331, a combined cytosolic (c) and secretory (s) PLA2 inhibitor, had little effect on the Cal-stimulated PAF synthesis, but it completely blocked the effect of PMA. It also blocked the Cal- and Cal+PMA-stimulated LTB4 synthesis. AACOCF3, a cPLA2 inhibitor, had no effect on either Cal or Cal+PMA-stimulated PAF synthesis. It reduced LTB4 synthesis, but it did so less effectively than Ro 25-4331. CoA-independent transacylase (CoAI-TA) activity in the AMs increased after stimulation and exposure to Ro 25-4331. SK&F 45905, a CoAI-TA inhibitor, reduced stimulated PAF synthesis by 30% to 40%. Patients with asthma had similar results except that cPLA2 had a greater role in stimulated LTB4 synthesis. These data indicate that PLA2 plays a direct role in human AM LT synthesis; both the cytosolic and secretory forms contribute to LT synthesis; PLA2 appears to have a more limited role in PAF synthesis, although it mediates the synergistic effect of PMA, probably via sPLA2; and CoAI-TA contributes to PAF synthesis during PLA2 inhibition. With the exception of the greater role for cPLA2 in stimulated LTB4 synthesis in the patients with asthma, the contributions of PLA2 and CoAI-TA to AM LT and PAF synthesis appear to be similar in normal subjects and patients with asthma.
[Mh] Termos MeSH primário: Leucotrienos/biossíntese
Macrófagos Alveolares/metabolismo
Fator de Ativação de Plaquetas/biossíntese
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Proteína de Transporte de Acila S-Acetiltransferase
Ácidos Araquidônicos/farmacologia
Asma/metabolismo
Benzenossulfonatos/farmacologia
Líquido da Lavagem Broncoalveolar
Calcimicina/farmacologia
Cálcio/fisiologia
Células Cultivadas
Citosol/enzimologia
Inibidores Enzimáticos/farmacologia
Seres Humanos
Ionóforos/farmacologia
Leucotrieno B4/biossíntese
Fosfolipases A/antagonistas & inibidores
Fosfolipases A/metabolismo
Fosfolipases A2
Acetato de Tetradecanoilforbol/farmacologia
Ureia/análogos & derivados
Ureia/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (2-(2-(3-(4-chloro-3-(trifluoromethyl)phenyl)ureido)-4-(trifluoromethyl)phenoxy)-4,5-dichlorobenzenesulfonic acid); 0 (Arachidonic Acids); 0 (Benzenesulfonates); 0 (Enzyme Inhibitors); 0 (Ionophores); 0 (Leukotrienes); 0 (Platelet Activating Factor); 00XIW1CR0F (arachidonyltrifluoromethane); 1HGW4DR56D (Leukotriene B4); 37H9VM9WZL (Calcimycin); 8W8T17847W (Urea); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); EC 3.1.1.32 (Phospholipases A); EC 3.1.1.4 (Phospholipases A2); NI40JAQ945 (Tetradecanoylphorbol Acetate); SY7Q814VUP (Calcium)
[Em] Mês de entrada:9801
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:980109
[St] Status:MEDLINE


  8 / 19 MEDLINE  
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[PMID]:8018868
[Au] Autor:Gulliver BS; Slabas AR
[Ad] Endereço:Department of Biological Sciences, University of Durham, UK.
[Ti] Título:Acetoacyl-acyl carrier protein synthase from avocado: its purification, characterisation and clear resolution from acetyl CoA:ACP transacylase.
[So] Source:Plant Mol Biol;25(2):179-91, 1994 May.
[Is] ISSN:0167-4412
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:beta-ketoacyl-ACP synthetase III (KAS III) has been purified from avocado using a six-step purification procedure. The enzyme, which is cerulenin-insensitive and thiolactomycin-sensitive, was assayed using a partial component reaction: acetyl CoA:ACP transacylase (ACAT) activity. KAS III activity is distinguished from ACAT activity on the basis that the former is highly stimulated by the addition of malonyl CoA in the presence of malonyl-CoA:ACP transacylase, and the latter is not. KAS III and ACAT activity have been separated from each other thus providing the first evidence that these two discrete activities exist in higher plants. Both of these enzymes have been implicated in the initial reactions of fatty acid synthesis. KAS III was purified 134-fold using a combination of PEG precipitation, Fast Q, ammonium sulphate precipitation, Phenyl Sepharose and ACP-affinity chromatography. The enzyme requires Triton X-100 for solubility and is highly salt sensitive. The subunit molecular mass of 37 kDa has been identified by SDS-PAGE. The results of gel filtration analysis are consistent with the native enzyme being homodimeric. The native molecular mass of KAS III is 69 kDa and that of ACAT 18.5 kDa. The enzyme has a pH optimum of 7.0-7.5, which is similar to the pH optimum of the ACAT reaction. The Km for acetyl CoA is 12.5 microM and the Km for malonyl-ACP is 14 microM. Both KAS III and ACAT are sensitive to thiolactomycin inhibition. The results are discussed with respect to the potential role of acetyl CoA:ACP transacylase in plants.
[Mh] Termos MeSH primário: 3-Oxoacil-(Proteína de Transporte de Acila) Sintase/isolamento & purificação
Acetiltransferases/isolamento & purificação
Frutas/enzimologia
[Mh] Termos MeSH secundário: 3-Oxoacil-(Proteína de Transporte de Acila) Sintase/química
3-Oxoacil-(Proteína de Transporte de Acila) Sintase/metabolismo
Acetilcoenzima A/metabolismo
Acetiltransferases/química
Acetiltransferases/metabolismo
Proteína de Transporte de Acila S-Acetiltransferase
Tampões (Química)
Cerulenina/farmacologia
Concentração de Íons de Hidrogênio
Cinética
Malonil Coenzima A/metabolismo
Peso Molecular
Tiofenos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Buffers); 0 (Thiophenes); 17397-89-6 (Cerulenin); 524-14-1 (Malonyl Coenzyme A); 72-89-9 (Acetyl Coenzyme A); 82079-32-1 (thiolactomycin); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.180 (3-ketoacyl-acyl carrier protein synthase III); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); EC 2.3.1.41 (3-Oxoacyl-(Acyl-Carrier-Protein) Synthase)
[Em] Mês de entrada:9408
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:940501
[St] Status:MEDLINE


  9 / 19 MEDLINE  
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[PMID]:8399328
[Au] Autor:Worsham LM; Williams SG; Ernst-Fonberg ML
[Ad] Endereço:Department of Biochemistry, James H. Quillen College of Medicine, East Tennessee State University, Johnson City 37614-0581.
[Ti] Título:Early catalytic steps of Euglena gracilis chloroplast type II fatty acid synthase.
[So] Source:Biochim Biophys Acta;1170(1):62-71, 1993 Sep 29.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Euglena gracilis is a very ancient eukaryote whose chloroplast acquisition and evolution has been independent of higher plants. The organism in unique in possessing two de novo fatty acid synthases, a true multienzyme complex of great size in the cytosol and a plastid-localized type II fatty acid synthase composed of discrete enzymes and acyl carrier protein (ACP). The enzymology of the early steps of fatty acid biosynthesis differed in the Euglena type II fatty acid synthase compared to those of Escherichia coli and plants. The enzymes of Euglena participating in both priming and elongation reactions to form a new carbon-carbon bond were acetyl-CoA-ACP transacylase, malonyl-CoA-ACP transacylase, and beta-ketoacyl-ACP synthase I. The effects of inhibitors on the three different enzymes were noted. All carbon-carbon bond formation was inhibited by cerulenin. Although neither fatty acid biosynthesis nor any of the isolated enzymes were sensitive to diisopropylphosphofluoridate, the three Euglena enzymes studied were sensitive to different sulfhydryl-alkylating agents. Acetyl-ACP supported fatty acid biosynthesis as effectively as did comparable amounts of ACPSH and acetyl-CoA. There was no evidence for a beta-ketoacyl-ACP synthase III for priming such as has been reported in type II fatty acid synthase of higher plants and bacteria. The roles of the acetyl-CoA-ACP transacylase and beta-ketoacyl-ACP synthase I appear to be unique in the type II fatty acid synthase of Euglena. Acetyl-CoA-ACP transacylase, malonyl-CoA-ACP transacylase, and beta-ketoacyl-ACP synthase I were separated from one another and shown to have different molecular weights.
[Mh] Termos MeSH primário: Euglena gracilis/enzimologia
Ácido Graxo Sintases/metabolismo
[Mh] Termos MeSH secundário: 3-Oxoacil-(Proteína de Transporte de Acila) Sintase/metabolismo
Acetiltransferases/metabolismo
Proteína de Transporte de Acila S-Acetiltransferase
Proteína de Transporte de Acila S-Maloniltransferase
Aciltransferases/metabolismo
Animais
Ácido Graxo Sintases/antagonistas & inibidores
Ácidos Graxos/biossíntese
Isoenzimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Isoenzymes); EC 2.3.- (Acyltransferases); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (beta-ketoacyl-acyl carrier protein synthase I); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase); EC 2.3.1.39 (Acyl-Carrier Protein S-Malonyltransferase); EC 2.3.1.41 (3-Oxoacyl-(Acyl-Carrier-Protein) Synthase); EC 2.3.1.85 (Fatty Acid Synthases)
[Em] Mês de entrada:9311
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:930929
[St] Status:MEDLINE


  10 / 19 MEDLINE  
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[PMID]:1621095
[Au] Autor:Voelker TA; Worrell AC; Anderson L; Bleibaum J; Fan C; Hawkins DJ; Radke SE; Davies HM
[Ad] Endereço:Calgene, Inc., Davis, CA 95616.
[Ti] Título:Fatty acid biosynthesis redirected to medium chains in transgenic oilseed plants.
[So] Source:Science;257(5066):72-4, 1992 Jul 03.
[Is] ISSN:0036-8075
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Medium-chain fatty acids (FAs), found in storage lipids of certain plants, are an important renewable resource. Seeds of undomesticated California bay accumulate laurate (12:0), and a 12:0-acyl-carrier protein thioesterase (BTE) has been purified from this tissue. Sequencing of BTE enabled the cloning of a complementary DNA coding for a plastid-targeted preprotein. Expression of the complementary DNA in the seeds of Arabidopsis thaliana resulted in BTE activity, and medium chains accumulated at the expense of long-chain (greater than or equal to 16) FAs. Laurate became the most abundant FA species and was deposited in the storage triacylglycerols. These results demonstrate a mechanism for medium-chain FA synthesis in plants.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Ácidos Graxos/biossíntese
Ácidos Láuricos/metabolismo
Plantas/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Proteína de Transporte de Acila S-Acetiltransferase
Sequência de Aminoácidos
DNA/genética
Ácidos Graxos/isolamento & purificação
Engenharia Genética
Dados de Sequência Molecular
Plantas/genética
Plantas Geneticamente Modificadas
Plasmídeos
Sementes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Lauric Acids); 1160N9NU9U (lauric acid); 9007-49-2 (DNA); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.38 (Acyl-Carrier Protein S-Acetyltransferase)
[Em] Mês de entrada:9208
[Cu] Atualização por classe:121115
[Lr] Data última revisão:
121115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:920703
[St] Status:MEDLINE



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