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[PMID]: 29229390 [Au] Autor: Wang J; Chen CC; Yang Y; Liu W; Ko TP; Shang N; Hu X; Xie Y; Huang JW; Zhang Y; Guo RT [Ad] Endereço: Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China. [Ti] Título: Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis. [So] Source: Biochem Biophys Res Commun;495(2):1782-1788, 2018 01 08. [Is] ISSN: 1090-2104 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: FamD1 is a novel CloQ/NphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central ß-barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed. [Mh] Termos MeSH primário: Proteínas de Bactérias/química Proteínas de Bactérias/metabolismo Dimetilaliltranstransferase/química Dimetilaliltranstransferase/metabolismo Alcaloides de Indol/metabolismo [Mh] Termos MeSH secundário: Proteínas de Bactérias/genética Domínio Catalítico Cristalografia por Raios X Cianobactérias/enzimologia Cianobactérias/genética Dimetilaliltranstransferase/genética Alcaloides de Indol/química Modelos Moleculares Conformação Proteica Dobramento de Proteína Proteínas Recombinantes/química Proteínas Recombinantes/genética Proteínas Recombinantes/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Bacterial Proteins); 0 (Indole Alkaloids); 0 (Recombinant Proteins); EC 2.5.1.1 (Dimethylallyltranstransferase) [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: 171213 [St] Status: MEDLINE

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[PMID]: 28842490 [Au] Autor: Grabinska KA; Edani BH; Park EJ; Kraehling JR; Sessa WC [Ad] Endereço: From the Department of Pharmacology and Vascular Biology and Therapeutics Program, Yale University School of Medicine, New Haven, Connecticut 06520. [Ti] Título: A conserved C-terminal R G motif in the NgBR subunit of -prenyltransferase is critical for prenyltransferase activity. [So] Source: J Biol Chem;292(42):17351-17361, 2017 Oct 20. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: -Prenyltransferases ( -PTs) constitute a large family of enzymes conserved during evolution and present in all domains of life. In eukaryotes and archaea, -PT is the first enzyme committed to the synthesis of dolichyl phosphate, an obligate lipid carrier in protein glycosylation reactions. The homodimeric bacterial enzyme, undecaprenyl diphosphate synthase, generates 11 isoprene units and has been structurally and mechanistically characterized in great detail. Recently, we discovered that unlike undecaprenyl diphosphate synthase, mammalian -PT is a heteromer consisting of NgBR (Nus1) and hCIT (dehydrodolichol diphosphate synthase) subunits, and this composition has been confirmed in plants and fungal -PTs. Here, we establish the first purification system for heteromeric -PT and show that both NgBR and hCIT subunits function in catalysis and substrate binding. Finally, we identified a critical R G sequence in the C-terminal tail of NgBR that is conserved and essential for enzyme activity across phyla. In summary, our findings show that eukaryotic -PT is composed of the NgBR and hCIT subunits. The strong conservation of the R G motif among NgBR orthologs indicates that this subunit is critical for the synthesis of polyprenol diphosphates and cellular function. [Mh] Termos MeSH primário: Alquil e Aril Transferases/química Dimetilaliltranstransferase/química Receptores de Superfície Celular/química Transferases/química [Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética Alquil e Aril Transferases/metabolismo Motivos de Aminoácidos Proteínas de Bactérias/química Proteínas de Bactérias/genética Proteínas de Bactérias/metabolismo Dimetilaliltranstransferase/genética Dimetilaliltranstransferase/metabolismo Proteínas Fúngicas/química Proteínas Fúngicas/genética Proteínas Fúngicas/metabolismo Seres Humanos Proteínas de Plantas/química Proteínas de Plantas/genética Proteínas de Plantas/metabolismo Receptores de Superfície Celular/genética Receptores de Superfície Celular/metabolismo Transferases/genética Transferases/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Bacterial Proteins); 0 (Fungal Proteins); 0 (NUS1 protein, human); 0 (Plant Proteins); 0 (Receptors, Cell Surface); EC 2.- (Transferases); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (cis-prenyl transferase); EC 2.5.1.- (dehydrodolichyl diphosphate synthetase); EC 2.5.1.1 (Dimethylallyltranstransferase) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171103 [Lr] Data última revisão: 171103 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170827 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M117.806034

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[PMID]: 28841019 [Au] Autor: Christianson DW [Ad] Endereço: Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania , 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States. [Ti] Título: Structural and Chemical Biology of Terpenoid Cyclases. [So] Source: Chem Rev;117(17):11570-11648, 2017 Sep 13. [Is] ISSN: 1520-6890 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The year 2017 marks the twentieth anniversary of terpenoid cyclase structural biology: a trio of terpenoid cyclase structures reported together in 1997 were the first to set the foundation for understanding the enzymes largely responsible for the exquisite chemodiversity of more than 80000 terpenoid natural products. Terpenoid cyclases catalyze the most complex chemical reactions in biology, in that more than half of the substrate carbon atoms undergo changes in bonding and hybridization during a single enzyme-catalyzed cyclization reaction. The past two decades have witnessed structural, functional, and computational studies illuminating the modes of substrate activation that initiate the cyclization cascade, the management and manipulation of high-energy carbocation intermediates that propagate the cyclization cascade, and the chemical strategies that terminate the cyclization cascade. The role of the terpenoid cyclase as a template for catalysis is paramount to its function, and protein engineering can be used to reprogram the cyclization cascade to generate alternative and commercially important products. Here, I review key advances in terpenoid cyclase structural and chemical biology, focusing mainly on terpenoid cyclases and related prenyltransferases for which X-ray crystal structures have informed and advanced our understanding of enzyme structure and function. [Mh] Termos MeSH primário: Alquil e Aril Transferases/química Terpenos/metabolismo [Mh] Termos MeSH secundário: Alquil e Aril Transferases/metabolismo Carbono-Carbono Liases/química Carbono-Carbono Liases/metabolismo Cristalografia por Raios X Dimetilaliltranstransferase/química Dimetilaliltranstransferase/metabolismo Liases Intramoleculares/química Liases Intramoleculares/metabolismo Estrutura Terciária de Proteína Terpenos/química [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Nm] Nome de substância: 0 (Terpenes); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (terpene carbocyclase); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 4.1.- (Carbon-Carbon Lyases); EC 4.2.3.6 (trichodiene synthetase); EC 5.5.- (Intramolecular Lyases); EC 5.5.- (pinene cyclase I) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170926 [Lr] Data última revisão: 170926 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170826 [St] Status: MEDLINE [do] DOI: 10.1021/acs.chemrev.7b00287

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[PMID]: 28754323 [Au] Autor: Marshall SA; Payne KAP; Leys D [Ad] Endereço: Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. [Ti] Título: The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN). [So] Source: Arch Biochem Biophys;632:209-221, 2017 Oct 15. [Is] ISSN: 1096-0384 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree. [Mh] Termos MeSH primário: Carboxiliases Dimetilaliltranstransferase Proteínas de Escherichia coli Escherichia coli Flavinas Flavoproteínas Prenilação/fisiologia [Mh] Termos MeSH secundário: Carboxiliases/química Carboxiliases/genética Carboxiliases/metabolismo Dimetilaliltranstransferase/química Dimetilaliltranstransferase/genética Dimetilaliltranstransferase/metabolismo Escherichia coli/química Escherichia coli/genética Escherichia coli/metabolismo Proteínas de Escherichia coli/química Proteínas de Escherichia coli/genética Proteínas de Escherichia coli/metabolismo Flavinas/biossíntese Flavinas/química Flavinas/genética Flavoproteínas/química Flavoproteínas/genética Flavoproteínas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; REVIEW [Nm] Nome de substância: 0 (Escherichia coli Proteins); 0 (Flavins); 0 (Flavoproteins); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 4.1.1.- (3-octaprenyl-4-hydroxybenzoate carboxy-lyase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.- (ubiX protein, E coli) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171026 [Lr] Data última revisão: 171026 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170730 [St] Status: MEDLINE

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[PMID]: 28570807 [Au] Autor: Pan LL; Song LF; Miao Y; Yang Y; Merz KM [Ad] Endereço: Department of Chemistry and Department of Biochemistry and Molecular Biology, Michigan State University , 578 South Shaw Lane, East Lansing, Michigan 48824, United States. [Ti] Título: Mechanism of Formation of the Nonstandard Product in the Prenyltransferase Reaction of the G115T Mutant of FtmPT1: A Case of Reaction Dynamics Calling the Shots? [So] Source: Biochemistry;56(24):2995-3007, 2017 Jun 20. [Is] ISSN: 1520-4995 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: FtmPT1 is a fungal indole prenyltransferase that affords Tryprostatin B from Brevianamide F and dimethylallyl pyrophosphate; however, when a single residue in the active site is mutated (Gly115Thr), a novel five-membered ring compound is obtained as the major product with Tryprostatin B as the minor product. Herein, we describe detailed studies of the catalysis of the Gly115Thr mutant of FtmPT1 with a focus on the observed regioselectivity of the reaction. We employ one- and two-dimensional potential of mean force simulations to explore the catalytic mechanism, along with molecular dynamics simulations exploring the reaction dynamics of the prenyl transfer reaction. Single-point electronic structure calculations were also used to explore the performance of the self-consistent charge density functional tight-binding method to model specific reaction steps. Importantly, we observe that the two reaction pathways have comparable activation parameters and propose that the origin of the novel product is predicated, at least in part, on the topology of the potential energy surface as revealed by reaction dynamics studies. [Mh] Termos MeSH primário: Dimetilaliltranstransferase/genética Dimetilaliltranstransferase/metabolismo Glicina/genética Proteínas Mutantes/metabolismo Mutação Treonina/genética [Mh] Termos MeSH secundário: Dimetilaliltranstransferase/química Conformação Molecular Simulação de Dinâmica Molecular Proteínas Mutantes/química Proteínas Mutantes/genética Teoria Quântica [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Mutant Proteins); 2ZD004190S (Threonine); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 2.5.1.1 (FtmPT1 protein, Aspergillus fumigatus); TE7660XO1C (Glycine) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170926 [Lr] Data última revisão: 170926 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170602 [St] Status: MEDLINE [do] DOI: 10.1021/acs.biochem.7b00248

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[PMID]: 28355308 [Au] Autor: Araya-Cloutier C; Martens B; Schaftenaar G; Leipoldt F; Gruppen H; Vincken JP [Ad] Endereço: Laboratory of Food Chemistry, Wageningen University, Wageningen, The Netherlands. [Ti] Título: Structural basis for non-genuine phenolic acceptor substrate specificity of Streptomyces roseochromogenes prenyltransferase CloQ from the ABBA/PT-barrel superfamily. [So] Source: PLoS One;12(3):e0174665, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Acceptor substrate specificity of Streptomyces roseochromogenes prenyltransferase SrCloQ was investigated using different non-genuine phenolic compounds. RP-UHPLC-UV-MSn was used for the tentative annotation and quantification of the prenylated products. Flavonoids, isoflavonoids and stilbenoids with different types of substitution were prenylated by SrCloQ, although with less efficiency than the genuine substrate 4-hydroxyphenylpyruvate. The isoflavan equol, followed by the flavone 7,4'-dihydroxyflavone, were the best non-genuine acceptor substrates. B-ring C-prenylation was in general preferred over A-ring C-prenylation (ratio 5:1). Docking studies of non-genuine acceptor substrates with the B-ring oriented towards the donor substrate dimethylallyl pyrophosphate, showed that the carbonyl group of the C-ring was able to make stabilizing interactions with the residue Arg160, which might determine the preference observed for B-ring prenylation. No reaction products were formed when the acceptor substrate had no phenolic hydroxyl groups. This preference can be explained by the essential hydrogen bond needed between a phenolic hydroxyl group and the residue Glu281. Acceptor substrates with an additional hydroxyl group at the C3' position (B-ring), were mainly O3'-prenylated (> 80% of the reaction products). This can be explained by the proximity of the C3' hydroxyl group to the donor substrate at the catalytic site. Flavones were preferred over isoflavones by SrCloQ. Docking studies suggested that the orientation of the B-ring and of the phenolic hydroxyl group at position C7 (A-ring) of flavones towards the residue Tyr233 plays an important role in this observed preference. Finally, the insights obtained on acceptor substrate specificity and regioselectivity for SrCloQ were extended to other prenyltransferases from the CloQ/NhpB family. [Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo Dimetilaliltranstransferase/metabolismo Flavonoides/metabolismo Isoflavonas/metabolismo Streptomyces/enzimologia [Mh] Termos MeSH secundário: Proteínas de Bactérias/química Domínio Catalítico Dimetilaliltranstransferase/química Equol/química Equol/metabolismo Flavonoides/química Ligações de Hidrogênio Isoflavonas/química Cinética Simulação de Acoplamento Molecular Estrutura Molecular Novobiocina/análogos & derivados Novobiocina/biossíntese Novobiocina/química Fenóis/química Fenóis/metabolismo Ácidos Fenilpirúvicos/química Ácidos Fenilpirúvicos/metabolismo Prenilação Ligação Proteica Estrutura Terciária de Proteína Estilbenos/química Estilbenos/metabolismo Streptomyces/metabolismo Especificidade por Substrato [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Bacterial Proteins); 0 (Flavonoids); 0 (Isoflavones); 0 (Phenols); 0 (Phenylpyruvic Acids); 0 (Stilbenes); 156-39-8 (4-hydroxyphenylpyruvic acid); 17EC19951N (Novobiocin); 39868-96-7 (clorobiocin); 531-95-3 (Equol); EC 2.5.1.1 (Dimethylallyltranstransferase) [Em] Mês de entrada: 1709 [Cu] Atualização por classe: 170906 [Lr] Data última revisão: 170906 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170330 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0174665

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[PMID]: 28166207 [Au] Autor: Elshahawi SI; Cao H; Shaaban KA; Ponomareva LV; Subramanian T; Farman ML; Spielmann HP; Phillips GN; Thorson JS; Singh S [Ad] Endereço: Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, Kentucky, USA. [Ti] Título: Structure and specificity of a permissive bacterial C-prenyltransferase. [So] Source: Nat Chem Biol;13(4):366-368, 2017 Apr. [Is] ISSN: 1552-4469 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: This study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug. [Mh] Termos MeSH primário: Dimetilaliltranstransferase/química Dimetilaliltranstransferase/metabolismo Streptomyces/enzimologia [Mh] Termos MeSH secundário: Modelos Moleculares Estrutura Molecular Especificidade por Substrato [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: EC 2.5.1.1 (Dimethylallyltranstransferase) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170806 [Lr] Data última revisão: 170806 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170207 [St] Status: MEDLINE [do] DOI: 10.1038/nchembio.2285

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[PMID]: 28065269 [Au] Autor: Yang Y; Ke N; Liu S; Li W [Ad] Endereço: Washington University School of Medicine, St. Louis, MO, United States. [Ti] Título: Methods for Structural and Functional Analyses of Intramembrane Prenyltransferases in the UbiA Superfamily. [So] Source: Methods Enzymol;584:309-347, 2017. [Is] ISSN: 1557-7988 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The UbiA superfamily is a group of intramembrane prenyltransferases that generate lipophilic compounds essential in biological membranes. These compounds, which include various quinones, hemes, chlorophylls, and vitamin E, participate in electron transport and function as antioxidants, as well as acting as structural lipids of microbial cell walls and membranes. Prenyltransferases producing these compounds are involved in important physiological processes and human diseases. These UbiA superfamily members differ significantly in their enzymatic activities and substrate selectivities. This chapter describes examples of methods that can be used to group these intramembrane enzymes, analyze their activity, and screen and crystallize homolog proteins for structure determination. Recent structures of two archaeal homologs are compared with structures of soluble prenyltransferases to show distinct mechanisms used by the UbiA superfamily to control enzymatic activity in membranes. [Mh] Termos MeSH primário: Membrana Celular/enzimologia Dimetilaliltranstransferase/química Ensaios Enzimáticos/métodos Relação Estrutura-Atividade [Mh] Termos MeSH secundário: Dimetilaliltranstransferase/genética Dimetilaliltranstransferase/metabolismo Seres Humanos Conformação Proteica [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: EC 2.5.1.1 (Dimethylallyltranstransferase) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170818 [Lr] Data última revisão: 170818 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170110 [St] Status: MEDLINE

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[PMID]: 27992881 [Au] Autor: Chen R; Gao B; Liu X; Ruan F; Zhang Y; Lou J; Feng K; Wunsch C; Li SM; Dai J; Sun F [Ad] Endereço: State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China. [Ti] Título: Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase. [So] Source: Nat Chem Biol;13(2):226-234, 2017 Feb. [Is] ISSN: 1552-4469 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Aromatic prenyltransferases (aPTases) transfer prenyl moieties from isoprenoid donors to various aromatic acceptors, some of which have the rare property of extreme enzymatic promiscuity toward both a variety of prenyl donors and a large diversity of acceptors. In this study, we discovered a new aPTase, AtaPT, from Aspergillus terreus that exhibits unprecedented promiscuity toward diverse aromatic acceptors and prenyl donors and also yields products with a range of prenylation patterns. Systematic crystallographic studies revealed various discrete conformations for ligand binding with donor-dependent acceptor specificity and multiple binding sites within a spacious hydrophobic substrate-binding pocket. Further structure-guided mutagenesis of active sites at the substrate-binding pocket is responsible for altering the specificity and promiscuity toward substrates and the diversity of product prenylations. Our study reveals the molecular mechanism underlying the promiscuity of AtaPT and suggests an efficient protein engineering strategy to generate new prenylated derivatives in drug discovery applications. [Mh] Termos MeSH primário: Aspergillus/enzimologia Dimetilaliltranstransferase/química Dimetilaliltranstransferase/metabolismo [Mh] Termos MeSH secundário: Dimetilaliltranstransferase/antagonistas & inibidores Descoberta de Drogas Inibidores Enzimáticos/química Inibidores Enzimáticos/farmacologia Interações Hidrofóbicas e Hidrofílicas Ligantes Simulação de Dinâmica Molecular Estrutura Molecular Relação Estrutura-Atividade Especificidade por Substrato [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Enzyme Inhibitors); 0 (Ligands); EC 2.5.1.1 (Dimethylallyltranstransferase) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170509 [Lr] Data última revisão: 170509 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161220 [St] Status: MEDLINE [do] DOI: 10.1038/nchembio.2263

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[PMID]: 27833992 [Au] Autor: Zhao W; Fan A; Tarcz S; Zhou K; Yin WB; Liu XQ; Li SM [Ad] Endereço: College of Life Sciences, Capital Normal University, No.105 Xisanhuan Beilu, Beijing, 100048, China. [Ti] Título: Mutation on Gly115 and Tyr205 of the cyclic dipeptide C2-prenyltransferase FtmPT1 increases its catalytic activity toward hydroxynaphthalenes. [So] Source: Appl Microbiol Biotechnol;101(5):1989-1998, 2017 Mar. [Is] ISSN: 1432-0614 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: The fungal cyclic dipeptide prenyltransferase FtmPT1 from Aspergillus fumigatus catalyzes a regular C2-prenylation of brevianamide F (cyclo-L-Trp-L-Pro) and is involved in the biosynthesis of a number of biologically active natural products including tryprostatins, spirotryprostatins, verruculogen, and fumitremorgins. FtmPT1, like other members of the dimethylallyltryptophan synthase superfamily, was shown to have high substrate promiscuity for tryptophan-containing cyclic dipeptides and a few other aromatic substrates. A previous study demonstrated the acceptance of 1-naphthol by FtmPT1, but with very low product yield. In this study, we report the significantly increased acceptance of 1-naphthol and other hydroxynaphthalenes by FtmPT1_G115A and six FtmPT1_Y205X single mutants as well as FtmPT1_G115A_Y205C. These results provided an example for creation of biocatalysts with improved catalytic activity by site-directed mutagenesis. [Mh] Termos MeSH primário: Aspergillus fumigatus/enzimologia Aspergillus fumigatus/genética Dimetilaliltranstransferase/genética Dimetilaliltranstransferase/metabolismo Naftóis/metabolismo [Mh] Termos MeSH secundário: Biocatálise Alcaloides de Indol/metabolismo Mutagênese Sítio-Dirigida Mutação Prenilação [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Indole Alkaloids); 0 (Naphthols); 0 (brevianamide F); 2A71EAQ389 (1-naphthol); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 2.5.1.1 (FtmPT1 protein, Aspergillus fumigatus) [Em] Mês de entrada: 1702 [Cu] Atualização por classe: 170227 [Lr] Data última revisão: 170227 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161112 [St] Status: MEDLINE [do] DOI: 10.1007/s00253-016-7966-x

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2	and or and not		PalavrasDescritor de assuntoDescritor de assunto primárioLimitesAutorPalavras do títuloPalavras do resumoIdiomaPaís de publicaçãoNome de substânciaNome de pessoa como assuntoRevistaAssunto de RevistaISSNTipo de publicaçãoIdentificador únicoMês de entradaAno de publicaçãoTexto completoAtualização por classeCategoria DeCSCategoria DeCS explodidaCategoria CID-10SubSetsPais de AfiliaçãoAfiliaçãoAfiliação 2
3	and or and not		PalavrasDescritor de assuntoDescritor de assunto primárioLimitesAutorPalavras do títuloPalavras do resumoIdiomaPaís de publicaçãoNome de substânciaNome de pessoa como assuntoRevistaAssunto de RevistaISSNTipo de publicaçãoIdentificador únicoMês de entradaAno de publicaçãoTexto completoAtualização por classeCategoria DeCSCategoria DeCS explodidaCategoria CID-10SubSetsPais de AfiliaçãoAfiliaçãoAfiliação 2

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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde