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[PMID]: 29193264 [Au] Autor: Kausar S; Abbas MN; Qian C; Zhu B; Gao J; Sun Y; Wang L; Wei G; Liu C [Ad] Endereço: College of Life Sciences, Anhui Agricultural University, Hefei, China. [Ti] Título: Role of Antheraea pernyi serpin 12 in prophenoloxidase activation and immune responses. [So] Source: Arch Insect Biochem Physiol;97(2), 2018 Feb. [Is] ISSN: 1520-6327 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Serine protease inhibitors play a key role in the immune system of invertebrates by controlling proteolytic cascades. Besides its importance, the knowledge on immune functions of serpins in most of insects is fragmentary. In the present study, we identified serpin-12 from Antheraea pernyi encoding a predicted 402 amino acid residue protein (Apserpin-12). We expressed the recombinant protein in Escherichia coli and the purified protein was used for the synthesis of rabbit anti-Apserpin-12 polyclonal antibodies and functional studies. Quantitative real-time ploymerase chain reaction (qRT-PCR) analysis revealed that the knock-down of Apserpin-12 enhanced the prophenoloxidase (PPO) cascade stimulated by Micrococcus luteus in hemolymph, whereas addition of recombinant Apserpin-12 protein along with same elicitor led to down-regulate PPO activation. Following different microbial challenge (E. coli, Beauveria bassiana, M. Luteus, and nuclear polyhedrosis virus), the expression of Apserpin-12 mRNA was induced significantly. Furthermore, the Apserpin-12 double-stranded RNA administration elicited the expression of antimicrobial peptides, while the treatment with recombinant protein suppressed their expression. Tissue profile of Apserpin-12 indicated that it is expressed in all examined tissues, that is, hemolymph, malpighian tubules, midgut, silk gland, integument, and fat body with variation in their transcript levels. We concluded that Apserpin-12 may regulate PPO activation and inhibit the production of antimicrobial peptides in A. pernyi, suggesting important role in its immune system. [Mh] Termos MeSH primário: Catecol Oxidase/metabolismo Precursores Enzimáticos/metabolismo Mariposas/química Serpinas/isolamento & purificação [Mh] Termos MeSH secundário: Sequência de Aminoácidos Animais Peptídeos Catiônicos Antimicrobianos/metabolismo Ativação Enzimática Escherichia coli Mariposas/fisiologia Filogenia Serpinas/química Serpinas/genética Serpinas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antimicrobial Cationic Peptides); 0 (Enzyme Precursors); 0 (Serpins); EC 1.10.3.- (pro-phenoloxidase); EC 1.10.3.1 (Catechol Oxidase) [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: 171202 [St] Status: MEDLINE [do] DOI: 10.1002/arch.21435

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[PMID]: 29218491 [Au] Autor: Prexler SM; Singh R; Moerschbacher BM; Dirks-Hofmeister ME [Ad] Endereço: Institute for Biology and Biotechnology of Plants, University of Münster, Schlossplatz 8, 48143, Münster, Germany. [Ti] Título: A specific amino acid residue in the catalytic site of dandelion polyphenol oxidases acts as 'selector' for substrate specificity. [So] Source: Plant Mol Biol;96(1-2):151-164, 2018 Jan. [Is] ISSN: 1573-5028 [Cp] País de publicação: Netherlands [La] Idioma: eng [Ab] Resumo: KEY MESSAGE: Successful site-directed mutagenesis combined with in silico modeling and docking studies for the first time offers experimental proof of the role of the 'substrate selector' residue in plant polyphenol oxidases. The plant and fungi enzymes responsible for tissue browning are called polyphenol oxidases (PPOs). In plants, PPOs often occur as families of isoenzymes which are differentially expressed, but little is known about their physiological roles or natural substrates. In a recent study that explored these structure-function relationships, the eleven known dandelion (Taraxacum officinale) PPOs were shown to separate into two different phylogenetic groups differing in catalytic cavity architecture, kinetic parameters, and substrate range. The same study proposed that the PPOs' substrate specificity is controlled by one specific amino acid residue positioned at the entrance to the catalytic site: whereas group 1 dandelion PPOs possess a hydrophobic isoleucine (I) at position H +1, group 2 PPOs exhibit a larger, positively charged arginine (R). However, this suggestion was only based on bioinformatic analyses, not experiments. To experimentally investigate this hypothesis, we converted group 1 ToPPO-2 and group 2 ToPPO-6 into PPO-2-I R and PPO-6-R I, respectively, and expressed them in E. coli. By performing detailed kinetic characterization and in silico docking studies, we found that replacing this single amino acid significantly changed the PPO's substrate specificity. Our findings therefore proof the role of the 'substrate selector' in plant PPOs. [Mh] Termos MeSH primário: Catecol Oxidase/metabolismo Taraxacum/metabolismo [Mh] Termos MeSH secundário: Domínio Catalítico Catecol Oxidase/genética Cinética Relação Estrutura-Atividade Especificidade por Substrato Taraxacum/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: EC 1.10.3.1 (Catechol Oxidase) [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: 171209 [St] Status: MEDLINE [do] DOI: 10.1007/s11103-017-0686-5

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[PMID]: 27770411 [Au] Autor: Minteer SD [Ad] Endereço: Departments of Chemistry and Materials Science and Engineering, University of Utah, Salt Lake City, UT, USA. minteer@chem.utah.edu. [Ti] Título: Micellar Enzymology for Thermal, pH, and Solvent Stability. [So] Source: Methods Mol Biol;1504:19-23, 2017. [Is] ISSN: 1940-6029 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: This chapter describes methods for enzyme stabilization using micellar solutions. Micellar solutions have been shown to increase the thermal stability, as well as the pH and solvent tolerance of enzymes. This field is traditionally referred to as micellar enzymology. This chapter details the use of ionic and nonionic micelles for the stabilization of polyphenol oxidase, lipase, and catalase, although this method could be used with any enzymatic system or enzyme cascade system. [Mh] Termos MeSH primário: Agaricales/enzimologia Catalase/química Catecol Oxidase/química Chromobacterium/enzimologia Lipase/química Micelas [Mh] Termos MeSH secundário: Agaricales/química Animais Bovinos Chromobacterium/química Estabilidade Enzimática Concentração de Íons de Hidrogênio Cinética Lipídeos/química Fígado/enzimologia Solventes/química Tensoativos/química Temperatura Ambiente [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Lipids); 0 (Micelles); 0 (Solvents); 0 (Surface-Active Agents); EC 1.10.3.1 (Catechol Oxidase); EC 1.11.1.6 (Catalase); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (lipase, Chromobacterium viscosum) [Em] Mês de entrada: 1801 [Cu] Atualização por classe: 180115 [Lr] Data última revisão: 180115 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161023 [St] Status: MEDLINE

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[PMID]: 28547775 [Au] Autor: Sun J; Wang M; Liu H; Xie J; Pan Y; Xu C; Zhao Y [Ad] Endereço: College of Food Science and Technology, Shanghai Ocean University, Shanghai, China. [Ti] Título: Acidic electrolysed water delays browning by destroying conformation of polyphenoloxidase. [So] Source: J Sci Food Agric;98(1):147-153, 2018 Jan. [Is] ISSN: 1097-0010 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: BACKGROUND: Browning frequently occurs at fruits, vegetables and aquatic products during storage, and it drastically reduces the consumer's acceptability, with considerable financial loss. The objective of this paper was to investigate the effects of acidic electrolysed water (AEW) technology on polyphenoloxidase (PPO), which is an essential enzyme for browning. RESULTS: AEW ice exhibited a good ability in delaying browning in shrimp. Kinetic study revealed that AEW exhibited the mixed type inhibition of PPO with a K value of 1.96 mmol L . Moreover, both the circular dichroism spectrum and Fourier transform infrared spectroscopy analyses revealed that the α-helix in PPO decreased whereas random coil increased which indicates that PPO conformation was destroyed. CONCLUSION: Thus, this paper may provide a deeper understanding of the application of AEW technology for preventing browning in the food industry. © 2017 Society of Chemical Industry. [Mh] Termos MeSH primário: Catecol Oxidase/química Palaemonidae/enzimologia Água/química [Mh] Termos MeSH secundário: Animais Dicroísmo Circular Cor Conservação de Alimentos Cinética Palaemonidae/química Conformação Proteica [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 059QF0KO0R (Water); EC 1.10.3.1 (Catechol Oxidase) [Em] Mês de entrada: 1801 [Cu] Atualização por classe: 180102 [Lr] Data última revisão: 180102 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170527 [St] Status: MEDLINE [do] DOI: 10.1002/jsfa.8449

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[PMID]: 28873535 [Au] Autor: Sikora M; Swieca M [Ad] Endereço: Department of Biochemistry and Food Chemistry, University of Life Sciences, Skromna Str. 8, 20-704 Lublin, Poland. Electronic address: malgorzata.sikora@up.lublin.pl. [Ti] Título: Effect of ascorbic acid postharvest treatment on enzymatic browning, phenolics and antioxidant capacity of stored mung bean sprouts. [So] Source: Food Chem;239:1160-1166, 2018 Jan 15. [Is] ISSN: 0308-8146 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Enzymatic browning limits the postharvest life of minimally processed foods, thus the study selected the optimal inhibitors of polyphenol oxidase (PPO) and evaluated their effect on enzymatic browning, phenolics and antioxidant capacity of stored mung bean sprouts. The sprouts treated with 2mM and 20mM ascorbic acid had a lowered PPO activity; compared to the control by 51% and 60%, respectively. The inhibition was reflected in a significant decrease in enzymatic browning. The sprouts treated with 20mM ascorbic acid had 22% and 23% higher phenolic content after 3 and 7days of storage, respectively. Both storage and ascorbic acid treatment increased potential bioaccessibility of phenolics. Generally, there was no effect of the treatments on the antioxidant capacity; however, a significant increase in the reducing potential was determined for the sprouts washed with 20mM ascorbic acid. In conclusion, ascorbic acid treatments may improve consumer quality of stored sprouts. [Mh] Termos MeSH primário: Vigna [Mh] Termos MeSH secundário: Antioxidantes Ácido Ascórbico Catecol Oxidase Fenóis [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antioxidants); 0 (Phenols); EC 1.10.3.1 (Catechol Oxidase); PQ6CK8PD0R (Ascorbic Acid) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171128 [Lr] Data última revisão: 171128 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170907 [St] Status: MEDLINE

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[PMID]: 28456299 [Au] Autor: Li J; Kang T; Talab KMA; Zhu F; Li J [Ad] Endereço: College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, China. [Ti] Título: Molecular and biochemical characterization of dimethachlone resistant isolates of Sclerotinia sclerotiorum. [So] Source: Pestic Biochem Physiol;138:15-21, 2017 May. [Is] ISSN: 1095-9939 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Sclerotinia sclerotiorum is a necrotrophic fungal plant pathogen with a broad host range. The dicarboximide fungicide dimethachlone has been used to control this pathogen for more than a decade and resistance to dimethachlone has recently been reported in China. Compared with sensitive isolates, the three dimethachlone resistant isolates with resistance ratios of 78.3, 85.5, and 94.8 exhibited significantly (P<0.05) higher cell membrane permeability and peroxidase and polyphenol oxidase activities. Dimethachlone at 0.25µg/mL significantly increased cell membrane permeability and enhanced activity of the two enzymes in both resistant and sensitive isolates. There were no significant differences in glycerol or oxalate content between the resistant and sensitive isolates. Dimethachlone treatment increased glycerol content in the resistant isolates and reduced in the sensitive isolates (P<0.01). Sequencing of three genes involved in two-component signal pathway and of three genes in mitogen-activated protein (MAP) kinase cascade demonstrated that the dimethachlone resistant isolates HLJ4 and HLJ6 harbored point mutations of I232T and G1087D, respectively, in the deduce amino acid sequence of the histidine kinase (HK) gene Sshk. HLJ4 had a point mutation of P96L in the deduced amino acid sequence of the MAP kinase-kinase gene SsPbs. The expression levels of the Sshk gene were higher in HLJ4 and HLJ6 than in HLJ3 and the sensitive isolate HLJMG2, and transcription of the Sshk gene was up-regulated by dimethachlone for the three resistant isolates. [Mh] Termos MeSH primário: Ascomicetos/efeitos dos fármacos Clorobenzenos/farmacologia Farmacorresistência Fúngica Fungicidas Industriais/farmacologia Succinimidas/farmacologia [Mh] Termos MeSH secundário: Sequência de Bases Catecol Oxidase/genética Catecol Oxidase/metabolismo Clonagem Molecular Proteínas Fúngicas/genética Proteínas Fúngicas/metabolismo Regulação Enzimológica da Expressão Gênica Regulação Fúngica da Expressão Gênica Mutação [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Chlorobenzenes); 0 (Fungal Proteins); 0 (Fungicides, Industrial); 0 (Succinimides); 0 (dimethachlon); EC 1.10.3.1 (Catechol Oxidase) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171128 [Lr] Data última revisão: 171128 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170501 [St] Status: MEDLINE

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[PMID]: 28844653 [Au] Autor: Vogelweith F; Moret Y; Thiéry D; Delbac L; Moreau J [Ad] Endereço: Johannes-Gutenberg University of Mainz, Institute of Organismic and Molecular Evolution, Behavioral Ecology and Social Evolution Group, Johannes-von-Müller-Weg 6, 55128 Mainz, Germany. Electronic address: fanny.vogelweith@gmail.com. [Ti] Título: No evidence of an immune adjustment in response to a parasitoid threat in Lobesia botrana larvae. [So] Source: J Insect Physiol;102:7-11, 2017 Oct. [Is] ISSN: 1879-1611 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Immune function is a key determinant of an organism's fitness, and natural insect populations are highly variable for this trait, mainly due to environmental heterogeneity and pathogen diversity. We previously reported a positive correlation between infection prevalence by parasitoids and host immunity in natural populations of the vineyard pest Lobesia botrana. Here, we tested whether this correlation reflects a plastic adjustment of host immunity in response to the local presence of parasites. To this end, we measured immunity of non-parasitized L. botrana larvae exposed, respectively, to one of the two most common species of parasitoids in vineyards, over 6days. Larvae were able to sense the parasitoid through visual, chemical, or mechanical cues, but contact larvae-parasitoid were excluded. Contrary to our hypothesis, we found that L. botrana larvae did not increase their immune defenses in the presence of parasitoids, despite their ability to sense a potential threat. Our results therefore suggest that the positive correlation between infection prevalence by parasitoids and L. botrana immunity among natural populations may result from micro-evolutionary changes resulting from long-term local selection pressures imposed by parasitoids in wild populations rather than plastic adjustments of immunity. [Mh] Termos MeSH primário: Mariposas/imunologia Mariposas/parasitologia Vespas/fisiologia [Mh] Termos MeSH secundário: Animais Catecol Oxidase/metabolismo Precursores Enzimáticos/metabolismo Hemócitos/metabolismo Proteínas de Insetos/metabolismo Larva/crescimento & desenvolvimento Larva/imunologia Larva/parasitologia Larva/fisiologia Mariposas/crescimento & desenvolvimento Vespas/crescimento & desenvolvimento [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Enzyme Precursors); 0 (Insect Proteins); EC 1.10.3.- (pro-phenoloxidase); EC 1.10.3.1 (Catechol Oxidase) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171025 [Lr] Data última revisão: 171025 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170829 [St] Status: MEDLINE

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[PMID]: 28812349 [Au] Autor: Derardja AE; Pretzler M; Kampatsikas I; Barkat M; Rompel A [Ad] Endereço: Universität Wien , Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090 Wien, Austria. [Ti] Título: Purification and Characterization of Latent Polyphenol Oxidase from Apricot (Prunus armeniaca L.). [So] Source: J Agric Food Chem;65(37):8203-8212, 2017 Sep 20. [Is] ISSN: 1520-5118 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Polyphenol oxidase from apricot (Prunus armeniaca) (PaPPO) was purified in its latent form (L-PaPPO), and the molecular weight was determined to be 63 kDa by SDS-PAGE. L-PaPPO was activated in the presence of substrate at low pH. The activity was enhanced by CuSO and low concentrations (≤ 2 mM) of SDS. PaPPO has its pH and temperature optimum at pH 4.5 and 45 °C for catechol as substrate. It showed diphenolase activity and highest affinity toward 4-methylcatechol (K = 2.0 mM) and chlorogenic acid (K = 2.7 mM). L-PaPPO was found to be spontaneously activated during storage at 4 °C, creating a new band at 38 kDa representing the activated form (A-PaPPO). The mass of A-PaPPO was determined by mass spectrometry as 37 455.6 Da (Asp102 → Leu429). Both L-PaPPO and A-PaPPO were identified as polyphenol oxidase corresponding to the known PaPPO sequence (UniProt O81103 ) by means of peptide mass fingerprinting. [Mh] Termos MeSH primário: Catecol Oxidase/química Catecol Oxidase/isolamento & purificação Proteínas de Plantas/química Proteínas de Plantas/isolamento & purificação Prunus armeniaca/enzimologia [Mh] Termos MeSH secundário: Catecol Oxidase/genética Catecol Oxidase/metabolismo Ácido Clorogênico/metabolismo Concentração de Íons de Hidrogênio Cinética Peso Molecular Proteínas de Plantas/genética Proteínas de Plantas/metabolismo Prunus armeniaca/química Prunus armeniaca/genética Especificidade por Substrato Temperatura Ambiente [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Plant Proteins); 318ADP12RI (Chlorogenic Acid); EC 1.10.3.1 (Catechol Oxidase) [Em] Mês de entrada: 1711 [Cu] Atualização por classe: 171113 [Lr] Data última revisão: 171113 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170817 [St] Status: MEDLINE [do] DOI: 10.1021/acs.jafc.7b03210

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[PMID]: 28681699 [Au] Autor: Noda T; Iimure K; Okamoto S; Saito A [Ad] Endereço: a Kumamoto Prefectural Agriculture Research Center , Koshi , Japan. [Ti] Título: Expression analysis of polyphenol oxidase isozymes by active staining method and tissue browning of head lettuce (Lactuca sativa L.). [So] Source: Biosci Biotechnol Biochem;81(8):1484-1488, 2017 Aug. [Is] ISSN: 1347-6947 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Browning of plant tissue is generally considered attributable to enzymatic oxidation by polyphenol oxidase (PPO). Electrophoresis followed by activity staining has been used as an effective procedure to visually detect and isolate isozymes; however, it has not been applied for examination of various PPO isozymes in lettuce. Our study demonstrated that different lettuce PPO isozymes could be detected at different pH in active staining, and multiple isozymes were detected only under alkaline conditions. As a result, we concluded that activity staining with approximately pH 8 enabled to detect various PPO isozymes in lettuce. By expression analysis of the PPO isozymes after wounding, PPO isozymes that correlated with time-course of tissue browning were detected. The wound-induced PPO may play a key role in enzymatic browning. [Mh] Termos MeSH primário: Catecol Oxidase/genética Regulação da Expressão Gênica de Plantas Alface/genética Folhas de Planta/genética Proteínas de Plantas/genética Coloração e Rotulagem/métodos [Mh] Termos MeSH secundário: Catecol Oxidase/metabolismo Eletroforese em Gel de Poliacrilamida Ensaios Enzimáticos Concentração de Íons de Hidrogênio Isoenzimas/genética Isoenzimas/metabolismo Alface/enzimologia Reação de Maillard Oxirredução Folhas de Planta/enzimologia Proteínas de Plantas/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Isoenzymes); 0 (Plant Proteins); EC 1.10.3.1 (Catechol Oxidase) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170726 [Lr] Data última revisão: 170726 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170707 [St] Status: MEDLINE [do] DOI: 10.1080/09168451.2017.1336921

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[PMID]: 28600687 [Au] Autor: Rowen E; Gutensohn M; Dudareva N; Kaplan I [Ad] Endereço: Department of Entomology, Pennsylvania State University, University Park, PA, 16802, USA. epr5119@psu.edu. [Ti] Título: Carnivore Attractant or Plant Elicitor? Multifunctional Roles of Methyl Salicylate Lures in Tomato Defense. [So] Source: J Chem Ecol;43(6):573-585, 2017 Jun. [Is] ISSN: 1573-1561 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Synthetic plant volatile lures attract natural enemies, but may have non-target effects due to the multifunctional nature of volatile signals. For example, methyl salicylate (MeSA) is used to attract predators, yet also serves as a signaling hormone involved in plant pathogen defense. We investigated the consequences of deploying MeSA lures to attract predators for tomato (Solanum lycopersicum) defense against herbivores. To understand the spatial distribution of the lure's effect, we exposed tomatoes in the field to MeSA along a linear distance gradient and induced defenses by simulating feeding by hornworm caterpillars in a fully crossed factorial design (+/- MeSA, +/- herbivory). Subsequently, we analyzed activity of several defensive proteins (protease inhibitors, polyphenol oxidase, peroxidase), development of hornworm larvae (Manduca sexta), growth of fungal pathogens (Cladosporium and Alternaria), and attractiveness to herbivores and predators. Overall, MeSA-exposed plants were more resistant to both insects and pathogens. Secondary pathogen infection was reduced by 25% in MeSA exposed plants, possibly due to elevated polyphenol oxidase activity. Interestingly, we found that lures affected plant pathogen defenses equivalently across all distances (up to 4 m away) indicating that horizontal diffusion of a synthetic volatile may be greater than previously assumed. While thrips avoided colonizing hornworm- damaged tomato plants, this induced resistance was not observed upon pre-exposure to MeSA, suggesting that MeSA suppresses the repellant effect induced by herbivory. Thus, using MeSA lures in biological control may inadvertently protect crops from pathogens, but has mixed effects on plant resistance to insect herbivores. [Mh] Termos MeSH primário: Herbivoria Lycopersicon esculentum Manduca/fisiologia Salicilatos/química Salicilatos/farmacologia [Mh] Termos MeSH secundário: Alternaria/crescimento & desenvolvimento Animais Catecol Oxidase/metabolismo Cladosporium/crescimento & desenvolvimento Larva/fisiologia Lycopersicon esculentum/metabolismo Lycopersicon esculentum/microbiologia Peroxidase/metabolismo Controle Biológico de Vetores Folhas de Planta/microbiologia Inibidores de Proteases/metabolismo Espectrometria de Massas em Tandem Compostos Orgânicos Voláteis/química Compostos Orgânicos Voláteis/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Protease Inhibitors); 0 (Salicylates); 0 (Volatile Organic Compounds); EC 1.10.3.1 (Catechol Oxidase); EC 1.11.1.7 (Peroxidase); LAV5U5022Y (methyl salicylate) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170801 [Lr] Data última revisão: 170801 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170611 [St] Status: MEDLINE [do] DOI: 10.1007/s10886-017-0856-6

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