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Alteração da atividade enzimática em organismos aquáticos por poluentes de origem agrícola: uma abordagem geral e sobre a suscetibilidade da fosfatase ácida Translated title: Alteration of enzymatic activity in aquatic organisms by agricultural pollutants: a general approach and the susceptibility of the acid phosphatase

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      Translated abstract

      The input of agrochemicals in the aquatic compartment can results in biochemical injuries for living organisms. In this context, the knowledge of alterations of enzymatic activities due the presence of agriculture pollutants contributes for the elucidation of the mechanisms of toxicity, implementation of economic methods for monitoring purposes and establishment of maximum allowed concentrations. In the present work, the above considerations are discussed, and data concerning changes in enzymatic function by pesticides and fertilizer contaminants are reviewed. Also, we focused on the acid phosphatase due its susceptibility to several pollutants and diversity in cellular functions.

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      FlhF is required for swimming and swarming in Pseudomonas aeruginosa.

      FlhF is a signal recognition particle-like protein present in monotrichous bacteria. The loss of FlhF in various bacteria results in decreased transcription of class II, III, or IV flagellar genes, leads to diminished or absent motility, and results in the assembly of flagella at nonpolar locations on the cell surface. In this work, we demonstrate that the loss of FlhF results in defective swimming and swarming motility of Pseudomonas aeruginosa. The FlhF protein localizes to the flagellar pole; in the absence of FlhF, flagellar assembly occurs but is no longer restricted to the pole. DeltaflhF bacteria swim at lower velocities than wild-type bacteria in liquid media and can no longer swarm when assayed under standard swarming conditions (0.5% agar). However, DeltaflhF bacteria regain swarming behavior when plated on 0.3% agar. DeltaflhF organisms show decreased transcription and expression of flagellin (FliC) both in liquid media and on swarming plates compared to wild-type bacteria. However, changes in flagellin expression do not explain the different motility patterns observed for DeltaflhF bacteria. Instead, the aberrant placement of flagella in DeltaflhF bacteria may reduce their ability to move this rod-shaped organism effectively.
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        Recent advances in QM/MM free energy calculations using reference potentials☆

        Background Recent years have seen enormous progress in the development of methods for modeling (bio)molecular systems. This has allowed for the simulation of ever larger and more complex systems. However, as such complexity increases, the requirements needed for these models to be accurate and physically meaningful become more and more difficult to fulfill. The use of simplified models to describe complex biological systems has long been shown to be an effective way to overcome some of the limitations associated with this computational cost in a rational way. Scope of review Hybrid QM/MM approaches have rapidly become one of the most popular computational tools for studying chemical reactivity in biomolecular systems. However, the high cost involved in performing high-level QM calculations has limited the applicability of these approaches when calculating free energies of chemical processes. In this review, we present some of the advances in using reference potentials and mean field approximations to accelerate high-level QM/MM calculations. We present illustrative applications of these approaches and discuss challenges and future perspectives for the field. Major conclusions The use of physically-based simplifications has shown to effectively reduce the cost of high-level QM/MM calculations. In particular, lower-level reference potentials enable one to reduce the cost of expensive free energy calculations, thus expanding the scope of problems that can be addressed. General significance As was already demonstrated 40 years ago, the usage of simplified models still allows one to obtain cutting edge results with substantially reduced computational cost. This article is part of a Special Issue entitled Recent developments of molecular dynamics.
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          Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12.

          The iron-regulated aerobactin operon, about 8 kilobase pairs in size, of the Escherichia coli plasmid ColV-K30 was shown by deletion and subcloning analyses to consist of at least five genes for synthesis (iuc, iron uptake chelate) and transport (iut, iron uptake transport) of the siderophore. The gene order iucABCD iutA was established. The genes were mapped within restriction nuclease fragments of a cloned 16.3-kilobase-pair HindIII fragment. Stepwise deletion and subsequent minicell analysis of the resulting plasmids allowed assignment of four of the five genes to polypeptides of molecular masses 63,000, 33,000 53,000, and 74,000 daltons, respectively. The 74-kilodalton protein, the product of gene iutA, is the outer membrane receptor for ferric aerobactin, whereas the remaining three proteins are involved in biosynthesis of aerobactin. The 33-kilodalton protein, the product of gene iucB, was identified as N epsilon-hydroxylysine:acetyl coenzyme A N epsilon-transacetylase (acetylase) by comparison of enzyme activity in extracts from various deletion mutants. The 53-kilodalton protein, the product of gene iucD, is required for oxygenation of lysine. The 63-kilodalton protein, the product of gene iucA, is assigned to the first step of the aerobactin synthetase reaction. The product of gene iucC, so far unidentified, performs the second and final step in this reaction. This is based on the chemical characterization of two precursor hydroxamic acids (N epsilon-acetyl-N epsilon-hydroxylysine and N alpha-citryl-N epsilon-acetyl-N epsilon-hydroxylysine) isolated from a strain carrying a 0.3-kilobase-pair deletion in the iucC gene. The results support the existence of a biosynthetic pathway in which aerobactin arises by oxygenation of lysine, acetylation of the N epsilon-hydroxy function, and condensation of 2 mol of the resulting aminohydroxamic acid with citric acid.
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            Author and article information

            Affiliations
            [1 ] Embrapa Meio Ambiente Brazil
            [2 ] Universidade Estadual de Campinas Brazil
            Contributors
            Role: ND
            Role: ND
            Journal
            qn
            Química Nova
            Quím. Nova
            Sociedade Brasileira de Química (São Paulo )
            1678-7064
            2010
            : 33
            : 4
            : 920-928
            S0100-40422010000400030 10.1590/S0100-40422010000400030

            http://creativecommons.org/licenses/by/4.0/

            Product
            Product Information: SciELO Brazil
            Categories
            CHEMISTRY, MULTIDISCIPLINARY

            General chemistry

            biomarker, enzyme, pollution

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