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      El complejo enzimático citocromo P450 en las plantas Translated title: Enzymatic complex cytochrome P450 in plants

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          Abstract

          Las enzimas dependientes del citocromo P450 (CYP450) son importantes en la biosíntesis de diversas sustancias y en la desintoxicación de xenobióticos. En las plantas, estas enzimas participan en la biosíntesis de productos secundarios (e.g. flavonoides, alkaloides) y de hormonas, así como en la desintoxicación de herbicidas. Por otra parte, el empleo de técnicas moleculares ha permitido la inserción de genes del CYP450 de mamíferos en un mayor número de especies de plantas para favorecer la tolerancia a herbicidas. La presente aportación es una revisión bibliográfica sobre el potencial biotecnológico del complejo enzimático del CYP450.

          Translated abstract

          Cytochrome P450 dependent enzymes (CYP450) are important in the biosynthesis of many substances and in the detoxification of xenobiotics. In plants, they are involved in the biosynthesis of secondary products (e.g. flavonoids, alkaloids) and hormones, but also in the detoxification of herbicides. On the other hand, the use of molecular techniques, has allowed the insertion of genes of the CYP450 of mammals in a greater number of plants, favoring the tolerance to herbicides. The present contribution is an overview of the biotechnological potentiality of the enzymatic complex CYP450.

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          Most cited references84

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          BRASSINOSTEROIDS: Essential Regulators of Plant Growth and Development.

          Brassinosteroids (BRs) are growth-promoting natural products found at low levels in pollen, seeds, and young vegetative tissues throughout the plant kingdom. Detailed studies of BR biosynthesis and metabolism, coupled with the recent identification of BR-insensitive and BR-deficient mutants, has greatly expanded our view of steroids as signals controlling plant growth and development. This review examines the microchemical and molecular genetic analyses that have provided convincing evidence for an essential role of BRs in diverse developmental programs, including cell expansion, vascular differentiation, etiolation, and reproductive development. Recent advances relevant to the molecular mechanisms of BR-regulated gene expression and BR signal transduction are also discussed.
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            Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid.

            Abscisic acid (ABA) is involved in a number of critical processes in normal growth and development as well as in adaptive responses to environmental stresses. For correct and accurate actions, a physiologically active ABA level is controlled through fine-tuning of de novo biosynthesis and catabolism. The hydroxylation at the 8'-position of ABA is known as the key step of ABA catabolism, and this reaction is catalyzed by ABA 8'-hydroxylase, a cytochrome P450. Here, we demonstrate CYP707As as the P450 responsible for the 8'-hydroxylation of (+)-ABA. First, all four CYP707A cDNAs were cloned from Arabidopsis and used for the production of the recombinant proteins in insect cells using a baculovirus system. The insect cells expressing CYP707A3 efficiently metabolized (+)-ABA to yield phaseic acid, the isomerized form of 8'-hydroxy-ABA. The microsomes from the insect cells exhibited very strong activity of 8'-hydroxylation of (+)-ABA (K(m) = 1.3 microm and k(cat) = 15 min(-1)). The solubilized CYP707A3 protein bound (+)-ABA with the binding constant K(s) = 3.5 microm, but did not bind (-)-ABA. Detailed analyses of the reaction products confirmed that CYP707A3 does not have the isomerization activity of 8'-hydroxy-ABA to phaseic acid. Further experiments revealed that Arabidopsis CYP707A1 and CYP707A4 also encode ABA 8'-hydroxylase. The transcripts of the CYP707A genes increased in response to salt, osmotic, and dehydration stresses as well as ABA. These results establish that the CYP707A family plays a key role in regulating the ABA level through the 8'-hydroxylation of (+)-ABA.
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              C6-volatiles derived from the lipoxygenase pathway induce a subset of defense-related genes.

              Six-Carbon (C6-) volatiles, including the aldehydes trans-2-hexenal, hexanal and cis-3-hexenal, as well as their corresponding alcohols, are produced from damaged or wounded plant tissue as a product of the enzymatic activity of hydroperoxide lyase (HPL), a component of the lipoxygenase (LOX) pathway. Aerial treatment of Arabidopsis seedlings with 10 microM concentrations of trans-2-hexenal induces several genes known to be involved in the plant's defense response, including phenylpropanoid-related genes as well as genes of the LOX pathway. Genes encoding the pathogenesis-related proteins PR-1 or PR-2, however, were not induced. Trans-2-hexenal induction thus closely mimics the group of genes induced by methyl jasmonate (MeJA), also a LOX-derived volatile. However, unlike MeJA, trans-2-hexenal did not induce hydroxymethylglutaryl-coenzyme A reductase (HMGR) or thionin2-1. The inductive effect seemed to be limited to C6-related volatiles, as C8-, C9- and other related volatiles did not induce LOX mRNA levels. As has been demonstrated for MeJA, trans-2-hexenal quantitatively reduced wild-type seed germination. Trans-2-hexenal also reduced the germination frequency of the MeJA resistant Arabidopsis mutant, jar1-1, supporting the notion that trans-2-hexenal and MeJA are recognized via different mechanisms. In addition, trans-2-hexenal had a moderate inhibitory effect on root length relative to similar concentrations of MeJA and was approximately 10-fold less effective than MeJA at inducing anthocyanin accumulation in Arabidopsis seedlings. These results suggest that C6-volatiles of the LOX pathway act as a wound signal in plants, but result in a moderate plant response relative to MeJA at both the physiological and molecular level.
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                Author and article information

                Journal
                rica
                Revista internacional de contaminación ambiental
                Rev. Int. Contam. Ambient
                Centro de Ciencias de la Atmósfera, UNAM (México, DF, Mexico )
                0188-4999
                December 2007
                : 23
                : 4
                : 177-183
                Affiliations
                [01] México DF orgnameInstituto Nacional de Cardiología orgdiv1Departamento de Bioquímica México daniasaf@ 123456gmail.com
                Article
                S0188-49992007000400003 S0188-4999(07)02300400003
                3880275d-4013-4719-817d-234a3d399733

                This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

                History
                : 01 January 2007
                : 01 October 2007
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 49, Pages: 7
                Product

                SciELO Mexico

                Categories
                Revisión

                cytochrome P450,plants,herbicides,plantas,citocromo P450,tolerance,herbicidas,tolerancia

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