Literature DB >> 8431598

Chitin synthesis and degradation as targets for pesticide action.

E Cohen1.   

Abstract

Various pesticides are being used to destabilize, perturb, or inhibit crucial biochemical and physiological targets related to metabolism, growth, development, nervous communication, or behavior in pestiferous organisms. Chitin is an eukaryotic extracellular aminosugar biopolymer, massively produced by most fungal systems and by invertebrates, notably arthropods. Being an integral supportive component in fungal cell wall, insect cuticle, and nematode egg shell, chitin has been considered as a selective target for pesticide action. Throughout the elaborate processes of chitin formation and deposition, only the polymerization events associated with the cell membrane compartment are so far available for chemical interference. Currently, the actinomycetes-derived nucleoside peptide fungicides such as the polyoxins and the insecticidal benzoylaryl ureas have reached commercial pesticide status. The polyoxins and other structurally-related antibiotics like nikkomycins are strong competitive inhibitors of the polymerizing enzyme chitin synthase. The exact biochemical lesion inflicted by the benzoylaryl ureas is still elusive, but a post-polymerization event, such as translocation of chitin chains across the cell membrane, is suggested. Hydrolytic degradation of the chitin polymer is essential for hyphal growth, branching, and septum formation in fungal systems as well as for the normal molting of arthropods. Recently, insect chitinase activity was strongly and specifically suppressed by allosamidin, an actimomycetes-derived metabolite. In part, the defense mechanism in plants against invasion of pathogens is associated with induced chitinases. Chitin, chitosan, and their oligomers are able to act as elicitors which induce enhanced levels of chitinases in various plants. Lectins which bind to N-acetyl-D-glucosamine strongly interfere with fungal and insect chitin synthases. Plant lectins with similar properties may be involved in plant-pathogen interaction inter alia by suppressing fungal invasion.

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Year:  1993        PMID: 8431598     DOI: 10.1002/arch.940220118

Source DB:  PubMed          Journal:  Arch Insect Biochem Physiol        ISSN: 0739-4462            Impact factor:   1.698


  19 in total

1.  High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate.

Authors:  Douglas R Houston; Kazuro Shiomi; Noriko Arai; Satoshi Omura; Martin G Peter; Andreas Turberg; Bjørnar Synstad; Vincent G H Eijsink; Daan M F van Aalten
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-01       Impact factor: 11.205

2.  Comparative studies of differential expression of chitinolytic enzymes encoded by chiA, chiB, chiC and nagA genes in Aspergillus nidulans.

Authors:  T Pusztahelyi; Z Molnár; T Emri; E Klement; M Miskei; J Kerékgyárto; J Balla; I Pócsi
Journal:  Folia Microbiol (Praha)       Date:  2006       Impact factor: 2.099

3.  Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.

Authors:  Henrik Zakariassen; Berit Bjugan Aam; Svein J Horn; Kjell M Vårum; Morten Sørlie; Vincent G H Eijsink
Journal:  J Biol Chem       Date:  2009-02-25       Impact factor: 5.157

4.  Molecular cloning and functional expression of chitinase-encoding cDNA from the cabbage moth, Mamestra brassicae.

Authors:  Aron Paek; Hee Yun Park; Seong Eun Jeong
Journal:  Mol Cells       Date:  2011-11-25       Impact factor: 5.034

Review 5.  Insect chitin synthases: a review.

Authors:  Hans Merzendorfer
Journal:  J Comp Physiol B       Date:  2005-08-02       Impact factor: 2.200

6.  Nikkomycin Z is a specific inhibitor of Saccharomyces cerevisiae chitin synthase isozyme Chs3 in vitro and in vivo.

Authors:  J P Gaughran; M H Lai; D R Kirsch; S J Silverman
Journal:  J Bacteriol       Date:  1994-09       Impact factor: 3.490

7.  The Saccharomyces cerevisiae chitinase, encoded by the CTS1-2 gene, confers antifungal activity against Botrytis cinerea to transgenic tobacco.

Authors:  M Carstens; M A Vivier; I S Pretorius
Journal:  Transgenic Res       Date:  2003-08       Impact factor: 2.788

8.  Analysis of a three-dimensional structure of human acidic mammalian chitinase obtained by homology modeling and ligand binding studies.

Authors:  Yong-Shan Zhao; Qing-Chuan Zheng; Hong-Xing Zhang; Hui-Ying Chu; Chia-Chung Sun
Journal:  J Mol Model       Date:  2008-12-16       Impact factor: 1.810

9.  Secretion of an enzymatically active Trichoderma harzianum endochitinase by Saccharomyces cerevisiae.

Authors:  H Draborg; S Christgau; T Halkier; G Rasmussen; H Dalbøge; S Kauppinen
Journal:  Curr Genet       Date:  1996-03       Impact factor: 3.886

10.  Setal-epidermal, muscular and enzymatic anomalies induced by certain agrochemicals in the earthworm Eudrilus eugeniae (Kinberg).

Authors:  Suryasikha Samal; C S K Mishra; Sunanda Sahoo
Journal:  Environ Sci Pollut Res Int       Date:  2019-01-26       Impact factor: 4.223

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