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  • 1
    Electronic Resource
    Electronic Resource
    Nitrogenous excretion by the terrestrial seed predator, Caryedes brasiliensis
    Amsterdam : Elsevier
    Biochemical Systematics and Ecology 9 (1981), S. 219-220 
    Details
    ISSN: 0305-1978
    Keywords: Bruchidae ; Caryedes brasiliensis ; Dioclea megacarpa ; Leguminosae ; insect nitrogen excretion ; l-canavanine ; plant-insect interaction
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0305-1978(81)90045-4
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  • 2
    Electronic Resource
    Electronic Resource
    Arginase and L-canavanine metabolism by the bruchid beetle, Caryedes brasiliensis (1983)
    Springer
    Entomologia experimentalis et applicata 34 (1983), S. 336-337 
    Details
    ISSN: 1570-7458
    Keywords: L-canavanine ; Caryedes brasiliensis ; Bruchidae ; Dioclea megacarpa ; Arginase ; Plant-insect interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00186935
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical insight into insecticidal properties ofl-Canavanine, a higher plant protective allelochemical (1986)
    Springer
    Journal of chemical ecology 12 (1986), S. 1145-1156 
    Details
    ISSN: 1573-1561
    Keywords: l-Canavanine ; Manduca sexta ; Lepidoptera ; Sphingidae ; Caryedes brasiliensis ; Dioclea megacarpa ; Leguminosae ; Sternechus tuberculatus ; Coleoptera ; Bruchidae ; Curculionidae ; Heliothis virescens ; Noctuidae ; allelochemicals ; toxicology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract l-Canavanine manifests potent insecticidal properties in a canavanine-sensitive insect such as the tobacco hornworm,Manduca sexta (L.) (Sphingidae). Investigations of the biochemical basis for the antimetabolic properties of this arginine analog reveal that it is activated and aminoacylated by arginyl tRNA synthetase and incorporated into the nascent polypeptide chain. This creates structurally aberrant, canavanine-containing proteins that can possess altered physicochemical properties. Evidence is presented in studies with the tobacco hornworm; the canavanine-adapted bruchid beetle,Caryedes brasiliensis (Bruchidae) and the weevil,Sternechus tuberculatus (Curculionidae); as well as the canavanine-resistant larvae ofHeliothis virescens [Noctuidae] to support the contention that formation of aberrant, canavanyl proteins produce deleterious biological effects and is a significant basis for canavanine's antimetabolic properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01639001
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  • 4
    Electronic Resource
    Electronic Resource
    Biochemical adaptations of the bruchid beetle,Caryedes brasiliensis tol-canavanine, a higher plant allelochemical (1983)
    Springer
    Journal of chemical ecology 9 (1983), S. 803-815 
    Details
    ISSN: 1573-1561
    Keywords: Caryedes brasiliensis ; Coleoptera ; Bruchidae ; l-canavanine ; l-canaline ; Dioclea megacarpa (Leguminosae) ; allelochemicals ; detoxification ; adaptation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract This communication reviews recent biochemical studies ofl-canavanine that have provided significant understanding of the interaction between the seed ofDioclea megacarpa (Leguminosae) and the bruchid beetleCaryedes brasiliensis (Bruchidae). The principal biochemical bases are proposed for: canavanine toxicity, the ability of the beetle larvae to adapt to its presence, the metabolic sequestration and detoxification of ammonia, and the potential amplification by microbial symbionts of the beetle's abilities to adapt to toxic components of the host.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00987806
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  • 5
    Electronic Resource
    Electronic Resource
    Ammonia utilization by the bruchid beetle,Caryedes brasiliensis [Bruchidae] (1985)
    Springer
    Journal of chemical ecology 11 (1985), S. 539-544 
    Details
    ISSN: 1573-1561
    Keywords: Ammonia utilization ; l-canavanine catabolism ; Caryedes brasiliensis ; Coleoptera ; Bruchidae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The seed predator,Caryedes brasiliensis [Bruchidae] generates appreciable ammonia in its dietary use and detoxification ofl-canavanine and its catabolic product,l-canaline.l-Canavanine is a toxic allelochemical ofDioclea megacarpa seeds, the food of the developing larvae. Bruchid beetle larvae rely upon glutamic acid dehydrogenase and glutamine synthetase to use ammonia for glutamic acid synthesis from 2-oxoglutaric acid and conversion of the former to glutamine. These reactions provide the larvae with a means for metabolically eliminating ammonia. Proline serves as a carbon skeleton source for glutamic acid formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00989564
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  • 6
    Electronic Resource
    Electronic Resource
    Avoidance of nonprotein amino acid incorporation into protein by the seed predator,Caryedes brasiliensis (Bruchidae) (1983)
    Springer
    Journal of chemical ecology 9 (1983), S. 1353-1361 
    Details
    ISSN: 1573-1561
    Keywords: Canavanine ; Caryedes brasiliensis ; Coleoptera ; Bruchidae ; Dioclea megacarpa ; plant-insect interactions ; amino acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Larvae of the bruchid beetle,Caryedes brasiliensis (Bruchidae) have the ability to avoid significant incorporation ofl-canavanine, the guanidinooxy structural analog ofl-arginine, into de novo synthesized proteins. This ability is related to a highly discriminatory protein-synthesizing system which exhibits marked ability to avoid processing an array of nonprotein amino acids structurally related to arginine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00994804
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