Systematic significance of canavanine in the Papilionoideae (faboideae)

Bell, E. A.; Lackey, James Alden; Polhill, R. M.

doi:10.1016/0305-1978(78)90008-x

Cited by 119 publications

(53 citation statements)

References 19 publications

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“…Consistent with previous reports showing that canavanine is absent from genus Hippocrepis [17], no canavanine was found in H. ciliata. However, the absence of canavanine in genus Scorpiurus does not agree with a previous report [14].…”

Section: Resultscontrasting

confidence: 96%

“…These results agree with previous reports of canavanine in Medicago [14]. In contrast, canavanine was not found at significant levels in Melilotus elegans and Ononis natrix, which also exhibited a relatively high content in total free amino acids.…”

Section: Resultssupporting

confidence: 92%

“…Our results are consistent with most of previous reports on the presence of canavanine in some species within tribe Loteae. Thus, our results confirm previous reports on the concentration of canavanine in Ornithopus compresus [14] in Lotus creticus [15], and in genus Hymenocarpos [14,16]. Although canavanine was previously found in Coronilla species [16], it was not found in Coronilla glauca (Table 1).…”

Section: Resultssupporting

confidence: 92%

See 2 more Smart Citations

Free Amino Acids, Including Canavanine, in the Seeds from 24 Wild Mediterranean Legumes

Megı́as¹,

Cortés-Giraldo²,

Girón‐Calle³

et al. 2016

J Food Chem Nanotechnol

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Section: Resultscontrasting

confidence: 96%

Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 92%

See 1 more Smart Citation

Free Amino Acids, Including Canavanine, in the Seeds from 24 Wild Mediterranean Legumes

Megı́as¹,

Cortés-Giraldo²,

Girón‐Calle³

et al. 2016

J Food Chem Nanotechnol

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“…L-Canavanine, a nonprotein amino acid found in at least 500 species of leguminous plants (2), is a potent antimetabolite, due in large measure to its structural analogy to L-arginine. Canavanine's marked insecticidal action, its ability to disrupt many essential biochemical reactions in a wide range of prokaryotic and eukaryotic organisms, and its appreciable storage in such important tissues as the seed are consistent with its allelochemical role in plant defense against phytophagous insects and other herbivores (14).…”

mentioning

confidence: 99%

l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. (Leguminosae)

Rosenthal¹

1982

Plant Physiol.

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L-Canavanine, a highly toxic arginine antimetabolite, is the principal nonprotein amino acid of many eguminous plants. Labeled-precursor feeding studies, conducted primarily with I'Clcarbamoyl sphate, and utilization of the seedlins of jack bean, Canavalia enuiformis (L.) DC. (Leguminosae), have provided evidence for L-canavanine biosynthesis from L-canaline via O-ureido-L-homoserine. This reaction pathway appears to constitute an important in vivo route ofcanavanine productiol Canavanine cleavage to canaline may represent a degradative phase of canavanine metabolism distinct from the anabolic reactions described above. Thus, while these reactions of canavanine metabolism bear analgy to the mammalian Krebs-Henseleit ornithie-urea cycle, no evidence has been obtained at present for the reutilization of canaline in ureidohonoserine formation.L-Canavanine, a nonprotein amino acid found in at least 500 species of leguminous plants (2), is a potent antimetabolite, due in large measure to its structural analogy to L-arginine. Canavanine's marked insecticidal action, its ability to disrupt many essential biochemical reactions in a wide range of prokaryotic and eukaryotic organisms, and its appreciable storage in such important tissues as the seed are consistent with its allelochemical role in plant defense against phytophagous insects and other herbivores (14).Canavanine is a major nitrogen storage metabolite of the seed, where it can account for 95% or more of the nitrogen found in the free amino acids (15). Its mobilization and utilization injack bean, Canavalia ens!formis (L.) DC. (Leguminosae), occurs via arginase (EC 3.5.3.1), which cleaves L-canavanine to L-canaline and urea (3). Urea is hydrolyzed by urease (EC 3.5.1.5) to CO2 and NH3; the latter, representing an important source of reduced nitrogen, is assimilated and incorporated into the amide nitrogen of asparagine (I 1).Experimental evidence has been obtained in jack bean for carbamylation ofcanaline with carbamoyl phosphate, in a reaction catalyzed by ornithine carbamoyltransferase (EC 2.1.3.3) to yield O-ureido-L-homoserine, a citrulline analog (12). Argininosuccinic acid lyase (EC 4.3.2.1), the enzyme-mediating conversion of Lcanavaninosuccinic acid to L-canavanine and fumaric acid, has been isolated and purified extensively from jack bean seed (16). Of the reactions depicted in Figure 1, it is the reaction fostered by argininosuccinic acid synthetase (EC 6.3 The enzymic reactions of the nonprotein amino acids depicted in Figure 1 result in a reaction pathway that bears similarity to mammalian urea production via the Krebs-Henseleit ornithineurea cycle. All of the ornithine-urea cycle enzymes have been isolated from several higher plants, including jack bean (18). Attempts have been made to isolate an enzyme responsible for the formation of one of the intermediates of canavanine metabolism that is distinct from its ornithine-urea cycle counterpart. These efforts have failed (3,9).One can readily demonstrate all of the ornithine-urea cycle e...

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“…L-Canavanine [L-2-amino-4-(guanidinooxy)butyric acid] is an L-arginine analog that occurs in at least 1500 legumes (1). This nonprotein amino acid can be the most abundant free amino acid of the plant (2).…”

mentioning

confidence: 99%

Purification and characterization of the higher plant enzyme L-canaline reductase.

Rosenthal

1992

Proc. Natl. Acad. Sci. U.S.A.

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A newly discovered enzyme, L-canaline reductase (NADPH:L-canaline oxidoreductase, EC 1.6.6.-), has been isolated and purified from 10-day-old leaves of the jack bean Canavalia ensiformis (Leguminosae). This higher plant is representative of a large number of legumes that synthesize L-canavanine, an important nitrogen-storing nonprotein amino acid. Canavanine-storing legumes contain arginase, which hydrolyzes L-canavanine to form the toxic metabolite L-canaline. Canaline reductase, having a mass of =167 kDa and composed of 82-kDa dimers, catalyzes a NADPH-dependent reductive cleavage of L-canaline to L-homoserine and ammonia. This is the only enzyme known to use reduced NADP to cleave an O-N bond. Canaline reductase performs at least three important functions for canavanine-synthesizing legumes. First, it detoxifies canaline. Second, it increases by one-half the overall yield of ammoniacal nitrogen released from canavanine. Third, it permits the carbon skeleton of canavanine, a secondary plant metabolite, to support vital primary metabolic reactions.

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Systematic significance of canavanine in the Papilionoideae (faboideae)

Cited by 119 publications

References 19 publications

Free Amino Acids, Including Canavanine, in the Seeds from 24 Wild Mediterranean Legumes

Free Amino Acids, Including Canavanine, in the Seeds from 24 Wild Mediterranean Legumes

l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. (Leguminosae)

Purification and characterization of the higher plant enzyme L-canaline reductase.

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