Canavanine

Canavanine

Names
Preferred IUPAC name Canavanine
Systematic IUPAC name (2S)-2-amino-4-{[(diaminomethylidene)amino]oxy}butanoic acid
Identifiers
CAS Number	543-38-4 N
ChEBI	CHEBI:609827
ChemSpider	388342
DrugBank	DB01833
Jmol 3D model	Interactive image
KEGG	C00308
MeSH	Canavanine
PubChem	275
InChI InChI=1S/C5H12N4O3/c6-3(4(10)11)1-2-12-9-5(7)8/h3H,1-2,6H2,(H,10,11)(H4,7,8,9)/t3-/m0/s1
SMILES N[C@@H](CCON=C(N)N)C(O)=O
Properties
Chemical formula	C5H12N4O3
Molar mass	176.18 g·mol−1
Density	1.61 g·cm−3 (predicted)
Melting point	184 °C (363 °F; 457 K)
Boiling point	366 °C (691 °F; 639 K)
Solubility in water	soluble
Solubility	insoluble in alcohol, ether, benzene
log P	-0.91 (predicted)
Vapor pressure	1.61 μPa (predicted)
Vapor pressure	{{{value}}}
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

L-(+)-(S)-Canavanine is a non-proteinogenic amino acid found in certain leguminous plants. It is structurally related to the proteinogenic α-amino acid L-arginine, the sole difference being the replacement of a methylene bridge (-CH
₂- unit) in arginine with an oxa group (i.e., an oxygen atom) in canavanine. Canavanine is accumulated primarily in the seeds of the organisms which produce it, where it serves both as a highly deleterious defensive compound against herbivores and a vital source of nitrogen for the growing embryo (see also L-canaline). The mechanism of canavanine's toxicity is that organisms that consume it typically mistakenly incorporate it into their own proteins in place of L-arginine, thereby producing structurally aberrant proteins that may not function properly.

File:Can-Arg.svg

Chemical structure of arginine compared to canavanine

Some specialized herbivores tolerate L-canavanine either because they metabolize it efficiently (cf. L-canaline) or avoid its incorporation into their own nascent proteins. An example of this ability can be found in the tobacco budworm Heliothis virescens the larvae of which can tolerate massive amounts of dietary canavanine. These larvae fastidiously avoid incorporation of L-canavanine into their nascent proteins (presumably by virtue of highly discriminatory Arginine—tRNA ligase, the enzyme responsible for the first step in the incorporation of arginine into proteins). In contrast, larvae of the tobacco hornworm Manduca sexta can only tolerate tiny amounts (1.0 microgram per kilogram of fresh body weight) of dietary canavanine because their arginine-tRNA ligase has little, if any, discriminatory capacity. No one has examined experimentally the arginine-tRNA synthetase of these organisms. But comparative studies of the incorporation of radiolabeled L-arginine and L-canavanine have shown that in Manduca sexta, the ratio of incorporation is about 3 to 1.

Dioclea megacarpa seeds contain high levels of canavanine. The beetle Caryedes brasiliensis is able to tolerate this however as it has the most highly discriminatory arginine-tRNA ligase known. In this insect, the level of radiolabeled L-canavanine incorporated into newly synthesized proteins is barely measurable. Moreover, this beetle uses canavanine as a nitrogen source to synthesize its other amino acids to allow it to develop.

NZB/W F1, NZB, and DBA/2 mice fed L-canavanine develop an SLE-like syndrome, while BALB/c mice fed a steady diet of protein containing 1% canavanine showed no change in lifespan. The toxicity of canavanine may be enhanced under conditions of protein starvation, and canavanine toxicity resulting from consumption of Hedysarum alpinum seeds, which contain quantities of canavanine around 1%, has been implicated in the death of Christopher McCandless.

Alfalfa seeds and sprouts contain L-canavanine. The L-canavanine in alfalfa has been linked to lupus-like symptoms in primates, including humans, and other auto-immune diseases. Often stopping consumption reverses the problem.

See also

• Canaline
• Arginine