Top 10 similar words or synonyms for canaline

hydroxyornithine    0.932518

canavine    0.896328

canavinyl    0.890169

hydroxyomithine    0.875725

canalinyl    0.872029

hydroxyornithinyl    0.862341

diaminodicarboxylic    0.849721

diaminosuccinic    0.847369

piperidinic    0.834601

hydroxypipecolic    0.815849

Top 30 analogous words or synonyms for canaline

Article Example
Canaline -Canaline is the only naturally occurring amino acid known that has an "O"-alkyl hydroxylamine functionality in the side chain. This amino acid is structurally related to ornithine (it is the 5-oxa derivative) and is a potent insecticide. Tobacco hornworm larvae fed a diet containing 2.5 mM canaline showed massive developmental aberrations, and most larvae so treated died at the pupal stage. It also exhibits potent neurotoxic effects in the moth.
Canaline Its toxicity stems primarily from the fact that it readily forms oximes with keto acids and aldehydes, especially the pyridoxal phosphate cofactor of many vitamin B-dependent enzymes. It inhibits ornithine aminotransferase at concentrations as low as 10 nM.
Canaline -Canaline (IUPAC name 2-amino-4-(aminooxy)butyric acid)) is a non-proteinogenic amino acid. The compound is found in legumes that contain canavanine, from which it is produced by the action of arginase. The most common-used source for this amino acid is the jack bean, "Canavalia ensiformis". It is grown commercially as a source of the enzyme urease.
Canaline -Canaline is a substrate for ornithine aminotransferase resulting in the synthesis of -ureidohomoserine (the corresponding analog of -citrulline). In turn, the latter forms -canavaninosuccinic acid in a reaction mediated by argininosuccinic acid synthetase. -Canavaninosuccinic acid is cleaved to form -canavanine by argininosuccinic acid synthetase. By these sequential reactions, the canaline-urea cycle (analogous to the ornithine-urea cycle) is formed. Every time a canavanine molecule runs through the canaline-urea cycle, the two terminal nitrogen atoms are released as urea. Urea is an important by-product of this reaction sequence because it makes ammonicial ammonia (urease-mediated) that is available to support intermediary nitrogen metabolism. -Canaline can by reductively cleaved to -homoserine, a non-protein amino acid of great importance in the formation of a host of essential amino acids. In this way, the third nitrogen atom of canavanine enters into the reactions of nitrogen metabolism of the plant. As homoserine, its carbon skeleton also finds an important use.
Canavanine -(+)-("S")-Canavanine is a non-proteinogenic amino acid found in certain leguminous plants. It is structurally related to the proteinogenic α-amino acid -arginine, the sole difference being the replacement of a methylene bridge (-- 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 -canaline). The mechanism of canavanine's toxicity is that organisms that consume it typically mistakenly incorporate it into their own proteins in place of -arginine, thereby producing structurally aberrant proteins that may not function properly.
Canavanine Some specialized herbivores tolerate -canavanine either because they metabolize it efficiently (cf. -canaline) or avoid its incorporation into their own nascent proteins. An example of this ability can be found in the larvae of the tobacco budworm "Heliothis virescens", which can tolerate massive amounts of dietary canavanine. These larvae fastidiously avoid incorporation of -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 -arginine and -canavanine have shown that in "Manduca sexta", the ratio of incorporation is about 3 to 1.