Canavanine utilization
Journal
RSC chemical biology
ISSN: 2633-0679
Titre abrégé: RSC Chem Biol
Pays: England
ID NLM: 101768727
Informations de publication
Date de publication:
05 Oct 2022
05 Oct 2022
Historique:
received:
24
05
2022
accepted:
18
08
2022
entrez:
2
11
2022
pubmed:
3
11
2022
medline:
3
11
2022
Statut:
epublish
Résumé
Canavanine, the δ-oxa-analogue of arginine, is produced as one of the main nitrogen storage compounds in legume seeds and has repellent properties. Its toxicity originates from incorporation into proteins as well as arginase-mediated hydrolysis to canaline that forms stable oximes with carbonyls. So far no pathway or enzyme has been identified acting specifically on canavanine. Here we report the characterization of a novel PLP-dependent enzyme, canavanine-γ-lyase, that catalyzes the elimination of hydroxyguanidine from canavanine to subsequently yield homoserine. Homoserine-dehydrogenase, aspartate-semialdehyde-dehydrogenase and ammonium-aspartate-lyase activities are also induced for facilitating canavanine utilization. We demonstrate that this novel pathway is found in certain
Identifiants
pubmed: 36320885
doi: 10.1039/d2cb00128d
pii: d2cb00128d
pmc: PMC9533460
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1240-1250Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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