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- W4386094120 abstract "Abstract Metabolism and biological functions of the nitrogen-rich compound guanidine have long been neglected. The discovery of four classes of guanidine-sensing riboswitches and two pathways for guanidine degradation in bacteria hint at hitherto overlooked but widespread sources of unconjugated guanidine in nature. So far, only three enzymes from a narrow range of bacteria and fungi have been shown to produce guanidine, with the ethylene-forming enzyme as the most prominent example. Here, we show that a related class of Fe 2+ - and 2-oxoglutarate-dependent dioxygenases (2-ODD-C23) highly conserved among plants and algae catalyze the hydroxylation of homoarginine at the C6-position. Spontaneous decay of 6-hydroxyhomoarginine yields guanidine and 2-aminoadipate-6-semialdehyde. The latter can be reduced to pipecolate by pyrroline-5-carboxylate reductase but is more likely to be oxidized to aminoadipate by aldehyde dehydrogenase ALDH7B in vivo . Arabidopsis has three 2-ODD-C23 isoforms, among which Din11 is unusual because it also accepted arginine as substrate, which was not the case for the other 2-ODD-C23 isoforms from Arabidopsis or other plants. Guanidine contents were typically between 10 and 20 nmol*(g fresh weight) -1 in Arabidopsis but increased to 100 or 300 nmol*(g fresh weight) -1 after homoarginine feeding or treatment with Din11-inducing methyljasmonate, respectively. In 2-ODD-C23 triple mutants, the guanidine content was strongly reduced, whereas it increased in overexpression plants. We discuss the implications of the finding of widespread guanidine-producing enzymes in photosynthetic eukaryotes as a so far underestimated branch of the bio-geochemical nitrogen cycle and propose possible functions of natural guanidine production." @default.
- W4386094120 created "2023-08-24" @default.
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- W4386094120 date "2023-08-22" @default.
- W4386094120 modified "2023-09-26" @default.
- W4386094120 title "Guanidine Production by Plant Homoarginine-6-hydroxylases" @default.
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- W4386094120 doi "https://doi.org/10.1101/2023.08.22.554250" @default.
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