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Evidence for folate‐salvage reactions in plants
Author(s) -
Orsomando Giuseppe,
Bozzo Gale G.,
Garza Rocío Díaz,
Basset Gilles J.,
Quinlivan Eoin P.,
Naponelli Valeria,
Rébeillé Fabrice,
Ravanel Stéphane,
Gregory Jesse F.,
Hanson Andrew D.
Publication year - 2006
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2006.02685.x
Subject(s) - pterin , biochemistry , pisum , biology , arabidopsis thaliana , chemistry , enzyme , cofactor , mutant , gene
Summary Folates in vivo undergo oxidative cleavage, giving pterin and p ‐aminobenzoylglutamate ( p ABAGlu) moieties. These breakdown products are excreted in animals, but their fate is unclear in microorganisms and unknown in plants. As indirect evidence from this and previous studies strongly suggests that plants can have high folate‐breakdown rates (approximately 10% per day), salvage of the cleavage products seems likely. Four sets of observations support this possibility. First, cleavage products do not normally accumulate: pools of p ABAGlu (including its polyglutamyl forms) are equivalent to, at most, 4–14% of typical total folate pools in Arabidopsis thaliana , Lycopersicon esculentum and Pisum sativum tissues. Pools of the pterin oxidation end‐product pterin‐6‐carboxylate are, likewise, fairly small (3–37%) relative to total folate pools. Second, little p ABAGlu built up in A. thaliana plantlets when net folate breakdown was induced by blocking folate synthesis with sulfanilamide. Third, A. thaliana and L. esculentum tissues readily converted supplied breakdown products to folate synthesis precursors: p ABAGlu was hydrolysed to p ‐aminobenzoate and glutamate, and dihydropterin‐6‐aldehyde was reduced to 6‐hydroxymethyldihydropterin. Fourth, both these reactions were detected in vitro ; the reduction used NADPH as cofactor. An alternative salvage route for p ABAGlu, direct reincorporation into dihydrofolate via the action of dihydropteroate synthase, appears implausible from the properties of this enzyme. We conclude that plants are excellent organisms in which to explore the biochemistry of folate salvage.

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