A. Wingler et al., Photorespiratory metabolism of glyoxylate and formate in glycine-accumulating mutants of barley and Amaranthus edulis, PLANTA, 207(4), 1999, pp. 518-526
Glycine-accumulating mutants of barley (Hordeum vulgare L.) and Amaranthus
edulis (Speg.), which lack the ability to decarboxylate glycine by glycine
decarboxylase (GDC; EC 2.1.2.10, were used to study the significance of an
alternative photorespiratory pathway of serine formation. In the normal pho
torespiratory pathway, 5,10-methylenetetrahydrofolate is formed in the reac
tion catalysed by GDC and transferred to serine by serine hydroxymethyltran
sferase. In an alternative pathway, glyoxylate could be decarboxylated to f
ormate and formate could be converted into 5,10-methylenetetrahydrofolate i
n the Cl-tetrahydrofolate synthase pathway. In contrast to wild-type plants
, the mutants showed a light-dependent accumulation of glyoxylate and forma
te, which was suppressed by elevated (0.7%) CO2 concentrations. After growt
h in air, the activity and amount of 10-formyltetrahydrofolate synthetase (
FTHF synthetase; EC 6.3.4.4), the first enzyme of the conversion of formate
into 5,10-methylenetetrahydrofolate, were increased in the mutants compare
d to the wild types. A similar increase in FTHF synthetase could be induced
by incubating leaves of wild-type plants with glycine under illumination,
but not in the dark. Experiments with C-14 showed that the barley mutants i
ncorporated [C-14]formate and [2-C-14]glycollate into serine. Together, the
accumulation of glyoxylate and formate under photorespiratory conditions,
the increase in FTHF synthetase and the ability to utilise formate and glyc
ollate for the formation of serine indicate that the mutants are able parti
ally to compensate for the lack of GDC activity by bypassing the normal pho
torespiratory pathway.