Decarboxylation of glycine contributes to carbon isotope fractionation in photosynthetic organisms.
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Igamberdiev AU, Ivlev AA, Bykova NV, Threlkeld CN, Lea PJ, Gardestrom P
Decarboxylation of glycine contributes to carbon isotope fractionation in photosynthetic organisms.
Photosynth Res. 2001;67(3):177-84.
- PubMed ID
- 16228305 [ View in PubMed]
- Abstract
Carbon isotope effects were investigated for the reaction catalyzed by the glycine decarboxylase complex (GDC; EC 2.1.2.10). Mitochondria isolated from leaves of pea (Pisum sativum L.) and spinach (Spinacia oleracea L.) were incubated with glycine, and the CO(2) evolved was analyzed for the carbon isotope ratio (delta(13)C). Within the range of parameters tested (temperature, pH, combination of cofactors NAD(+), ADP, pyridoxal 5-phosphate), carbon isotope shifts of CO(2) relative to the C(1)-carboxyl carbon of glycine varied from +14 per thousand to -7 per thousand. The maximum effect of cofactors was observed for NAD(+), the removal of which resulted in a strong (12)C enrichment of the CO(2) evolved. This indicates the possibility of isotope effects with both positive and negative signs in the GDC reaction. The measurement of delta(13)C in the leaves of the GDC-deficient barley (Hordeum vulgare L.) mutant (LaPr 87/30) plants indicated that photorespiratory carbon isotope fractionation, opposite in sign when compared to the carbon isotope effect during CO(2) photoassimilation, takes place in vivo. Thus the key reaction of photorespiration catalyzed by GDC, together with the key reaction of CO(2) fixation catalyzed by ribulose-1,5-bisphosphate carboxylase, both contribute to carbon isotope fractionation in photosynthesis.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Pyridoxal phosphate Glycine dehydrogenase [decarboxylating], mitochondrial Protein Humans UnknownCofactorDetails