The pathway of serine synthesis was investigated in six species of cya
nobacteria: Anabaena cylindrica, A. variabilis, A. flos-aquae, Coccoch
loris peniocystis, Gleocapsa alpicola and Phormidium molle. Activity o
f the enzymes phosphoglycerate (PGA) dehydrogenase (EC 1.1.1.95), phos
phoserine transaminase (EC 2.6.1.52) and phosphoserine phosphatase (EC
3.1.3.3) was detected in vitro in all species, but no PGA phosphatase
(EC 3.1.3.20) or hydroxypyruvate reductase (EC 1.1.1.26) activity cou
ld be detected. Metabolism of [1-C-14]PGA by cell-free extracts of C.
peniocystis resulted in the labelling of serine, alanine and aspartate
, which represented 84, 11 and 4% of the labelled amino acid pool, res
pectively. Labelled serine isolated from these experiments was 100% ca
rboxyl-labelled indicating that it was formed directly from PGA. The l
abelling of serine was markedly reduced by 5 mM phosphoserine. These i
n vitro findings indicate that cyanobacteria are capable of synthesizi
ng serine directly from PGA, independent of ribulose-1,5-bisphosphate
oxidation, and that the route of serine synthesis via phosphohydroxypy
ruvate and phosphoserine is the predominant pathway in these organisms
.