G. Tissot et al., PROTEIN BIOTINYLATION IN HIGHER-PLANTS - CHARACTERIZATION OF BIOTIN HOLOCARBOXYLASE SYNTHETASE-ACTIVITY FROM PEA (PISUM-SATIVUM) LEAVES, Biochemical journal, 314, 1996, pp. 391-395
Biotin holocarboxylase synthetase was partially purified from pea leav
es by a sequence of ammonium sulphate fractionation and DEAE 52-cellul
ose chromatography. Enzyme activity was assayed using apo-(biotin carb
oxyl carrier protein) from an Escherichia coli bir A mutant affected i
n biotin holocarboxylase synthetase activity. Conditions for optimal c
atalytic activity and biochemical parameters of the plant enzyme were
determined. This is the first direct evidence of the existence of biot
in holocarboxylase synthetase activity in plants.