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Extraction And Partial Characterization Of The Glycine Decarboxylase Multienzyme Complex From Pea Leaf Mitochondria, G. Sarojini, David J. Oliver

David J. Oliver

Glycine decarboxylase has been successfully solubilized from pea (Pisum sativum) leaf mitochondria as an acetone powder. The enzyme was dependent on added dithiothreitol and pyridoxal phosphate for maximal activity. The enzyme preparation could catalyze the exchange of CO2 into the carboxyl carbon of glycine, the reverse of the glycine decarboxylase reaction by converting serine, NH4+, and CO2 into glycine, and 14CO2 release from [1-14C]glycine. The half-maximal concentrations for the glycine-bicarbonate exchange reaction were 1.7 millimolar glycine, 16 millimolar NaH14CO2, and 0.006 millimolar pyridoxal phosphate. The enzyme (glycine-bicarbonate exchange reaction) was active in the assay conditions for 1 hour and could …