Purification and primary amino acid sequence of the L subunit of glycine decarboxylase. Evidence for a single lipoamide dehydrogenase in plant mitochondria.

摘要: Abstract In order to purify the lipoamide dehydrogenase associated with glycine decarboxylase complex of pea leaf mitochondria, activity free has been separated from those pyruvate and 2-oxoglutarate complexes under conditions in which dissociates into its component subunits. This is normally further purified N-terminal amino acid sequence determined. Positive cDNA clones isolated both a embryo lambda gt11 expression library using an antibody raised against proved be product single gene. The deduced open reading frame included matching that determined directly N terminus mature protein. shows good homology Escherichia coli, yeast, humans. corresponding mRNA strongly light-induced etiolated seedlings leaves plants following period darkness. evidence suggests mitochondrial enzyme complexes: dehydrogenase, all use same subunit.