Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Isolation and sequence of a peptide containing an essential lysine

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Abstract
Interaction of glucose-6-phosphate dehydrogenase from L. mesenteroides with pyridoxal 5''-phosphate and sodium borohydride leads to inactivation and modification of 2 lysine residues per enzyme dimer that are thought to bind G-6-P (Milhausen, M., and Levy, H. R., 1975). The amino acid sequence surrouding this lysine residue is reported. Following tryptic hydrolysis of the modified enzyme, 2 peptides, each containing 2 pyridoxyllysine residue, were purified to homogeneity and subjected to automated Edman degradation. The sequences revealed that one of these, a heptapeptide, was derived from the other, containing 11 amino acids. End-group analysis of the native enzyme reveals that valine is the N-terminal and glycine the C-terminal amino acid and provides support for the identity of the enzyme''s 2 subunits.