Identification of lysine at the active site of human 5-aminolaevulinate dehydratase

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Abstract
1. Reduction of human 5-aminolevulinate dehydratase with NaBH4 in the presence of 14C-labelled substrate led to complete loss of catalytic activity and to incorporation of label into the enzyme protein. 2. By comparison with authentic lysyl-aminolaevulinic acid, prepared chemically, the modified active-site amino acid obtained by acid hydrolysis was shown to be lysine. 3. Sequencing of a CNBr-cleavage peptide isolated from the inactivated 14C-labeled enzyme revealed that the lysine was present within the sequence M-V-K-P-G-M.