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pubmed:abstractText |
Reduction of human 5-aminolaevulinate 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. By comparison with authentic lysyl-aminolaevulinic acid, prepared chemically, the modified active-site amino acid obtained by acid hydrolysis was shown to be lysine. Sequencing of a CNBr-cleavage peptide isolated from the inactivated 14C-labelled enzyme revealed that the lysine was present within the sequence M-V-K-P-G-M.
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