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. 1986 Jun 1;236(2):447–451. doi: 10.1042/bj2360447

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

P N Gibbs, P M Jordan
PMCID: PMC1146860  PMID: 3092810

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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