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Literature summary for 4.2.1.24 extracted from

  • Shoolingin-Jordan, P.M.; Spencer, P.; Sarwar, M.; Erskine, P.E.; Cheung, K.M.; Cooper, J.B.; Norton, E.B.
    5-Aminolaevulinic acid dehydratase: metals, mutants and mechanism (2002), Biochem. Soc. Trans., 30, 584-590.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K195A mutant enzyme with only 0.1% of the wild-type activity Escherichia coli
K195C mutant enzyme with only 0.1% of the wild-type activity, 2-bromethylamine results in recovery of 10% of the wild-type activity Escherichia coli
K247A inactive mutant enzyme Escherichia coli
K247C inactive mutant enzyme, 2-bromethylamine results in recovery of 6% of the wild-type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5-chlorolevulinic acid inactivation results fromthe initial formation of a Schiff base with lysine-247, followed by alkylation of lysine-195 by the resulting reactive chloroimide Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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