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Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase
Author(s) -
Jordan Peter M.,
Warren Martin J.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81136-5
Subject(s) - porphobilinogen deaminase , chemistry , catalysis , porphobilinogen , cofactor , biochemistry , enzyme , heme
Porphobilinogen deaminase isolated from Escherichia coli is shown to contain a dipyrromethane cofactor (DPMC) linked covalently to the enzyme. The structure of the cofactor is proposed on the basis of its reaction with Ehrlich's reagent and from its chemical properties. The cofactor is involved in the binding of intermediates during the catalytic reaction but is not incorporated into the product preuroporphyrinogen, E. coli strains containing the cloned porphobilinogen deaminase gene ( hemC ) when grown on 5‐amino[ 14 C]‐levulinic acid incorporate 14 C radioactivity specifically into the dipyrromethane cofactor of porphobilinogen deaminase.