Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase

FEBS Letters

Warren, Martin J.¹  Jordan, Peter M.¹ 

[1] Department of Biochemistry, University of Southampton, Southampton SO9 3TU, England

关键词: Porphobilinogen deaminase;    Dipyrromethane cofactor;    Enzyme intermediate complex;    (E. coli);   

DOI  :  10.1016/0014-5793(87)81136-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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[¹⁴C]-levulinic acid incorporate ¹⁴C radioactivity specifically into the dipyrromethane cofactor of porphobilinogen deaminase.

【 授权许可】

Unknown