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

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...

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Bibliographic Details
Published in:FEBS letters 1987-12, Vol.225 (1), p.87-92
Main Authors: Jordan, Peter M., Warren, Martin J.
Format: Article
Language:English
Subjects:
Ammonia-Lyases - metabolism
Analytical, structural and metabolic biochemistry
Benzaldehydes
Binding Sites
Biological and medical sciences
Catalysis
Chemical Phenomena
Chemistry
Chromatography, High Pressure Liquid
dipyrromethane
Dipyrromethane cofactor
E. coli
Enzyme intermediate complex
Enzymes and enzyme inhibitors
Escherichia coli
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydroxymethylbilane Synthase - metabolism
Indicators and Reagents
Lyases
Porphobilinogen - metabolism
Porphobilinogen deaminase
Porphyrins - metabolism
Pyrroles - metabolism
Spectrophotometry
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)81136-5