Identification of a cysteine residue as the binding site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase

FEBS Letters

Williams, Howard J.²  Warren, Martin J.¹  Grant, Stephen K.²  Scott, A.Ian²  Jordan, Peter M.¹  Roessner, Charles A.²  Stolowich, Neal J.² 

[1] Department of Biochemistry, University of Southampton, Southampton SO9 3TU, England;Department of Chemistry, Texas A&M University, College Station, TX 77843-3255, USA

关键词: Porphobilinogen deaminase;    Dipyrromethane cofactor;    Cysteine;    13C-NMR;    (E. coli);   

DOI  :  10.1016/0014-5793(88)81260-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase was specifically labelled with ¹³C by growth of the bacteria in the presence of 5-amino[5-¹³C]levulinic acid. Using ¹³C-NMR spectroscopy, the structure of the cofactor was confirmed as a dipyrromethane made up of two linked pyrrole rings each derived from porphobilinogen. The chemical shift data indicate that one of the pyrrole rings of the cofactor is covalently linked to the deaminase enzyme through a cysteine residue. Evidence from protein chemistry studies suggest that cysteine-242 is the covalent binding site for the cofactor.

【 授权许可】

Unknown