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. 2014 Feb 15;70(Pt 3):744–751. doi: 10.1107/S139900471303294X

Figure 2.

Figure 2

The dipyrromethane cofactor of porphobilinogen deaminase is covalently attached to the enzyme by a thioether bond to a cysteine residue. Four substrate pyrroles are added linearly to the cofactor; finally, hydrolysis of the linkage between the substrate and the cofactor releases the tetrapyrrole product hydroxymethylbilane.