Dimethylformamidase with a Unique Iron Center

Abstract

N, N ‐Dimethylformamide is an abundant and one of the most used solvents in the chemical industry. The enzyme dimethylformamidase catalyzes the hydrolytic cleavage of the highly stable formamide bond. Sequence analysis of the enzyme suggested that it does not belong to the known family of amidohydrolases. The enzyme in its smallest form, is a tetramer made of two large and two small subunits. It is a very halotolerant enzyme that oligomerizes to form a dimer of tetramers with increasing salt concentration. The domain that contains the active site is a new fold. The active site is a Fe(III) center coordinated by two tyrosines and glutamic acid. Site‐directed mutagenesis shows that glutamic acid, histidine, and asparagine around the active site are critical for the catalysis by the enzyme. The evolution of the enzyme to break down the man‐made dimethylformamide is still a mystery.