peptide deformylase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: formyl-L-methionyl peptide + H2O = formate + methionyl peptide. [EC:3.5.1.88, GOC:jl]

Peptide deformylase activity is a crucial enzymatic function involved in the maturation of newly synthesized proteins in bacteria. It catalyzes the removal of the N-formyl group from the N-terminal methionine residue of nascent polypeptides. This step is essential for proper protein folding and function. The formyl group, attached during translation initiation, can interfere with interactions between the nascent polypeptide and chaperones, as well as hinder subsequent processing events like N-terminal acetylation. Peptide deformylase enzymes are highly conserved across bacteria and are essential for their survival. They are recognized as potential targets for antimicrobial drug development. The active site of these enzymes typically contains a zinc ion, which plays a crucial role in the catalytic mechanism. The enzyme binds to the N-formylmethionine substrate, and through a series of steps involving the zinc ion and a conserved glutamate residue, the formyl group is removed and released as formate. This reaction is crucial for bacterial protein synthesis and is a key target for antibacterial drugs.'
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Proteins (1)

Compounds (2)