User:Jiri.kubicek22/sandbox

In enzymology, a peptide deformylase is an enzyme which removes the formyl group from the N terminus of nascent polypeptide chains in eubacteria. The fact, that in human bodies are not peptide deformylases active makes peptide deformylases unique enzymes for targeting antibiotics. That's why in these days many scientists are focusing on discovering inhibitor of peptide deformylases. Peptide deformylases are metaloenzymes, which means, that in active sites of peptide deformylases are metals. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain

Function
Peptide deformylase removes formyl group, which is present in N terminus of nascent polypeptide. The function of peptide deformylase could be described by the following equation, where formyl-L-methionyl peptide and H2O react under the formation of formate and methionyl peptide:


 * H2O + formyl-L-methionyl peptide $$\rightleftharpoons$$ methionyl peptide + formate



This reaction takes place on surface of the ribosome to which is peptide deformylase directly bounded. The way how peptide deformylases bound on ribosom is not certainly clear yet.

For its function this enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formyl-L-methionyl peptide amidohydrolase.

Structural studies
As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and.