In enzymology, a peptide deformylase (EC 3.5.1.88) is an enzyme that removes the formyl group from the N terminus of nascent polypeptide chains in eubacteria, mitochondria and chloroplasts.[1]
Peptide deformylases are metaloenzymes monomers and bind a metal cofactor, typically Fe(II) or Zn, in an active site. Cofactor identity impacts catalytic efficiency.[2]
There are two types of peptide deformylases, types I and II, which differ in structure mainly in the outer surface of the protein.
Human gene PDF (gene) possesses this activity.
^Escobar-Alvarez S, Goldgur Y, Yang G, Ouerfelli O, Li Y, Scheinberg DA (April 2009). "Structure and activity of human mitochondrial peptide deformylase, a novel cancer target". Journal of Molecular Biology. 387 (5): 1211–1228. doi:10.1016/j.jmb.2009.02.032. PMC 2782631. PMID 19236878.
^Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF (May 1998). "Structure of peptide deformylase and identification of the substrate binding site". The Journal of Biological Chemistry. 273 (19): 11413–11416. doi:10.1074/jbc.273.19.11413. PMID 9565550.
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