Peptide deformylase
| Peptide deformylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Escherichia coli peptide deformylase structure | |||||||||
| Identifiers | |||||||||
| EC no. | 3.5.1.88 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
Peptide deformylases are metaloenzymes monomers and bind a metal cofactor, typically Fe(II) or Zn, in an active site. Cofactor identity impacts catalytic efficiency.
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.