Peptide deformylase

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In enzymology, a peptide deformylase (Template:EC number) 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.

Function

Peptide deformylase removes the formyl group from the N terminus of nascent polypeptides as they are synthesized by the ribosome. The function of peptide deformylase can be described by the following equation, where formyl-L-methionyl peptide and water react under the formation of formate and methionyl peptide:

H2O + formyl-L-methionyl peptide methionyl peptide + formate
Activity of peptide deformylase
Activity of peptide deformylase

This reaction takes place on the surface of the ribosome, where the C-terminal alpha-helix of the peptide deformylase interacts with a grove between ribosomal proteins uL22 and bL32, and rRNA.[3]

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 Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, Template:PDB link, and Template:PDB link.

See also

References

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Further reading

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