EC 3.5.1.88 - Peptide deformylase

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IntEnz Enzyme Nomenclature
EC 3.5.1.88

Names

Accepted name:
peptide deformylase
Systematic name:
formyl-L-methionyl peptide amidohydrolase

Reaction

Cofactor

Comments:

Requires Fe(II). Also requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Differs in substrate specifity from EC 3.5.1.27 (N-formylmethionylaminoacyl-tRNA deformylase) and EC 3.5.1.31 (formylmethionine demethylase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0042586
UniProtKB/Swiss-Prot: (471) [show] [UniProt]

References

  1. Adams, J.M.
    On the release of the formyl group from nascent protein.
    J. Mol. Biol. 33: 571-589 (1968). [PMID: 4973445]
  2. Mazel, D., Pochet, S. and Marliere, P.
    Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation.
    EMBO J. 13: 914-923 (1994). [PMID: 8112305]
  3. Chan, M.K., Gong, W., Rajagopalan, P.T.R., Hao, B., Tsai, C.M. and Pei, D.
    Crystal structure of the Escherichia coli peptide deformylase.
    Biochemistry 36: 13904-13909 (1997). [PMID: 9374869]
  4. Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V.
    Structure of peptide deformylase and identification of the substrate binding site.
    J. Biol. Chem. 273: 11413-11416 (1998). [PMID: 9565550]
  5. Becker, A., Schlichting, I., Kabsch, W., Groche, D., Schultz, S. and Wagner, A.F.
    Iron center, substrate recognition, and mechanism of peptide deformylase.
    Nat. Struct. Biol. 5: 1053-1058 (1998). [PMID: 9846875]
  6. Rajagopalan, P.T.R., Yu, X.C. and Pei, D.
    Peptide deformylase: a new type of mononuclear iron protein.
    J. Am. Chem. Soc. 119: 12418-12419 (1997).
  7. Groche, D., Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A.F.V.
    Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site.
    Biochem. Biophys. Res. Commun. 246: 342-346 (1998). [PMID: 9610360]
  8. Rajagopalan, P.T.R., Grimme, S. and Pei, D.
    Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133.
    Biochemistry 39: 779-790 (2000). [PMID: 10651644]
  9. Hu, Y.J., Wei, Y., Zhou, Y., Rajagopalan, P.T.R. and Pei, D.
    Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library.
    Biochemistry 38: 643-650 (1999). [PMID: 9888804]
  10. Ragasu, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T.
    Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin.
    J. Mol. Biol. 289: 1445-1457 (1999). [PMID: 10373378]
  11. Giglione, C., Pierre, M. and Meinnel, T.
    Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents.
    Mol. Microbiol. 36: 1197-1205 (2000). [PMID: 10931273]
  12. Pei, D.
    Peptide deformylase: a target for novel antibiotics?
    Emerging Therapeutic Targets 5: 23-40 (2001).

[EC 3.5.1.88 created 2001]