NP_417745.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
21.2 kDa
NCBI Official Full Name
peptide deformylase
NCBI Protein Information
peptide deformylase
UniProt Protein Name
Peptide deformylase
UniProt Synonym Protein Names
Polypeptide deformylase
UniProt Synonym Gene Names
UniProt Entry Name
DEF_ECOLI
NCBI Summary for def
The def gene is essential unless the fmt formylase gene is also inactivated. [More information is available at EcoGene: EG11440]. Peptide deformylase releases the formyl group from the amino terminal methionine residue of most nascent proteins . [More information is available at EcoCyc: EG11440].
UniProt Comments for def
Removes the formyl group from the N-terminal Met of newly synthesized proteins. 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.
Product References and Citations for def recombinant protein
Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation.Mazel D., Pochet S., Marliere P.EMBO J. 13:914-923(1994)
Disruption of the gene for Met-tRNA(fMet)
formyltransferase severely impairs growth of Escherichia coli.Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G.J. Bacteriol. 174:4294-4301(1992)
The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997)
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006)
The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet)
formyltransferase, escapes metabolic control.Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S.J. Bacteriol. 175:993-1000(1993)
Enzymatic properties of Escherichia coli peptide deformylase.Meinnel T., Blanquet S.J. Bacteriol. 177:1883-1887(1995)
Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site.Groche D., Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.Biochem. Biophys. Res. Commun. 246:342-346(1998)
A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase.Meinnel T., Blanquet S., Dardel F.J. Mol. Biol. 262:375-386(1996)
Solution structure of nickel-peptide deformylase.Dardel F., Ragusa S., Lazennec C., Blanquet S., Meinnel T.J. Mol. Biol. 280:501-513(1998)
Crystal structure of the Escherichia coli peptide deformylase.Chan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.Biochemistry 36:13904-13909(1997)
ErratumChan M.K., Gong W., Rajagopalan P.T.R., Hao B., Tsai C.M., Pei D.Biochemistry 37:13042-13042(1998)
Structure of peptide deformylase and identification of the substrate binding site.Becker A., Schlichting I., Kabsch W., Schultz S., Wagner A.F.J. Biol. Chem. 273:11413-11416(1998)
Iron center, substrate recognition and mechanism of peptide deformylase.Becker A., Schlichting I., Kabsch W., Groche D., Schultz S., Wagner A.F.Nat. Struct. Biol. 5:1053-1058(1998)
Structural basis for the design of antibiotics targeting peptide deformylase.Hao B., Gong W., Rajagopalan P.T.R., Zhou Y., Pei D., Chan M.K.Biochemistry 38:4712-4719(1999)
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Products associated with def recombinant protein
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