Peptide deformylase
Details
- Name
- Peptide deformylase
- Synonyms
- 3.5.1.88
- fms
- Polypeptide deformylase
- Gene Name
- def
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011040|Peptide deformylase MSVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYAEEGIGLAATQVDIHQRIIV IDVSENRDERLVLINPELLEKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFE LEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEKLDRLKARA
- Number of residues
- 169
- Molecular Weight
- 19328.23
- Theoretical pI
- 5.0
- GO Classification
- Functionsferrous iron binding / hydrolase activity / peptide deformylase activity / ribosome binding / zinc ion bindingProcessesco-translational protein modification / N-terminal protein amino acid modification / translationComponentscytosol
- General Function
- Zinc ion binding
- Specific Function
- 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.
- Pfam Domain Function
- Pep_deformylase (PF01327)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011041|Peptide deformylase (def) ATGTCAGTTTTGCAAGTGTTACATATTCCGGACGAGCGGCTTCGCAAAGTTGCTAAACCG GTAGAAGAAGTGAATGCAGAAATTCAGCGTATCGTCGATGATATGTTCGAGACGATGTAC GCAGAAGAAGGTATTGGCCTGGCGGCAACCCAGGTTGATATCCATCAACGTATCATTGTT ATTGATGTTTCGGAAAACCGTGACGAACGGCTAGTGTTAATCAATCCAGAGCTTTTAGAA AAAAGCGGCGAAACAGGCATTGAAGAAGGTTGCCTGTCGATCCCTGAACAACGTGCTTTA GTGCCGCGCGCAGAGAAAGTTAAAATTCGCGCCCTTGACCGCGACGGTAAACCATTTGAA CTGGAAGCAGACGGTCTGTTAGCCATCTGTATTCAGCATGAGATGGATCACCTGGTCGGC AAACTGTTTATGGATTATCTGTCACCGCTGAAACAACAACGTATTCGTCAGAAAGTTGAA AAACTGGATCGTCTGAAAGCCCGGGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6K3 UniProtKB Entry Name DEF_ECOLI GenBank Protein ID 471304 GenBank Gene ID X77800 - General References
- Mazel D, Pochet S, Marliere P: Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 1994 Feb 15;13(4):914-23. [Article]
- Guillon JM, Mechulam Y, Schmitter JM, Blanquet S, Fayat G: Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli. J Bacteriol. 1992 Jul;174(13):4294-301. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Meinnel T, Guillon JM, Mechulam Y, Blanquet S: The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control. J Bacteriol. 1993 Feb;175(4):993-1000. [Article]
- Meinnel T, Blanquet S: Enzymatic properties of Escherichia coli peptide deformylase. J Bacteriol. 1995 Apr;177(7):1883-7. [Article]
- Groche D, Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF: Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem Biophys Res Commun. 1998 May 19;246(2):342-6. [Article]
- Meinnel T, Blanquet S, Dardel F: A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase. J Mol Biol. 1996 Sep 27;262(3):375-86. [Article]
- Dardel F, Ragusa S, Lazennec C, Blanquet S, Meinnel T: Solution structure of nickel-peptide deformylase. J Mol Biol. 1998 Jul 17;280(3):501-13. [Article]
- Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D: Crystal structure of the Escherichia coli peptide deformylase. Biochemistry. 1997 Nov 11;36(45):13904-9. [Article]
- Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF: Structure of peptide deformylase and identification of the substrate binding site. J Biol Chem. 1998 May 8;273(19):11413-6. [Article]
- Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF: Iron center, substrate recognition and mechanism of peptide deformylase. Nat Struct Biol. 1998 Dec;5(12):1053-8. [Article]
- Hao B, Gong W, Rajagopalan PT, Zhou Y, Pei D, Chan MK: Structural basis for the design of antibiotics targeting peptide deformylase. Biochemistry. 1999 Apr 13;38(15):4712-9. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01942 Formic acid experimental, investigational unknown Details DB02276 (S)-2-(Phosphonoxy)Caproyl-L-Leucyl-P-Nitroanilide experimental unknown Details DB04310 2-[(Formyl-Hydroxy-Amino)-Methyl]-Heptanoic Acid [1-(2-Hydroxymethyl-Pyrrolidine-1-Carbonyl)-2-Methyl-Propyl]-Amide experimental unknown Details DB04368 Bb-3497 experimental unknown Details DB08523 [HYDROXY(3-PHENYLPROPYL)AMINO]METHANOL experimental unknown Details