Recombinant Escherichia coli Peptide deformylase | MyBioSource MBS1238309 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Escherichia coli Peptide deformylase

catalog :

MBS1238309

quantity :

0.05 mg (E-Coli)

price :

185 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS1238309

products type :

Recombinant Protein

products full name :

Recombinant Escherichia coli Peptide deformylase

products short name :

Peptide deformylase

products name syn :

Polypeptide deformylase

other names :

peptide deformylase; Peptide deformylase; peptide deformylase; Polypeptide deformylase

products gene name :

def

other gene names :

def; def; ECK3273; fms; JW3248; fms; PDF

uniprot entry name :

DEF_ECOLI

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

2-169

sequence length :

169

sequence :

SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMY
AEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELL
EKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKP
FELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQ
KVEKLDRLKARA

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products description :

Roves 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.

products references :

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)

ncbi gi num :

16131166

ncbi acc num :

NP_417745.1

ncbi gb acc num :

NC_000913.3

uniprot acc num :

P0A6K3

ncbi mol weight :

35.2kD

ncbi summary :

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].

size1 :

0.05 mg (E-Coli)

price1 :

185 USD

size2 :

0.2 mg (E-Coli)

price2 :

420

size3 :

0.5 mg (E-Coli)

price3 :

680

size4 :

1 mg (E-Coli)

price4 :

1070

more info or order :

MyBioSource product webpage