catalog number :
MBS1250406
products type :
Recombinant Protein
products full name :
Recombinant Staphylococcus aureus Enterotoxin type E (entE)
products short name :
[Enterotoxin type E (entE)]
products name syn :
[Polypeptide deformylase]
other names :
[peptide deformylase; Peptide deformylase; peptide deformylase; Polypeptide deformylase]
products gene name :
[entE]
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 :
[2-169aa; Full Length of Mature Protein]
sequence :
SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMY
AEEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELL
EKSGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKP
FELEADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQ
KVEKLDRLKARA
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
image1 heading :
SDS-Page
other info2 :
Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to support@mybiosource.com for more details.
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 acc num :
NP_417745.1
ncbi gb acc num :
NC_000913.3
ncbi mol weight :
35.19kD
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].
uniprot summary :
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.