Methionine Aminopeptidase (map) Escherichia Coli Recombinant Protein

Roves the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.

Processing of the initiation methionine from proteins properties of the Escherichia coli methionine aminopeptidase and its gene structure.Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S.J. Bacteriol. 169:751-757(1987) Systematic sequencing of the Escherichia coli genome analysis of the 2.4-4.1 min (110,917-193,643 bp) region.Fujita N., Mori H., Yura T., Ishihama A.Nucleic Acids Res. 22:1637-1639(1994) Sequence of minutes 4-25 of Escherichia coli.Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. 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) Escherichia coli proteome analysis using the gene-protein database.VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.Electrophoresis 18:1243-1251(1997) The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme.D'souza V.M., Holz R.C.Biochemistry 38:11079-11085(1999) Divalent metal binding properties of the methionyl aminopeptidase from Escherichia coli.D'souza V.M., Bennett B., Copik A.J., Holz R.C.Biochemistry 39:3817-3826(2000) Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli.Copik A.J., Swierczek S.I., Lowther W.T., D'souza V.M., Matthews B.W., Holz R.C.Biochemistry 42:6283-6292(2003) Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli.Watterson S.J., Mitra S., Swierczek S.I., Bennett B., Holz R.C.Biochemistry 47:11885-11893(2008) Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.Mitra S., Job K.M., Meng L., Bennett B., Holz R.C.FEBS J. 275:6248-6259(2008) Analysis of the stoichiometric metal activation of methionine aminopeptidase.Chai S.C., Ye Q.Z.BMC Biochem. 10:32-32(2009) Protein N-terminal processing substrate specificity of Escherichia coli and human methionine aminopeptidases.Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.Biochemistry 49:5588-5599(2010) Probing the metal ion selectivity in methionine aminopeptidase via changes in the luminescence properties of the enzyme bound europium ion.Sule N., Singh R.K., Zhao P., Srivastava D.K.J. Inorg. Biochem. 106:84-89(2012) Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli a new type of proteolytic enzyme.Roderick S.L., Mathews B.W.Biochemistry 32:3907-3912(1993) Escherichia coli methionine aminopeptidase implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis.Lowther W.T., Orville A.M., Madden D.T., Lim S., Rich D.H., Matthews B.W.Biochemistry 38:7678-7688(1999) Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.Lowther W.T., Zhang Y., Sampson P.B., Honek J.F., Matthews B.W.Biochemistry 38:14810-14819(1999) Structural basis of catalysis by monometalated methionine aminopeptidase.Ye Q.Z., Xie S.X., Ma Z.Q., Huang M., Hanzlik R.P.Proc. Natl. Acad. Sci. U.S.A. 103:9470-9475(2006) Structural analysis of inhibition of E. coli methionine aminopeptidase implication of loop adaptability in selective inhibition of bacterial enzymes.Ma Z.-Q., Xie S.-X., Huang Q.-Q., Nan F.-J., Hurley T.D., Ye Q.-Z.BMC Struct. Biol. 7:84-84(2007) Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.Evdokimov A.G., Pokross M., Walter R.L., Mekel M., Barnett B.L., Amburgey J., Seibel W.L., Soper S.J., Djung J.F., Fairweather N., Diven C., Rastogi V., Grinius L., Klanke C., Siehnel R., Twinem T., Andrews R., Curnow A.Proteins 66:538-546(2007) Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II) -form selectivity and antibacterial activity.Wang W.-L., Chai S.C., Huang M., He H.-Z., Hurley T.D., Ye Q.-Z.J. Med. Chem. 51:6110-6120(2008)

Small volumes of map recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS1012623 is a recombinant protein targeting map. Also known as Recombinant Escherichia coli Methionine aminopeptidase. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.