Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts(340 views) Castellano I, Di Salle A, Merlino A, Rossi M, La Cara F
CNR, Institute of Protein Biochemistry, via Pietro Castellino 111, 80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy
References: Boanca, G., Sand, A., Barycki, J.J., Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase (2006) J Biol Chem, 281, pp. 19029-1903
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Bryson, K., McGuffin, L.J., Marsden, R.L., Ward, J.J., Sodhi, J.S., Jones, D.T., Protein structure prediction servers at University College London (2005) Nucl Acids Res, 33, pp. W36-W38. , (Web Server issue)
Castellano, I., Merlino, A., Rossi, M., la Cara, F., Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity (2010) Biochimie, 92, pp. 464-474
de Vendittis, E., Castellano, I., Cotugno, R., Ruocco, M.R., Raimo, G., Masullo, M., Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition (2008) J Theor Biol, 250, pp. 156-171
Emdin, M., Pompella, A., Paolicchi, A., Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque (2005) Circulation, 112, pp. 2130-2137
Henne, A., Brüggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H.J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Ikeda, Y., Fujii, J., Anderson, M.E., Taniguchi, N., Meister, A., Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase (1995) J Biol Chem, 270, pp. 22223-22228
Jones, T.A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C.L., Poland, P.A., Bruns, J.B., Hughey, R.P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Higgins, D.G., Clustal W and Clustal X version 2.0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L.L., Chou, P.R., Hua, Y.W., Hsu, W.H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Lo, H.F., Ong, P.L., Chang, H.P., Lin, L.L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Minami, H., Suzuki, H., Kumagai, H., A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity (2003) FEMS Microbiol Lett, 224, pp. 169-173
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006) Proc Natl Acad Sci USA, 103, pp. 6471-6476
Pompella, A., Corti, A., Paolicchi, A., Giommarelli, C., Zunino, F., Gamma-glutamyltransferase, redox regulation and cancer drug resistance (2007) Curr Opin Pharmacol, 7, pp. 360-366
Ruepp, A., Graml, W., Santos-Martinez, M.L., Koretke, K.K., Volker, C., Mewes, H.W., Frishman, D., Baumeister, W., The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum (2000) Nature, 407, pp. 508-513
Suzuki, H., Yamada, C., Kato, K., Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase (2007) Amino Acids, 32, pp. 333-340
Szilagyi, A., Zavodsky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey (2000) Struct Fold Des, 8, pp. 493-504
Takami, H., Nakasone, K., Takaki, Y., Maeno, G., Sasaki, R., Masui, N., Fuji, F., Horikoshi, K., Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis (2000) Nucleic Acids Res, 28, pp. 4317-4331
Tate, S.S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
van der Spoel, D., van Druner, R., Berendsen, H.J.C., (1994) GROningen MAchine for Chemical Simulation, , Groningen: Department of Biophysical Chemistry, BIOSON Research Institute
Vermeulen, N., Gänzle, M.G., Vogel, R.F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Wada, K., Irie, M., Suzuki, H., Fukuyama, K., Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket (2010) FEBS J, 277, pp. 1000-1009
White, O., Eisen, J.A., Heidelberg, J.F., Hickey, E.K., Peterson, J.D., Dodson, R.J., Haft, D.H., Fraser, C.M., Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1 (1999) Science, 286, pp. 1571-1577
Wiederstein, M., Sippl, M.J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins (2007) Nucleic Acids Res, 35, pp. 407-410
Willard, L., Ranjan, A., Zhang, H., Monzavi, H., Boyko, R.F., Sykes, B.D., Wishart, D.S., VADAR: a web server for quantitative evaluation of protein structure quality (2003) Nucleic Acids Res, 31, pp. 3316-3319
Williams, K., Cullati, S., Sand, A., Biterova, E.I., Barycki, J.J., Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis (2009) Biochemistry, 48, pp. 2459-2467
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Henne, A., Br ggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H. J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Jones, T. A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C. L., Poland, P. A., Bruns, J. B., Hughey, R. P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Higgins, D. G., Clustal W and Clustal X version 2. 0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L. L., Chou, P. R., Hua, Y. W., Hsu, W. H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R. C., Hu, H. Y., Kuo, L. Y., Lo, H. F., Ong, P. L., Chang, H. P., Lin, L. L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I. K., Thornton, J. M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Tate, S. S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
Vermeulen, N., G nzle, M. G., Vogel, R. F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
No results.
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts