Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.
作者： Hideyuki Hayashi , Yasushi Inoue , Seiki Kuramitsu , Yoshimasa Morino , Hiroyuki Kagamiyama
DOI: 10.1016/0006-291X(90)92037-Z
关键词: Site-directed mutagenesis 、 Glycine 、 Phenylalanine 、 Enzyme kinetics 、 Mutagenesis 、 Enzyme 、 Chemistry 、 Escherichia coli 、 Tryptophan 、 Stereochemistry 、 Biochemistry
摘要: Trp140 of E. coli aspartate aminotransferase has been converted to Phe or Gly by site-directed mutagenesis. As compared the wild-type enzyme, either mutant enzymes showed 10- 100-fold increase in Km's for natural dicarboxylic substrates, but did not show appreciable changes aromatic substrates. Teh kcat values and substrates were greatly decreased [Trp140----Gly] mutation, lesser extents [Trp140----Phe] mutation. These findings suggested that N(1) may be essential catalysis, partly involved binding distal carboxylate group
elsevier.com
sci-hub.se 参考文章(11)
Hideyuki Hayashi, Seiki Kuramitsu, Yasushi Inoue, Yoshimasa Morino, Hiroyuki Kagamiyama, [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids. Biochemical and Biophysical Research Communications. ,vol. 159, pp. 337- 342 ,(1989) , 10.1016/0006-291X(89)92443-1
Shigehiro Kamitori, Ken Hirotsu, Taiichi Higuchi, Kiyoshi Kondo, Katsura Inoue, Seiki Kuramitsu, Hiroyuki Kagamiyama, Yoshiki Higuchi, Noritake Yasuoka, Masami Kusunoki, Yoshiki Matsuura, Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution. Journal of Biochemistry. ,vol. 104, pp. 317- 318 ,(1988) , 10.1093/OXFORDJOURNALS.JBCHEM.A122464
Y Inoue, S Kuramitsu, K Inoue, H Kagamiyama, K Hiromi, S Tanase, Y Morino, Substitution of a lysyl residue for arginine 386 of Escherichia coli aspartate aminotransferase. Journal of Biological Chemistry. ,vol. 264, pp. 9673- 9681 ,(1989) , 10.1016/S0021-9258(18)60583-6
E Sandmeier, P Christen, Chemical modification of a functional arginyl residue (Arg 292) of mitochondrial aspartate aminotransferase. Identification as the binding site for the distal carboxylate group of the substrate. Journal of Biological Chemistry. ,vol. 257, pp. 6745- 6750 ,(1982) , 10.1016/S0021-9258(18)34493-4
N. Yasuoka, M. Kusunoki, Y. Matsuura, S. Kamitori, K. Hirotsu, T. Higuchi, K. Kondo, K. Inoue, S. Kuramitsu, H. Kagamiyama, Y. Higuchi, Overproduction and preliminary X-ray characterization of aspartate aminotransferase from Escherichia coli. Journal of Biochemistry. ,vol. 101, pp. 813- 816 ,(1987) , 10.1093/JB/101.3.813
Toshiharu Yagi, Hiroyuki Kagamiyama, Kenzo Motosugi, Mitsuhiro Nozaki, Kenji Soda, Crystallization and properties of aspartate aminotransferase from escherichia coli
B FEBS Letters. ,vol. 100, pp. 81- 84 ,(1979) , 10.1016/0014-5793(79)81135-7
Johan N. Jansonius, Heinz Gehring, Philipp Christen, Jack F. Kirsch, Gregor Eichele, Geoffrey C. Ford, Michael G. Vincent, Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. Journal of Molecular Biology. ,vol. 174, pp. 497- 525 ,(1984) , 10.1016/0022-2836(84)90333-4
Ciaran N. Cronin, Jack F. Kirsch, Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry. ,vol. 27, pp. 4572- 4579 ,(1988) , 10.1021/BI00412A052
Celeste Yanisch-Perron, Jeffrey Vieira, Joachim Messing, Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors Gene. ,vol. 33, pp. 103- 119 ,(1985) , 10.1016/0378-1119(85)90120-9
Joachim Messing, Roberto Crea, Peter H. Seeburg, A system for shotgun DNA sequencing. Nucleic Acids Research. ,vol. 9, pp. 309- 321 ,(1981) , 10.1093/NAR/9.2.309