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Biochemistry|October 17, 1995
Fructose-1,6-bisphosphatase: arginine-22 is involved in stabilization of the T allosteric stateG Lu, M K Williams, E L Giroux, et al.The Journal of Biological Chemistry|October 7, 1994
Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interfaceD P Baker, J W Stebbins, E DeSena, et al.Proceedings of the National Academy of Sciences of the United States of America|January 1, 1977
Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylaseE R Kantrowitz, L B Jacobsberg, S M Landfear, et al.Bioresource Technology|May 3, 2001
The effect of supplementation by different nitrogen sources on the production of lactic acid from date juice by Lactobacillus casei subsp. rhamnosusN Nancib, A Nancib, A Boudjelal, et al.The Journal of Biological Chemistry|October 15, 1989
Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chainF C Wedler, Y C Hsuanyu, E R Kantrowitz, et al.Biochemistry|August 5, 2000
Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatasesK M Holtz, I E Catrina, A C Hengge, et al.The Journal of Biological Chemistry|November 22, 1996
Engineered complementation in Escherichia coli aspartate transcarbamoylase. Heterotropic regulation by quaternary structure stabilizationJ M Aucoin, E J Pishko, D P Baker, et al.Journal of Molecular Biology|August 25, 1983
Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutionsR S Silver, J P Daigneault, P D Teague, et al.Journal of Molecular Biology|May 23, 1998
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102B Stec, M J Hehir, C Brennan, et al.Biochemistry|February 21, 1989
Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanismJ E Gouaux, W N Lipscomb, S A Middleton, et al.Pageof 14