Mechanism of adenylate kinase. Demonstration of a functional relationship between Aspartate 93 and Mg2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR. Export

@article{Yan91, abstract = {Earlier magnetic resonance studies suggested no direct interaction between Mg2+ ions and adenylate kinase (AK) in the AK.MgATP (adenosine 5'-triphosphate) complex. However, recent NMR studies concluded that the carboxylate of aspartate 119 accepts a hydrogen bond from a water ligand of the bound Mg2+ ion in the muscle AK.MgATP complex [Fry, D.C., Kuby, S.A., \& Mildvan, A.S. (1985) Biochemistry 24, 4680-4694]. On the other hand, in the 2.6-A crystal structure of the yeast AK.MgAP5A [P1,P5-bis(5'-adenosyl)pentaphosphate] complex, the Mg2+ ion is in proximity to aspartate 93 [Egner, U., Tomasselli, A.G., \& Schulz, G.E. (1987) J. Mol. Biol. 195, 649-658]. Substitution of Asp-93 with alanine resulted in no change in dissociation constants, 4-fold increases in Km, and a 650-fold decrease in kcat. Notable changes have been observed in the chemical shifts of the aromatic protons of histidine 36 and a few other aromatic residues. Ho...}, address = {Department of Chemistry, Ohio State University, Columbus 43210.}, author = {Yan, H. G. and Tsai, M. D.}, citeulike-article-id = {388925}, editor = {1991/06/04}, journal = {Biochemistry}, keywords = {asp, enzyme, kinase, mechanism, nmr}, number = {22}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {Mechanism of adenylate kinase. Demonstration of a functional relationship between Aspartate 93 and Mg2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR.}, volume = {30}, year = {1991} }

TY - JOUR ID - Yan91 L3 - citeulike-article-id:388925 N2 - Earlier magnetic resonance studies suggested no direct interaction between Mg2+ ions and adenylate kinase (AK) in the AK.MgATP (adenosine 5'-triphosphate) complex. However, recent NMR studies concluded that the carboxylate of aspartate 119 accepts a hydrogen bond from a water ligand of the bound Mg2+ ion in the muscle AK.MgATP complex [Fry, D.C., Kuby, S.A., & Mildvan, A.S. (1985) Biochemistry 24, 4680-4694]. On the other hand, in the 2.6-A crystal structure of the yeast AK.MgAP5A [P1,P5-bis(5'-adenosyl)pentaphosphate] complex, the Mg2+ ion is in proximity to aspartate 93 [Egner, U., Tomasselli, A.G., & Schulz, G.E. (1987) J. Mol. Biol. 195, 649-658]. Substitution of Asp-93 with alanine resulted in no change in dissociation constants, 4-fold increases in Km, and a 650-fold decrease in kcat. Notable changes have been observed in the chemical shifts of the aromatic protons of histidine 36 and a few other aromatic residues. Ho... IS - 22 JF - Biochemistry AD - Department of Chemistry, Ohio State University, Columbus 43210. TI - Mechanism of adenylate kinase. Demonstration of a functional relationship between Aspartate 93 and Mg2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR. VL - 30 KW - asp KW - enzyme KW - kinase KW - mechanism KW - nmr AU - Yan, HG AU - Tsai, MD A2 - 1991/06/04 PY - 1991/// ER -