Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.
暂无分享,去创建一个
N. J. Baxter | A. Hounslow | J. Waltho | J. Szabó | M. Vas | M. Bowler | M. Cliff | G. Blackburn | A. Varga | James P. Marston
[1] M. Vas,et al. Insight into the mechanism of domain movements and their role in enzyme function: example of 3-phosphoglycerate kinase. , 2010, Current protein & peptide science.
[2] N. J. Baxter,et al. Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF 3 - rather than by phosphoranes , 2010, Proceedings of the National Academy of Sciences.
[3] N. J. Baxter,et al. MgF(3)(-) and alpha-galactose 1-phosphate in the active site of beta-phosphoglucomutase form a transition state analogue of phosphoryl transfer. , 2009, Journal of the American Chemical Society.
[4] J. Szabó,et al. Direct kinetic evidence that lysine 215 is involved in the phospho-transfer step of human 3-phosphoglycerate kinase. , 2009, Biochemistry.
[5] W. Lam,et al. Effect of hypoxia on the expression of phosphoglycerate kinase and antitumor activity of troxacitabine and gemcitabine in non-small cell lung carcinoma , 2009, Molecular Cancer Therapeutics.
[6] Winnie Yang,et al. Phosphoglycerate kinase 1‐overexpressing lung cancer cells reduce cyclooxygenase 2 expression and promote anti‐tumor immunity in vivo , 2008, International journal of cancer.
[7] Beáta Flachner,et al. Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase. , 2008, Biochemistry.
[8] S. Arold,et al. Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinase , 2008, Nucleic acids research.
[9] F. Hollfelder,et al. Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes. , 2008, Journal of the American Chemical Society.
[10] Arieh Warshel,et al. On the interpretation of the observed linear free energy relationship in phosphate hydrolysis: a thorough computational study of phosphate diester hydrolysis in solution. , 2008, Biochemistry.
[11] A. Brunger. Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.
[12] V. Schramm. Enzymatic Transition State Theory and Transition State Analogue Design* , 2007, Journal of Biological Chemistry.
[13] A. Leslie,et al. Ground State Structure of F1-ATPase from Bovine Heart Mitochondria at 1.9 Å Resolution* , 2007, Journal of Biological Chemistry.
[14] D. Flot,et al. Expression, crystallization and X-ray data collection from microcrystals of the extracellular domain of the human inhibitory receptor expressed on myeloid cells IREM-1. , 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.
[15] Wei Yang,et al. UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke , 2006, Cell.
[16] F. Hollfelder,et al. A Trojan horse transition state analogue generated by MgF3− formation in an enzyme active site , 2006, Proceedings of the National Academy of Sciences.
[17] C. Mathé,et al. L-nucleoside enantiomers as antivirals drugs: a mini-review. , 2006, Antiviral research.
[18] A. Warshel,et al. Electrostatic basis for enzyme catalysis. , 2006, Chemical reviews.
[19] W. Cleland,et al. Enzymatic mechanisms of phosphate and sulfate transfer. , 2006, Chemical reviews.
[20] Beáta Flachner,et al. Substrate‐induced double sided H‐bond network as a means of domain closure in 3‐phosphoglycerate kinase , 2006, FEBS letters.
[21] Beáta Flachner,et al. Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase. , 2005, Biochemistry.
[22] S. Shetty,et al. Regulation of urokinase receptor expression by phosphoglycerate kinase is independent of its catalytic activity. , 2005, American journal of physiology. Lung cellular and molecular physiology.
[23] Richard J Morris,et al. Towards complete validated models in the next generation of ARP/wARP. , 2004, Acta crystallographica. Section D, Biological crystallography.
[24] Beáta Flachner,et al. Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. , 2004, Biochemistry.
[25] L. Pearl,et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery , 2004, The EMBO journal.
[26] Elizabeth A. Gullen,et al. Novel Role of 3-Phosphoglycerate Kinase, a Glycolytic Enzyme, in the Activation of L-Nucleoside Analogs, a New Class of Anticancer and Antiviral Agents* , 2003, Journal of Biological Chemistry.
[27] R. Wolfenden,et al. The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[28] J. Stivers,et al. Powering DNA repair through substrate electrostatic interactions. , 2003, Biochemistry.
[29] D. Hilvert,et al. Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor. , 2003, Journal of the American Chemical Society.
[30] Steven Hayward,et al. Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50. , 2002, Journal of molecular graphics & modelling.
[31] S. Smerdon,et al. MgF(3)(-) as a transition state analog of phosphoryl transfer. , 2002, Chemistry & biology.
[32] Aaron R. Dinner,et al. Uracil-DNA glycosylase acts by substrate autocatalysis , 2001, Nature.
[33] J. Tainer,et al. Structure and mechanism of the RuvB Holliday junction branch migration motor. , 2001, Journal of molecular biology.
[34] E. Scherzinger,et al. Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010. , 2001, Journal of molecular biology.
[35] M Ghosh,et al. A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure. , 2001, Journal of molecular biology.
[36] P. Hogg,et al. Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase , 2000, Nature.
[37] R. Raines,et al. Pentavalent Organo-Vanadates as Transition State Analogues for Phosphoryl Transfer Reactions. , 2000, Journal of the American Chemical Society.
[38] I. Schlichting,et al. pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog , 1999, Nature Structural Biology.
[39] T. Harris,et al. High‐Precision Measurement of Hydrogen Bond Lengths in Proteins by Nuclear Magnetic Resonance Methods , 1999, Proteins.
[40] M. Williamson,et al. Synthesis and binding of stable bisubstrate ligands for phosphoglycerate kinase. , 1998, Bioorganic & medicinal chemistry letters.
[41] O. Popanda,et al. Modulation of DNA polymerases α, δ and ε by lactate dehydrogenase and 3-phosphoglycerate kinase , 1998 .
[42] R. Huber,et al. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. , 1997, Structure.
[43] A. Wittinghofer. Signaling mechanistics: Aluminum fluoride for molecule of the year , 1997, Current Biology.
[44] Katrin Rittinger,et al. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue , 1997, Nature.
[45] Mohammad Reza Ahmadian,et al. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras , 1997, Nature Structural Biology.
[46] W. Kabsch,et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. , 1997, Science.
[47] P. Frey,et al. Understanding enzymic catalysis: the importance of short, strong hydrogen bonds. , 1997, Chemistry & biology.
[48] Bradley E. Bernstein,et al. Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation , 1997, Nature.
[49] R. Martin. Ternary complexes of Al3+ and F− with a third ligand , 1996 .
[50] M. J. Parker,et al. The development of tertiary interactions during the folding of a large protein. , 1996, Folding & design.
[51] R. G. Kemp,et al. Phosphofructo-1-kinase: role of charge neutralization in the active site. , 1995, Biochemical and biophysical research communications.
[52] J. Reinstein,et al. Crystallization and preliminary X‐ray analysis of UMP/CMP‐kinase from Dictyostelium discoideum with the specific bisubstrate inhibitor P1‐(adenosine 5′)‐P5‐(uridine 5′)‐pentaphosphate (UP5A) , 1995, FEBS letters.
[53] A. Fersht,et al. Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'. , 1993, Biochemistry.
[54] A. Mathiowetz,et al. Probing the role of arginines and histidines in the catalytic function and activation of yeast 3-phosphoglycerate kinase by site-directed mutagenesis. , 1990, The Journal of biological chemistry.
[55] F. Westheimer. Why nature chose phosphates. , 1987, Science.
[56] E. Jaffe,et al. Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ADP and ATP and reactivity of Cr(III)ATP in the 3-phosphoglycerate kinase reaction. Structure of the metal nucleotide substrates. , 1982, The Journal of biological chemistry.
[57] R. Scopes. The Steady‐State Kinetics of Yeast Phosphoglycerate Kinase , 1978 .
[58] G. Lienhard,et al. P 1 ,P 5 -Di(adenosine-5')pentaphosphate, a potent multisubstrate inhibitor of adenylate kinase. , 1973, The Journal of biological chemistry.
[59] F. Opperdoes. Compartmentation of carbohydrate metabolism in trypanosomes. , 1987, Annual review of microbiology.
[60] Fei Long,et al. ARP/wARP and molecular replacement: the next generation , 2007, Acta crystallographica. Section D, Biological crystallography.