Enrico Di Cera in Enzyme Function + and K + Role of
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Role of Na+ and K+ in enzyme function.
Metal complexation is a key mediator or modifier of enzyme structure and function. In addition to divalent and polyvalent metals, group IA metals Na+ and K+ play important and specific roles that assist function of biological macromolecules. We examine the diversity of monovalent cation (M+)-activated enzymes by first comparing coordination in small molecules followed by a discussion of theoret...
متن کاملRedesigning the monovalent cation specificity of an enzyme.
Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K+, whereas a few of them show preferential activation by Na+. The monovalent cation specificity of these enzymes remains elusive in molecular terms and has not been reengineered by site-directed mutagenesis. Here we demonstrate that thrombin, a N...
متن کاملA . Pelc and Enrico Di Cera
10.1074/jbc.M113.451542 Access the most updated version of this article at doi: . JBC Affinity Sites Find articles, minireviews, Reflections and Classics on similar topics on the Alerts: When a correction for this article is posted • When this article is cited • to choose from all of JBC's e-mail alerts Click here http://www.jbc.org/content/288/16/11601.full.html#ref-list-1 This article cites 5...
متن کاملArticle title: RELATIVE ANTITHROMBOTIC AND ANTIHEMOSTATIC EFFECTS OF PROTEIN C ACTIVATOR VERSUS LOW MOLECULAR WEIGHT HEPARIN IN PRIMATES Short Title: Hemostatic Safety of Protein C Activators
Short Title: Hemostatic Safety of Protein C Activators Authors: András Gruber, Ulla M. Marzec, Leslie Bush, Enrico Di Cera, José A. Fernández, Michelle A. Berny, Erik I. Tucker, Owen J.T. McCarty, John H. Griffin, and Stephen R. Hanson Institutions: From the Department of Biomedical Engineering, Oregon Health & Science University, Portland, OR; the Department of Biochemistry and Molecular Bioph...
متن کاملRigidification of the autolysis loop enhances Na(+) binding to thrombin.
Binding of Na(+) to thrombin ensures high activity toward physiological substrates and optimizes the procoagulant and prothrombotic roles of the enzyme in vivo. Under physiological conditions of pH and temperature, the binding affinity of Na(+) is weak due to large heat capacity and enthalpy changes associated with binding, and the K(d)=80 mM ensures only 64% saturation of the site at the conce...
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تاریخ انتشار 2006