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Bui Kevin Fauman Jacob Kes David Torres Mandiola Leticia Ciomaga Adina Salazar Ricardo Bertozzi Andrea L. Gilles Jérôme Goronzy Dominic P. Guttentag Andrew I. Weiss Paul S. 《Pattern Analysis & Applications》2020,23(2):625-651
Pattern Analysis and Applications - In the fields of nanoscience and nanotechnology, it is important to be able to functionalize surfaces chemically for a wide variety of applications. Scanning... 相似文献
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Finer-Moore Janet S.; Fauman Eric B.; Morse Richard J.; Santi Daniel V.; Stroud Robert M. 《Protein engineering, design & selection : PEDS》1996,9(1):69-75
Invariant arginine 179, one of four arginines that are conservedin all thymidylate synthases (TS) and that bind the phosphatemoiety of the substrate 2'-deoxyuridine-5'-monophosphate (dUMP),can be altered even to a negatively charged glutainic acid withlittle effect on kcat. In the mutant structures, ordered wateror the other phosphate binding arginines compensate for thehydrogen bonds made by Arg179 in the wild-type enzyme and thereis almost no change in the conformation or binding site of dUMP.Correlation of dUMP Kds for TS R179A and TS R179K with the structuresof their binary complexes shows that the positive charge onArg179 contributes significantly to dUMP binding affinity. kcat/Kmfor dUMP measures the rate of dUMP binding to TS during theordered bi-substrate reaction, and in the ternary complex dUMPprovides a binding surface for the cofactor. kcat/Km reflectsthe ability of the enzyme to accept a properly oriented dUMPfor catalysis and is less sensitive than is Kd to the changesin electrostatics at the phosphate binding site. 相似文献
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