@article{ba3e95445ac8421ea72402d7a080b784,
title = "The role of lysine residues 297 and 306 in nucleoside triphosphate regulation of E. coli CTP synthase: Inactivation by 2′,3′-dialdehyde ATP and mutational analyses",
author = "MacLeod, {Travis J.} and Lunn, {Faylene A.} and Bearne, {Stephen L.}",
note = "Funding Information: This work was supported by an operating grant from the Canadian Institutes of Health Research (SLB) and graduate student fellowships from the Natural Sciences and Engineering Research Council of Canada (TJM), the Walter C. Sumner Foundation (FAL), and the Nova Scotia Health Research Foundation (FAL). We thank Professor Enoch Baldwin (University of California, Davis, CA, USA) for kindly providing us with the structural coordinates for both E. coli CTPS complexed with ADP and CTP (PDB 2AD5) and GTP modeled into the GTP-binding site, and for his discussions regarding interactions between ADP and CTPS. We also thank Mark Charman for conducting some preliminary kinetic experiments.",
year = "2006",
month = feb,
doi = "10.1016/j.bbapap.2005.11.021",
language = "English",
volume = "1764",
pages = "199--210",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",
}