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Phe\u201086 and Tyr\u2010133, which are in close contact with the inhibitor Ap<jats:sub>5<\/jats:sub>A according to previous crystallographic results, have been independently changed to tryptophan and other amino acids. The Phe\u201086\u2192Trp mutant had a 3\u2010 to 6\u2010fold change in the <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> for ATP and a 44\u2010fold increase in the <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> for AMP with a simultaneous loss of AMP substrate inhibition. Thus Phe\u201086 is probably in close contact with bound AMP. The Tyr\u2010133\u2192Trp mutant showed no large effects on enzyme kinetics and suggests that the previous assignment of Ap<jats:sub>5<\/jats:sub>A occupying natural adenosine binding sites is probably incorrect. A temperature\u2010sensitive Leu\u2010107\u2192Gln mutant showed a 6\u2010fold decrease in the <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> for ATP and no effect on AMP binding, suggesting that this amino acid is near the ATP binding site.<\/jats:p><jats:p>Changes in the fluorescence of single tryptophan\u2010containing mutant enzymes provided specific information about AMP and ATP binding. The fluorescence results are consistent with the kinetic studies, and also suggest that AMP substrate inhibition is caused by the formation of an abortive complex that prevents the release of product.<\/jats:p>","DOI":"10.1002\/prot.340090105","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T01:14:01Z","timestamp":1117329241000},"page":"28-36","source":"Crossref","is-referenced-by-count":30,"title":["Assignment of the nucleotide binding sites and the mechanism of substrate inhibition of <i>Escherichia coli<\/i> adenylate kinase"],"prefix":"10.1002","volume":"9","author":[{"given":"Peng","family":"Liang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"suffix":"Jr.","given":"George N.","family":"Phillips","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Glaser","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00338a030"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00380a024"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-9861(78)90338-7"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(77)90281-9"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(87)90188-4"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(88)90567-0"},{"key":"e_1_2_1_8_2","doi-asserted-by":"crossref","first-page":"1705","DOI":"10.1096\/fasebj.3.6.2649401","article-title":"NMR studies of the interactions of substrates with enzymes and their peptide fragments","volume":"3","author":"Mildvan A. 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