{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T20:02:48Z","timestamp":1760644968742},"reference-count":28,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T00:00:00Z","timestamp":1109808000000},"content-version":"vor","delay-in-days":11810,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[1972,11]]},"abstract":"<jats:p>The specificity of yeast hexokinase for ATP was examined with the aid of a number of synthetic and natural analogs. The main features observed are:<\/jats:p><jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>The presence of a 2\u2010amino group either alone or in combination with a 6\u2010amino or 6\u2010hydroxyl group inhibits catalysis.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The replacement of one or both hydrogen atoms of the 6\u2010amino group with methyl groups does not have a large effect on either binding or catalysis.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The replacement of the nitrogen at position 7 with a carbon atom has virtually no effect.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The movement of the glycosidic bond from the N<jats:sup>9<\/jats:sup> to the N<jats:sup>3<\/jats:sup> position has only a moderate effect on both <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> and <jats:italic>V<\/jats:italic>.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The presence of both of the 2\u2032\u2010 and 3\u2032\u2010<jats:italic>cis<\/jats:italic> hydroxyls in the ribose is important for catalysis.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The replacement of ribose with arabinose or glucose produces a large decrease in catalysis. Inhibitor experiments were carried out with the ATP analog containing glucose instead of ribose. It was found to be competitive for ATP and uncompetitive for glucose under the conditions used. These results are consistent with an ordered reaction mechanism.<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p>","DOI":"10.1111\/j.1432-1033.1972.tb02517.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T15:01:12Z","timestamp":1109862072000},"page":"180-185","source":"Crossref","is-referenced-by-count":22,"title":["The Effect of Structural Modifications of ATP on the Yeast\u2010Hexokinase Reaction"],"prefix":"10.1111","volume":"31","author":[{"given":"David C.","family":"Hohnadel","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cecil","family":"Cooper","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,3,3]]},"reference":[{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)34158-4"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)97083-3"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1970.tb01075.x"},{"key":"e_1_2_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(62)05209-X"},{"key":"e_1_2_3_6_2","first-page":"11","volume-title":"Methods in Enzymatic Analysis","author":"Bergmeyer H. 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