An exploration of the active site of aldolase using structural analogs of fructose diphosphate.
An exploration of the active site of aldolase using structural analogs of fructose diphosphate.
复制标题
使用果糖二磷酸的结构类似物探索醛缩酶的活性位点。
DOI:
10.1021/bi00882a014
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发表时间:
1965
期刊:
影响因子:
2.9
通讯作者:
R. Barker
中科院分区:
文献类型:
--
作者:
F. C. Hartman;R. Barker
Frederick C. Hartman f and Robert Barker+ abstract: A number of compounds which are structural analogs of fructose diphosphate were found to be competitive inhibitors of aldolase. It is concluded from comparison of the K,(enzyme-inhibitor dissocia-tion constant) values of these compounds that the binding of fructose diphosphate is primarily due to the phosphate groups, that hydroxyl groups donot contribute significantly to the binding, that the keto form is not bound preferentially, and that all forms of fructose diphosphate are acted upon by aldolase. The compounds and their K¡ values are: D-arabinitol 1, 5-diphosphate (1.5 X 10-6); L-arabinitol 1, 5-diphosphate (4.1 X 10-5); xylitol 1, 5-diphosphate (2.8 X 10-6); ribitol 1, 5-diphosphate (2.0 X 10~ 5); 1, 4-anhydro-DL-