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.
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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
R. Barker
中科院分区:
生物学3区
文献类型:
--
作者:
F. C. Hartman;R. Barker

文献摘要

被引文献

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弗雷德里克·C Hartman f和Robert Barker+摘要:许多果糖二磷酸结构类似物的化合物被发现是醛缩酶的竞争性抑制剂。通过比较这些化合物的K_i(酶-抑制剂解离常数)值,得出结论:果糖二磷酸的结合主要是由于磷酸基团,羟基对结合没有显著贡献,酮形式不优先结合,所有形式的果糖二磷酸都被醛缩酶作用。化合物及其K…值为:D-阿拉伯糖醇1,5-二磷酸(1.5 X 10-6); L-阿拉伯糖醇1,5-二磷酸(4.1 X 10-5);木糖醇1,5-二磷酸(2.8 X 10-6);核糖醇1,5-二磷酸(2.0 X 10 - 5); 1,4-脱水-DL-
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-