Flavonols from Heterotheca inuloides:: Tyrosinase inhibitory activity and structural criteria
Flavonols from Heterotheca inuloides:: Tyrosinase inhibitory activity and structural criteria
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DOI：
10.1016/s0968-0896(00)00102-4
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发表时间：
2000-07-01
影响因子：
3.5
通讯作者：
Ogura, T
中科院分区：
文献类型：
--
作者：
Kubo, I;Kinst-Hori, I;Ogura, T
黄酮醇、高良姜素、山奈酚和槲皮素的酪氨酸酶抑制活性被发现来自于它们在酶中螯合铜的能力。相反，相应的黄酮、白杨素、芹菜素和木犀草素则不螯合酶中的铜。只要 3-羟基是游离的，螯合机制似乎是黄酮醇所特有的。有趣的是，黄酮醇以不同的方式影响酶的活性。例如，槲皮素充当辅助因子并且不抑制单酚酶活性。另一方面，高良姜素抑制单酚酶活性并且不充当辅因子。山奈酚既不作为辅助因子也不抑制单酚酶活性。然而，这三种黄酮醇通常通过螯合酶中的铜来抑制二酚酶活性。 (C) 2000 Elsevier Science Ltd. 保留所有权利。
Tyrosinase inhibitory activity of flavonols, galangin, kaempferol and quercetin, was found to come from their ability to chelate copper in the enzyme. In contrast, the corresponding flavones, chrysin, apigenin and luteolin, did not chelate copper in the enzyme. The chelation mechanism seems to be specific to flavonols as long as the 3-hydroxyl group is free. Interestingly, flavonols affect the enzyme activity in different ways. For example, quercetin behaves as a cofactor and does not inhibit monophenolase activity. On the other hand, galangin inhibits monophenolase activity and does not act as a cofactor. Kaempferol neither acts as a cofactor nor inhibits monophenolase activity. However, these three flavonols are common to inhibit diphenolase activity by chelating copper in the enzyme. (C) 2000 Elsevier Science Ltd. All rights reserved.