TYROSINASE AND HEMOCYANIN

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 研究中心，而研究中心不一定是研究者所在的机构。 血蓝蛋白（HC）是许多节肢动物和软体动物的含蓝铜的氧转运蛋白，可通过SDS或酶促裂解激活以发挥酶促酚氧化酶活性;从而模拟酪氨酸酶（Ty）或儿茶酚氧化酶（CO）的活性。 我们的合作者提出，血蓝蛋白亚基的第一个结构域屏蔽了活性位点入口，并在血蓝蛋白激活后倾斜、无序或切割，为底物打开入口。这种机制应该是相同的情况下，酪氨酸酶从节肢动物，具有相同的四级结构的血蓝蛋白。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Hemocyanins (HC), the blue copper-containing oxygen-transporting proteins of many arthropods and molluscs can be activated by SDS or enzymatic cleavage to exert an enzymatic phenoloxidase activity; thereby mimicking the activity of tyrosinases (Ty) or catecholoxidases (CO). Our collaborators proposed that the first domain of a hemocyanin subunit shields the active site entrance and is tilted, disordered or cleaved upon activation in hemocyanin, opening an entrance for the substrates. This mechanism should be the same in the case of tyrosinase from arthropods, which have the same quaternary structure as hemocyanins.