大肠杆菌的甲硫氨酰 - tRNA合成酶。一种锌金属蛋白。

Methionyl-tRNA synthetase of Escherichia coli. A zinc metalloprotein.

作者信息

Posorske L H, Cohn M, Yanagisawa N, Auld D S

出版信息

Biochim Biophys Acta. 1979 Jan 25;576(1):128-33. doi: 10.1016/0005-2795(79)90491-4.

Abstract

The native dimeric form of methionyl-tRNA synthetase of Escherichia coli contains two zinc atoms per dimer, one per subunit. The bound zinc is retained upon trypsin modification which yields a monomer with one zinc atom. The enzymatic activity of both the dimeric forms is reversibly inhibited by 1,10-phenanthroline but not by its non-chelating analogues. In addition, the native enzyme binds two Mn2+ per dimer with a binding constant of approx. 70 micron but no binding is observed with the trypsin-modified monomer.

摘要

大肠杆菌甲硫氨酰 - tRNA合成酶的天然二聚体形式每个二聚体含有两个锌原子，每个亚基一个。在胰蛋白酶修饰后，结合的锌得以保留，产生含有一个锌原子的单体。两种二聚体形式的酶活性都受到1,10 - 菲咯啉的可逆抑制，但不受其非螯合类似物的抑制。此外，天然酶每个二聚体结合两个Mn2 +，结合常数约为70微摩尔，但胰蛋白酶修饰的单体未观察到结合。