METHIONYL-TRANSFER RNA-SYNTHETASE OF ESCHERICHIA-COLI - ZINC METALLOPROTEIN

被引:57
作者
POSORSKE, LH [1 ]
COHN, M [1 ]
YANAGISAWA, N [1 ]
AULD, DS [1 ]
机构
[1] HARVARD UNIV, SCH MED, DEPT BIOL CHEM, BOSTON, MA 02115 USA
关键词
(Escherichia coli); Metalloprotein; methionyl-tRNA synthetase; Zn[!sup]2+[!/sup;
D O I
10.1016/0005-2795(79)90491-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 μM but no binding is observed with the trypsin-modified monomer. © 1979.
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页码:128 / 133
页数:6
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