| Literature DB >> 367445 |
L H Posorske, M Cohn, N Yanagisawa, D S Auld.
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.Entities:
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Year: 1979 PMID: 367445 DOI: 10.1016/0005-2795(79)90491-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002