Methionyl-tRNA synthetase of Escherichia coli A zinc metalloprotein |
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| Affiliation: | 1. Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19174 U.S.A.;2. Department of Biological Chemistry, Harvard Medical School, Boston MA 02115 U.S.A.;1. Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA;2. Department of Biological Sciences, Wayne State University, Detroit, MI 48202, USA;1. Department of Cancer Biology, The Scripps Research Institute, Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, USA;2. Department of Cell and Molecular Biology, The Scripps Research Institute, Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, USA;3. School of Biology and Basic Medical Sciences, Soochow University, Suzhou 215123, People''s Republic of China |
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| 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 μM but no binding is observed with the trypsin-modified monomer. |
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