Methionyl-tRNA synthetase of Escherichia coli. A zinc metalloprotein.
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.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D002614:Chelating Agents / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008345:Manganese; D008667:Metalloproteins; D008718:Methionine-tRNA Ligase / Q000378:metabolism; D011485:Protein Binding; D015032:Zinc / Q000032:analysis
D002614:Chelating Agents; D046911:Macromolecular Substances; D008667:Metalloproteins; D008345:Manganese; D000604:Amino Acyl-tRNA Synthetases; D008718:Methionine-tRNA Ligase; D015032:Zinc