Nucleoside triphosphatase activity associated with the N‐terminal domain of mammalian tryptophanyl‐tRNA synthetase
- 6 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 335 (2) , 198-202
- https://doi.org/10.1016/0014-5793(93)80729-e
Abstract
Bovine tryptophanyl-tRNA synthetase (EC 6.1.1.2) deprived of Zn2+ by chelation with the phosphonate analog of Ap4A hydrolized ATP(GTP) to ADP(GDP) although its ability to form tryptophanyl adenylate was impaired. This hydrolytic activity is stimulated by Mg2+ and Mn2+ ions and inhibited by Zn2+. Monoclonal antibody Aml against the N-terminal domain of the enzyme completely abolished ATP(GTP)ase activity. The core peptide generated after proteolytic splitting of the N-domain lacks this activity. We suggest that the nucleotide binding site(s) different from ATP sites involved in aminoacylation reaction reside(s) at the N-terminal domain(s) of the enzymeKeywords
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