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Nucleoside triphosphatase activity associated with the N‐terminal domain of mammalian tryptophanyl‐tRNA synthetase
Author(s) -
Kovaleva Galina,
Nikitushkina Tatyana,
Kisselev Lev
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80729-e
Subject(s) - aminoacylation , gtp' , biochemistry , nucleotide , adenylate kinase , enzyme , adenosine triphosphate , nucleoside , chemistry , nucleoside triphosphate , biology , transfer rna , rna , gene
Bovine tryptophanyl‐tRNA synthetase (EC 6.1.1.2) deprived of Zn 2+ by chelation with the phosphonate analog of Ap 4 A hydrolized ATP(GTP) to ADP(GDP) although its ability to form tryptophanyl adenylate was impaired. This hydrolytic activity is stimulated by Mg 2+ and Mn 2+ ions and inhibited by Zn 2+ . 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 enzyme.