Nucleoside triphosphatase activity associated with the N‐terminal domain of mammalian tryptophanyl‐tRNA synthetase

FEBS Letters

Kovaleva, Galina¹  Kisselev, Lev¹  Nikitushkina, Tatyana¹ 

[1] Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilova, 117984 Moscow B-334, Russian Federation

关键词: Mammalian aminoacyl-tRNA synthetase;    ATP/GTP hydrolysis;    Non-canonical enzymatic activity;    Zn2+ chelation;    Ap4A phosphonate analog;    aaRS;    aminoacyl-tRNA synthetase;    Ap3A;    P1;    P3-bis(5'-adenosyl)triphosphate;    Ap4A;    P1;    P4-bis(5'-adenosyl)tetraphosphate;    ATP(GTP)ase;    adenosine (guanosine) triphosphatase;    GlyRS;    glycyl-tRNA synthetase;    E(Trp ~ AMP);    tryptophanyl adenylate enzyme complex;    E(−Zn);    Zn2+-deprived enzyme;    mAbs;    monoclonal antibodies;    PEI-cellulose;    polyethylene iminocellulose;    PheRS;    phenylalanyl-tRNA synthetase;    TrpRS;    tryptophanyl-tRNA synthetase;   

DOI  :  10.1016/0014-5793(93)80729-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 enzyme.

【 授权许可】

Unknown