Literature DB >> 7049888

Survey on substrate specificity with regard to ATP analogs of aminoacyl-tRNA synthetases from E. coli and from Baker's yeast. Correlation to synthetase families.

W Freist, H Sternbach, F Cramer.   

Abstract

The substrate specificity of twenty aminoacyl-tRNA synthetases from E. coli and thirteen enzymes from baker's yeast with regard to eight ATP analogs is investigated for a comparison of the active-site topography. The enzymes are arranged in a scheme of possible "enzyme families" and compared to earlier schemes.

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Year:  1981        PMID: 7049888     DOI: 10.1515/bchm2.1981.362.2.1247

Source DB:  PubMed          Journal:  Hoppe Seylers Z Physiol Chem        ISSN: 0018-4888


  3 in total

1.  A paradoxical increase of a metabolite upon increased expression of its catabolic enzyme: the case of diadenosine tetraphosphate (Ap4A) and Ap4A phosphorylase I in Saccharomyces cerevisiae.

Authors:  D M Avila; A K Robinson; V Kaushal; L D Barnes
Journal:  J Bacteriol       Date:  1991-12       Impact factor: 3.490

2.  Cloning of the tyrocidine synthetase 1 gene from Bacillus brevis and its expression in Escherichia coli.

Authors:  M A Marahiel; M Krause; H J Skarpeid
Journal:  Mol Gen Genet       Date:  1985

3.  Molecular cloning of an ornithine-activating fragment of the gramicidin S synthetase 2 gene from Bacillus brevis and its expression in Escherichia coli.

Authors:  M Krause; M A Marahiel; H von Döhren; H Kleinkauf
Journal:  J Bacteriol       Date:  1985-06       Impact factor: 3.490

  3 in total

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