A peculiar property of aspartyl-tRNA synthetase from bakers' yeast: chemical modification of the protein by the enzymically synthesized aminoacyl adenylate-Reference-Cited by-同舟云学术

A peculiar property of aspartyl-tRNA synthetase from bakers' yeast: chemical modification of the protein by the enzymically synthesized aminoacyl adenylate

Published:1985-03-12 Issue:6 Volume:24 Page:1321-1332
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kern Daniel,Lorber Bernard,Boulanger Yves,Giege Richard

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00327a009

Reference40 articles.

1. Conformational Activation of Aminoacyl-tRNA Synthetases upon Binding of tRNA. A Facet of a Multi-Step Adaptation Process Leading to the Optimal Biological Activity

2. Yeast Phenylalanyl-tRNA Synthetase. Affinity and Photoaffinity Labelling of the Stereospecific Binding Sites

3. Yeast phenylalanyl-tRNA synthetase: symmetric behavior of the enzyme during activation of phenylalanine as shown by a rapid kinetic investigation

4. Crystals of Bacillus stearothermophilus tryptophanyl-tRNA synthetase containing enzymatically formed acyl transfer product tryptophanyl-ATP, an active site marker for the 3' CCA terminus of tryptophanyl-tRNATrp

5. Crystallographic studies on the aspartyl-tRNA synthetase-tRNAAsp system from yeast

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