The conserved residues glutamate-37, aspartate-100, and arginine-269, are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase-Reference-Cited by-同舟云学术

The conserved residues glutamate-37, aspartate-100, and arginine-269, are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase

Published:1993-09-28 Issue:38 Volume:32 Page:10150-10158
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Baker Darren P.,Kantrowitz Evan R.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00089a034

Reference64 articles.

1. Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli

2. Comparison of the aspartate transcarbamoylases from Serratia marcescens and Escherichia coli

3. The DNA sequence ofargIfromEscherichia coliK12

4. Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

5. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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