Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-.ANG. resolution-Reference-Cited by-同舟云学术

Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-.ANG. resolution

Published:1990-08 Issue:33 Volume:29 Page:7691-7701
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stevens Raymond C.,Gouaux J. Eric,Lipscomb William N.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00485a019

Reference52 articles.

1. Quaternary structural changes in aspartate carbamoyltransferase of Escherichia coli at pH 8.3 and pH 5.8

2. L-Alanosine: a noncooperative substrate for Escherichia coli aspartate transcarbamylase

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

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

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