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

作者信息

Altman R B, Ladner J E, Lipscomb W N

出版信息

Biochem Biophys Res Commun. 1982 Sep 30;108(2):592-5. doi: 10.1016/0006-291x(82)90869-5.

DOI:10.1016/0006-291x(82)90869-5
PMID:6756403
Abstract
摘要

相似文献

1
Quaternary structural changes in aspartate carbamoyltransferase of Escherichia coli at pH 8.3 and pH 5.8.大肠杆菌天冬氨酸氨甲酰基转移酶在pH 8.3和pH 5.8条件下的四级结构变化
Biochem Biophys Res Commun. 1982 Sep 30;108(2):592-5. doi: 10.1016/0006-291x(82)90869-5.
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Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.大肠杆菌天冬氨酸转氨甲酰酶催化链中的Glu-50在R四级结构的稳定性中起关键作用。
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引用本文的文献

1
The pAR5 mutation and the allosteric mechanism of Escherichia coli aspartate carbamoyltransferase.大肠杆菌天冬氨酸氨甲酰基转移酶的pAR5突变与别构机制
EMBO J. 1987 Sep;6(9):2843-7. doi: 10.1002/j.1460-2075.1987.tb02581.x.
2
Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.天冬氨酸氨甲酰基转移酶的Glu-239----Gln突变体在3.1埃分辨率下的晶体结构：一种中间四级结构。
Proc Natl Acad Sci U S A. 1989 Nov;86(21):8212-6. doi: 10.1073/pnas.86.21.8212.