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Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.

作者信息

Shrake A, Ginsburg A, Schachman H K

出版信息

J Biol Chem. 1981 May 25;256(10):5005-15.

PMID:7014568
Abstract
摘要

相似文献

1
Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli.大肠杆菌天冬氨酸转氨甲酰酶底物促进构象转变的焓变的量热法估计。
J Biol Chem. 1981 May 25;256(10):5005-15.
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Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.双底物类似物的结合促进了天冬氨酸转氨甲酰酶非调节性催化三聚体的巨大结构变化：对别构调节的影响。
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A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.大肠杆菌天冬氨酸转氨甲酰酶活性位点上的单个氨基酸取代会阻止别构转变。
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Submicromolar phosphinic inhibitors of Escherichia coli aspartate transcarbamoylase.亚微摩尔浓度的大肠埃希菌天冬氨酸转氨甲酰酶的膦酸抑制剂。
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引用本文的文献

1
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.双底物类似物的结合促进了天冬氨酸转氨甲酰酶非调节性催化三聚体的巨大结构变化：对别构调节的影响。
Proc Natl Acad Sci U S A. 2000 May 9;97(10):5077-82. doi: 10.1073/pnas.090087197.
2
Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.效应物结合和亚基缔合对大肠杆菌天冬氨酸转氨甲酰酶氢交换动力学的影响。
Proc Natl Acad Sci U S A. 1981 Nov;78(11):6759-63. doi: 10.1073/pnas.78.11.6759.
3
Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase.
大肠杆菌天冬氨酸转氨甲酰酶组装的热力学
Proc Natl Acad Sci U S A. 1983 Nov;80(22):6824-8. doi: 10.1073/pnas.80.22.6824.