天冬氨酸转氨甲酰酶的别构调节。双底物类似物N-（膦酰乙酰基）-L-天冬氨酸引发的沉降系数变化。 - Suppr

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超能文献

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.

作者信息

Howlett G J, Schachman H K

出版信息

Biochemistry. 1977 Nov 15;16(23):5077-83. doi: 10.1021/bi00642a021.

DOI:10.1021/bi00642a021

PMID:334255

Abstract

摘要

相似文献

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.天冬氨酸转氨甲酰酶的别构调节。双底物类似物N-（膦酰乙酰基）-L-天冬氨酸引发的沉降系数变化。

Biochemistry. 1977 Nov 15;16(23):5077-83. doi: 10.1021/bi00642a021.

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.

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Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments.天冬氨酸转氨甲酰酶中配体促进的全局构象变化分析。沉降速度实验中边界扩展表明存在双态转变的证据。

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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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Revisiting the allosteric mechanism of aspartate transcarbamoylase.重新审视天冬氨酸转氨甲酰酶的变构机制。

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Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains.镍（II）取代的天冬氨酸转氨甲酰酶构象变化的传播：活性位点配体对调节链的影响

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Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogues to the native enzyme and catalytic subunit.

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Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?天冬氨酸氨甲酰基转移酶的同促效应。当该酶结合双底物类似物N-膦酰乙酰-L-天冬氨酸的单个分子时会发生什么？

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Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.基于大肠杆菌天冬氨酸转氨甲酰酶与双底物类似物N-磷酰乙酰-L-天冬氨酸在2.1埃分辨率下的复合物结构，对其催化机制和变构调节的深入了解。

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Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits.天冬氨酸转氨甲酰酶的别构调节。活性位点配体对调节亚基巯基反应性的影响。

Biochemistry. 1977 Nov 15;16(23):5084-91. doi: 10.1021/bi00642a022.

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Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.随机环形排列导致天冬氨酸转氨甲酰酶催化链中α螺旋内部及附近的链断裂：对组装、稳定性和功能的影响。

Protein Sci. 2001 Mar;10(3):528-37. doi: 10.1110/ps.39001.

In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.由片段化和环状排列的催化多肽链在体内组装天冬氨酸转氨甲酰酶。

Protein Sci. 2001 Mar;10(3):519-27. doi: 10.1110/ps.38901.

Proc Natl Acad Sci U S A. 2000 May 9;97(10):5077-82. doi: 10.1073/pnas.090087197.

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit.基于未调控催化亚基的晶体结构对天冬氨酸转氨甲酰酶变构机制的评估。

Proc Natl Acad Sci U S A. 1999 May 11;96(10):5388-93. doi: 10.1073/pnas.96.10.5388.

Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases.温度对天然和嵌合天冬氨酸转氨甲酰酶变构反应的影响。

J Mol Biol. 1998 Oct 2;282(4):891-901. doi: 10.1006/jmbi.1998.2054.

Determination of sedimentation coefficients for small peptides.小肽沉降系数的测定

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Substrate-induced conformational change in a trimeric ornithine transcarbamoylase.底物诱导的三聚体鸟氨酸转氨甲酰酶构象变化。

Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9550-5. doi: 10.1073/pnas.94.18.9550.

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