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Ligand-promoted strengthening of interchain bonding domains in catalytic subunits of aspartate transcarbamoylase.

作者信息

Burns D L, Schachman H K

出版信息

J Biol Chem. 1982 Oct 25;257(20):12214-8.

PMID:7118940
Abstract
摘要

相似文献

1
Ligand-promoted strengthening of interchain bonding domains in catalytic subunits of aspartate transcarbamoylase.
J Biol Chem. 1982 Oct 25;257(20):12214-8.
2
Spectral alterations associated with the ligand-promoted gross conformational change in aspartate transcarbamoylase.
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3
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.来自天冬氨酸转氨甲酰酶调节链的一个70个氨基酸的锌结合多肽片段导致催化三聚体的动力学机制发生显著变化。
Protein Sci. 1994 Jun;3(6):967-74. doi: 10.1002/pro.5560030612.
4
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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6
On conformational changes in the regulatory enzyme aspartate transcarbamoylase.关于调节酶天冬氨酸转氨甲酰酶的构象变化
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Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli.大肠杆菌活性突变体与野生型天冬氨酸转氨甲酰酶的比较。
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8
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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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。
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Phosphorus-containing inhibitors of aspartate transcarbamoylase from Escherichia coli.
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引用本文的文献

1
Assembly of the aspartate transcarbamoylase holoenzyme from transcriptionally independent catalytic and regulatory cistrons.天冬氨酸转氨甲酰酶全酶由转录独立的催化和顺反子组装而成。
J Bacteriol. 1984 Mar;157(3):891-8. doi: 10.1128/jb.157.3.891-898.1984.