Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil.

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作者信息

Kerbiriou D, Hervé G

出版信息

J Mol Biol. 1972 Mar 14;64(2):379-92. doi: 10.1016/0022-2836(72)90505-0.

DOI:10.1016/0022-2836(72)90505-0

PMID:4554017

Abstract

摘要

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Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil.

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引用本文的文献

The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.大肠杆菌天冬氨酸转氨甲酰酶催化链的80s环对于催化作用和同促协同效应至关重要。

Protein Sci. 1999 Jun;8(6):1305-13. doi: 10.1110/ps.8.6.1305.

Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.来自深海嗜热古菌深渊热球菌的天冬氨酸转氨甲酰酶：基因组织、结构及在大肠杆菌中的表达

J Bacteriol. 1997 Jul;179(13):4143-57. doi: 10.1128/jb.179.13.4143-4157.1997.

Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R state.天冬氨酸氨甲酰基转移酶的分子动力学模拟与刚体（TLS）分析：非偶联R态的证据

Protein Sci. 1993 Jun;2(6):927-35. doi: 10.1002/pro.5560020606.

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.天冬氨酸转氨甲酰酶中的异向相互作用：由于单个酪氨酸突变为苯丙氨酸，变构ATP激活转变为抑制作用。

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Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue.通过对单个酪氨酸残基进行硝化作用消除天冬氨酸转氨甲酰酶的协同性

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