The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherichia coli.

The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherichia coli.
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N-(膦乙酰基)-L-天冬氨酸与大肠杆菌天冬氨酸氨基甲酰基转移酶的结合。

DOI:
10.1016/0006-291x(86)90514-0
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发表时间:
1986
影响因子:
3.1
通讯作者:
Lipscomb,WN
Lipscomb,WN
中科院分区:
生物学4区
文献类型:
--
作者:
Volź,KW;Krause,KL;Lipscomb,WN

文献摘要

被引文献

相似文献

对N-(磷酸乙酰基)- l -天冬氨酸与天冬氨酸氨基甲酰转移酶催化链结合的更精确描述阐明了该酶对其底物氨基甲酰磷酸和l -天冬氨酸的特异性,并提出了His-134的催化作用。
A more precise description of the binding of N-(phosphonacetyl)- L-aspartate to the catalytic chains of aspartate carbamoyltransferase clarifies aspects of the specificity of this enzyme toward its substrates, carbamoylphosphate and L-aspartate, and suggests a catalytic role for His-134.