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。

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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。

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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。

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