大肠杆菌鸟氨酸转氨甲酰酶和天冬氨酸转氨甲酰酶中必需精氨酸残基的比较。 - Suppr | 超能文献

Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases.

作者信息

Fortin A F, Hauber J M, Kantrowitz E R

出版信息

Biochim Biophys Acta. 1981 Nov 13;662(1):8-14. doi: 10.1016/0005-2744(81)90216-3.

DOI:10.1016/0005-2744(81)90216-3

Abstract

摘要

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Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases.大肠杆菌鸟氨酸转氨甲酰酶和天冬氨酸转氨甲酰酶中必需精氨酸残基的比较。

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Protonation of arginine 57 of Escherichia coli ornithine transcarbamoylase regulates substrate binding and turnover.大肠杆菌鸟氨酸转氨甲酰酶的精氨酸57质子化调节底物结合和周转。

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Evidence for an exceptionally reactive arginyl residue at the binding site for carbamyl phosphate in bovine ornithine transcarbamylase.牛鸟氨酸转氨甲酰酶中氨甲酰磷酸结合位点处存在一个异常活泼的精氨酰残基的证据。

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Biochemical and genetic characterization of a carbamyl phosphate synthetase mutant of Escherichia coli K12.大肠杆菌K12氨甲酰磷酸合成酶突变体的生化与遗传学特性

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The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.

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