来自大肠杆菌的天冬氨酸转氨甲酰酶催化亚基的氨基酸序列。
Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli.
作者信息
Konigsberg W H, Henderson L
出版信息
Proc Natl Acad Sci U S A. 1983 May;80(9):2467-71. doi: 10.1073/pnas.80.9.2467.
Abstract
We propose a primary structure for the catalytic subunit of aspartate transcarbamoylase (aspartate carbamoyltransferase; carbamoylphosphate: L-aspartate carbamoyltransferase, EC 2.1.3.2) from Escherichia coli based on amino acid sequences of fragments obtained by cyanogen bromide cleavage, by tryptic digestion of the succinylated polypeptide, and by chymotryptic and proteinase C digestion of the intact catalytic chain. The protein contains 310 amino acids and has a calculated molecular weight of 33,944. The negatively and positively charged residues are distributed uniformly, and there is no indication of charge clustering in the linear sequence.
摘要
我们基于通过溴化氰裂解、琥珀酰化多肽的胰蛋白酶消化以及完整催化链的胰凝乳蛋白酶和蛋白酶C消化所获得的片段的氨基酸序列，提出了来自大肠杆菌的天冬氨酸转氨甲酰酶（天冬氨酸氨甲酰转移酶；氨甲酰磷酸：L-天冬氨酸氨甲酰转移酶，EC 2.1.3.2）催化亚基的一级结构。该蛋白质含有310个氨基酸，计算分子量为33,944。带负电荷和正电荷的残基均匀分布，在线性序列中没有电荷聚集的迹象。
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The enzymology of control by feedback inhibition.反馈抑制控制的酶学
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Inactivation of the catalytic subunit of aspartate transcarbamylase by nitration with tetranitromethane.用四硝基甲烷硝化使天冬氨酸转氨甲酰酶催化亚基失活。
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Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study.N-（膦酰乙酰基）-L-天冬氨酸的结合诱导了天冬氨酸氨甲酰基转移酶的四级结构显著变化：一项3.5埃分辨率的研究。
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Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli.来自大肠杆菌的天然及CTP配体结合的天冬氨酸氨甲酰基转移酶的晶体结构和分子结构
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