来自嗜热真细菌海栖热袍菌的天冬氨酸转氨甲酰酶：融合的催化和调节多肽形成一种别构酶。
Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme.
作者信息
Chen P, Van Vliet F, Van De Casteele M, Legrain C, Cunin R, Glansdorff N
机构信息
Laboratory for Genetics and Microbiology, Vrije Universiteit Brussel, Brussels, Belgium.
出版信息
J Bacteriol. 1998 Dec;180(23):6389-91. doi: 10.1128/JB.180.23.6389-6391.1998.
Abstract
In the allosteric aspartate transcarbamylase (ATCase) from the hyperthermophilic eubacterium Thermotoga maritima, the catalytic and regulatory functions, which in class B ATCases are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers. The ATCases from T. maritima and Treponema denticola present intriguing similarities, suggesting horizontal gene transfer.
摘要
在嗜热真细菌海栖热袍菌的别构天冬氨酸转氨甲酰酶（ATCase）中，在B类ATCase中由特定多肽执行的催化和调节功能，在组装成三聚体的单一类型多肽上结合在一起。来自海栖热袍菌和齿垢密螺旋体的ATCase呈现出有趣的相似性，表明存在水平基因转移。
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